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Bifunctional ligase/repressor BirA (Biotin operon repressor) (Biotin--[acetyl-CoA-carboxylase] ligase) (EC 6.3.4.15) (Biotin--protein ligase) (Biotin-[acetyl-CoA carboxylase] synthetase)

 BIRA_SALTY              Reviewed;         320 AA.
P37416; Q9L9K4;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
29-AUG-2001, sequence version 2.
27-SEP-2017, entry version 121.
RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000255|HAMAP-Rule:MF_00978};
AltName: Full=Biotin operon repressor {ECO:0000255|HAMAP-Rule:MF_00978};
AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000255|HAMAP-Rule:MF_00978};
EC=6.3.4.15 {ECO:0000255|HAMAP-Rule:MF_00978};
AltName: Full=Biotin--protein ligase {ECO:0000255|HAMAP-Rule:MF_00978};
AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000255|HAMAP-Rule:MF_00978};
Name=birA {ECO:0000255|HAMAP-Rule:MF_00978};
OrderedLocusNames=STM4138; ORFNames=STMF1.2;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
STRAIN=LT2;
PubMed=8048842; DOI=10.1007/BF00307771;
Dombrosky P.M., Schmid M.B., Young K.D.;
"Sequence divergence of the murB and rrfB genes from Escherichia coli
and Salmonella typhimurium.";
Arch. Microbiol. 161:501-507(1994).
-!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase
and a biotin-operon repressor. In the presence of ATP, BirA
activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-
5'-AMP or holoBirA) complex. HoloBirA can either transfer the
biotinyl moiety to the biotin carboxyl carrier protein (BCCP)
subunit of acetyl-CoA carboxylase, or bind to the biotin operator
site and inhibit transcription of the operon. {ECO:0000255|HAMAP-
Rule:MF_00978}.
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide
ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-
dioxide ligase (ADP-forming)]. {ECO:0000255|HAMAP-Rule:MF_00978}.
-!- SIMILARITY: Belongs to the biotin--protein ligase family.
{ECO:0000255|HAMAP-Rule:MF_00978}.
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EMBL; AF170176; AAF33493.1; -; Genomic_DNA.
EMBL; AE006468; AAL22971.1; -; Genomic_DNA.
EMBL; L14816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_463012.1; NC_003197.2.
RefSeq; WP_000655752.1; NC_003197.2.
ProteinModelPortal; P37416; -.
SMR; P37416; -.
STRING; 99287.STM4138; -.
PaxDb; P37416; -.
PRIDE; P37416; -.
EnsemblBacteria; AAL22971; AAL22971; STM4138.
GeneID; 1255664; -.
KEGG; stm:STM4138; -.
PATRIC; fig|99287.12.peg.4354; -.
eggNOG; ENOG4105HJX; Bacteria.
eggNOG; COG0340; LUCA.
eggNOG; COG1654; LUCA.
HOGENOM; HOG000041812; -.
KO; K03524; -.
OMA; RAAVWKH; -.
PhylomeDB; P37416; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd16442; BPL; 1.
Gene3D; 1.10.10.10; -; 1.
HAMAP; MF_00978; Bifunct_BirA; 1.
InterPro; IPR030855; Bifunct_BirA.
InterPro; IPR004408; Biotin_CoA_COase_ligase.
InterPro; IPR004409; Biotin_operon_repress_HTH.
InterPro; IPR003142; BPL_C.
InterPro; IPR004143; BPL_LPL_catalytic.
InterPro; IPR013196; HTH_11.
InterPro; IPR008988; Transcriptional_repressor_C.
InterPro; IPR011991; WHTH_DNA-bd_dom.
PANTHER; PTHR12835:SF10; PTHR12835:SF10; 1.
Pfam; PF02237; BPL_C; 1.
Pfam; PF03099; BPL_LplA_LipB; 1.
Pfam; PF08279; HTH_11; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50037; SSF50037; 1.
TIGRFAMs; TIGR00121; birA_ligase; 1.
TIGRFAMs; TIGR00122; birA_repr_reg; 1.
PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
3: Inferred from homology;
ATP-binding; Biotin; Complete proteome; DNA-binding; Ligase;
Nucleotide-binding; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 320 Bifunctional ligase/repressor BirA.
/FTId=PRO_0000064935.
DOMAIN 66 254 BPL/LPL catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01067}.
DNA_BIND 22 41 H-T-H motif. {ECO:0000255|HAMAP-
Rule:MF_00978}.
REGION 89 91 Biotin binding. {ECO:0000255|HAMAP-
Rule:MF_00978}.
REGION 116 118 Biotin binding. {ECO:0000255|HAMAP-
Rule:MF_00978}.
BINDING 112 112 Biotin. {ECO:0000255|HAMAP-
Rule:MF_00978}.
BINDING 183 183 Biotin. {ECO:0000255|HAMAP-
Rule:MF_00978}.
CONFLICT 100 101 EL -> DV (in Ref. 2). {ECO:0000305}.
SEQUENCE 320 AA; 35395 MW; 010E8483093297F5 CRC64;
MKDTTVPLTL ISLLADGEFH SGEQLGERLG MSRAAINKHI QTLRDWGVDV FTVPGKGYSL
PEPIQLLDAD RIHSQLDSGN VAVLPVIDST NQYLLDRIGE LRSGDACVAE YQQAGRGRRG
RKWFSPFGAN LYLSMYWRLE QGPAAAIGLS LVIGIVMAEV LRKLGADKVR VKWPNDLYLL
DRKLAGILVE LTGKTGDAAQ IVIGAGINMA MRRVEEDVIN QGWITLQEAG ITLDRNMLAA
KLIYKLRAAL ELFEQEGLSP YLSRWKKLDN FIDRPVKLII GDKEIFGISR GIDTQGALLL
EQDGVIKPWM GGEISLRSAE


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