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ID B4ST95_STRM5 Unreviewed; 322 AA.
AC B4ST95;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 08-MAY-2019, entry version 59.
DE RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000256|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin operon repressor {ECO:0000256|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE EC=6.3.4.15 {ECO:0000256|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--protein ligase {ECO:0000256|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000256|HAMAP-Rule:MF_00978};
GN Name=birA {ECO:0000256|HAMAP-Rule:MF_00978};
GN OrderedLocusNames=Smal_0233 {ECO:0000313|EMBL:ACF49938.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas;
OC Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49938.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF49938.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF49938.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase
CC and a biotin-operon repressor. In the presence of ATP, BirA
CC activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-
CC 5'-AMP or holoBirA) complex. HoloBirA can either transfer the
CC biotinyl moiety to the biotin carboxyl carrier protein (BCCP)
CC subunit of acetyl-CoA carboxylase, or bind to the biotin operator
CC site and inhibit transcription of the operon. {ECO:0000256|HAMAP-
CC Rule:MF_00978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate +
CC H(+) + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.15; Evidence={ECO:0000256|HAMAP-Rule:MF_00978};
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|HAMAP-Rule:MF_00978}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00978}.
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DR EMBL; CP001111; ACF49938.1; -; Genomic_DNA.
DR RefSeq; WP_012509776.1; NC_011071.1.
DR STRING; 391008.Smal_0233; -.
DR EnsemblBacteria; ACF49938; ACF49938; Smal_0233.
DR KEGG; smt:Smal_0233; -.
DR eggNOG; ENOG4105HJX; Bacteria.
DR eggNOG; COG0340; LUCA.
DR HOGENOM; HOG000041812; -.
DR KO; K03524; -.
DR OMA; RAAVWKH; -.
DR OrthoDB; 1842956at2; -.
DR BioCyc; SMAL391008:SMAL_RS01175-MONOMER; -.
DR Proteomes; UP000001867; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009305; P:protein biotinylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00978; Bifunct_BirA; 1.
DR InterPro; IPR030855; Bifunct_BirA.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR013196; HTH_11.
DR InterPro; IPR008988; Transcriptional_repressor_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF08279; HTH_11; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
DR PRODOM; B4ST95.
DR SWISS-2DPAGE; B4ST95.
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW Biotin {ECO:0000256|HAMAP-Rule:MF_00978};
KW Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00978, ECO:0000313|EMBL:ACF49938.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_00978};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00978};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00978}.
FT DOMAIN 69 257 BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT PS51733}.
FT DNA_BIND 17 36 H-T-H motif. {ECO:0000256|HAMAP-Rule:
FT MF_00978}.
FT REGION 90 92 Biotin binding. {ECO:0000256|HAMAP-Rule:
FT MF_00978}.
FT REGION 117 119 Biotin binding. {ECO:0000256|HAMAP-Rule:
FT MF_00978}.
FT BINDING 113 113 Biotin. {ECO:0000256|HAMAP-Rule:
FT MF_00978}.
SQ SEQUENCE 322 AA; 34312 MW; F23A4972BBD8BF77 CRC64;
MDDRQLLAKL AAGRLSGDAL ARELGQTRAA IWKRIQGLRA AGVDVEGRAG EGYGLTRPVD
LLDPDAIRAG LPAGVLPLLH DLQVAWTVDS TNAELLRCSA PQRGVSVLLA ERQTGGRGRR
GRAWASPLAA HIYLSVLRLY SGGLGRLAGL SLVAGIAVAE ALHDLGYTQA QLKWPNDLIV
DGRRKLVGLL AEGGGEYAGP ARAVIGIGIN THMPPSFAEQ ITQPWVDLDT LAGKPVDRNV
VVAAVLTRLL PALEEFDREG LAPFLPRYAA FDMLAGREVR VELDGQWQHG TALGLADDGA
LRVRIDGQER LLHAGEVSVR AA
//
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