BIRA_SALTY
ID BIRA_SALTY Reviewed; 320 AA.
AC P37416; Q9L9K4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin operon repressor {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE EC=6.3.4.15 {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--protein ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000255|HAMAP-Rule:MF_00978};
GN Name=birA {ECO:0000255|HAMAP-Rule:MF_00978}; OrderedLocusNames=STM4138;
GN ORFNames=STMF1.2;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=LT2;
RX PubMed=8048842; DOI=10.1007/bf00307771;
RA Dombrosky P.M., Schmid M.B., Young K.D.;
RT "Sequence divergence of the murB and rrfB genes from Escherichia coli and
RT Salmonella typhimurium.";
RL Arch. Microbiol. 161:501-507(1994).
CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a
CC biotin-operon repressor. In the presence of ATP, BirA activates biotin
CC to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA)
CC complex. HoloBirA can either transfer the biotinyl moiety to the biotin
CC carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or
CC bind to the biotin operator site and inhibit transcription of the
CC operon. {ECO:0000255|HAMAP-Rule:MF_00978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC 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:0000255|HAMAP-Rule:MF_00978};
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000255|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; AF170176; AAF33493.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22971.1; -; Genomic_DNA.
DR EMBL; L14816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_463012.1; NC_003197.2.
DR RefSeq; WP_000655752.1; NC_003197.2.
DR AlphaFoldDB; P37416; -.
DR SMR; P37416; -.
DR STRING; 99287.STM4138; -.
DR PaxDb; P37416; -.
DR EnsemblBacteria; AAL22971; AAL22971; STM4138.
DR GeneID; 1255664; -.
DR KEGG; stm:STM4138; -.
DR PATRIC; fig|99287.12.peg.4354; -.
DR HOGENOM; CLU_051096_4_0_6; -.
DR OMA; AVWKHIE; -.
DR PhylomeDB; P37416; -.
DR BioCyc; SENT99287:STM4138-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; 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 Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00978; Bifunct_BirA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR030855; Bifunct_BirA.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR004409; Biotin_operon_repress_HTH.
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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR TIGRFAMs; TIGR00122; birA_repr_reg; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin; DNA-binding; Ligase; Nucleotide-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..320
FT /note="Bifunctional ligase/repressor BirA"
FT /id="PRO_0000064935"
FT DOMAIN 66..254
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT DNA_BIND 22..41
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 89..91
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 112
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 116..118
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 183
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT CONFLICT 100..101
FT /note="EL -> DV (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ 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
