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BAEB_BACVZ
ID   BAEB_BACVZ              Reviewed;         225 AA.
AC   A7Z4X7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable polyketide biosynthesis zinc-dependent hydrolase BaeB;
DE            EC=3.-.-.-;
GN   Name=baeB; OrderedLocusNames=RBAM_016900;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
RN   [2]
RP   PATHWAY, AND FUNCTION IN BACILLAENE BIOSYNTHESIS.
RX   PubMed=16707694; DOI=10.1128/jb.00052-06;
RA   Chen X.-H., Vater J., Piel J., Franke P., Scholz R., Schneider K.,
RA   Koumoutsi A., Hitzeroth G., Grammel N., Strittmatter A.W., Gottschalk G.,
RA   Suessmuth R.D., Borriss R.;
RT   "Structural and functional characterization of three polyketide synthase
RT   gene clusters in Bacillus amyloliquefaciens FZB 42.";
RL   J. Bacteriol. 188:4024-4036(2006).
CC   -!- FUNCTION: Probably involved in some intermediate steps for the
CC       synthesis of the antibiotic polyketide bacillaene which is involved in
CC       secondary metabolism. {ECO:0000269|PubMed:16707694}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000269|PubMed:16707694}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000560; ABS74053.1; -; Genomic_DNA.
DR   RefSeq; WP_012117588.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4X7; -.
DR   SMR; A7Z4X7; -.
DR   STRING; 326423.RBAM_016900; -.
DR   EnsemblBacteria; ABS74053; ABS74053; RBAM_016900.
DR   KEGG; bay:RBAM_016900; -.
DR   HOGENOM; CLU_030571_5_3_9; -.
DR   OMA; SHYDHVN; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..225
FT                   /note="Probable polyketide biosynthesis zinc-dependent
FT                   hydrolase BaeB"
FT                   /id="PRO_0000388005"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  25875 MW;  8BE4834197B31975 CRC64;
     MDHTYEVHQI KTYHQMWSNY CYIIADRSKK SAIAVDPSWE IDKITDKLHE LDVDLSAILL
     THSHYDHVNL AEPLQQIYHS DIYMSSAEID FYQFRCRNLI ALEDGQTFAA GGFIIRSILT
     PGHTAGGMCY LLSDHLFTGD TVFTEGCGIC GDRGSSAEDM FHSIQRIKAS IPPHVRVYPG
     HSFGEKPGQK MESLLKNNIY FQIEKKEHFV NFRNRKNQKG LFHFK
 
 
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