(data stored in SCRATCH zone)

SWISSPROT: B4ST95_STRM5

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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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
//

If you have problems or comments...

PBIL Back to PBIL home page