BIRA_BACSH
ID BIRA_BACSH Reviewed; 325 AA.
AC E0U174; P42975;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Bifunctional ligase/repressor BirA {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};
GN OrderedLocusNames=BSUW23_11005;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=7730294; DOI=10.1128/jb.177.9.2572-2575.1995;
RA Bower S., Perkins J.P., Yocum R.R., Serror P., Sorokin A.V., Rahaim P.,
RA Howitt C.L., Prasad N., Ehrlich S.D., Pero J.;
RT "Cloning and characterization of the Bacillus subtilis birA gene encoding a
RT repressor of the biotin operon.";
RL J. Bacteriol. 177:2572-2575(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a
CC repressor. {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}.
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DR EMBL; U20445; AAB60184.1; -; Genomic_DNA.
DR EMBL; CP002183; ADM38241.1; -; Genomic_DNA.
DR RefSeq; WP_003225583.1; NC_014479.1.
DR AlphaFoldDB; E0U174; -.
DR SMR; E0U174; -.
DR EnsemblBacteria; ADM38241; ADM38241; BSUW23_11005.
DR GeneID; 64304024; -.
DR KEGG; bss:BSUW23_11005; -.
DR HOGENOM; CLU_051096_0_0_9; -.
DR OMA; AVWKHIE; -.
DR Proteomes; UP000002233; 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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProt.
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; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..325
FT /note="Bifunctional ligase/repressor BirA"
FT /id="PRO_0000403660"
FT DOMAIN 74..262
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT DNA_BIND 23..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 118
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 122..124
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 189
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
SQ SEQUENCE 325 AA; 36123 MW; 8766A1EF8DD9D572 CRC64;
MRSTLRKDLI ELFSQAGSEF ISGQKISDAL GCSRTAVWKH IEELRKEGYE VEAVRRKGYR
LIKKPGKLSE SEIRFGLKTE VMGQHLIYQD VISSTQKTAH ELANNNAPEG TLVVADKQTA
GRGRMSRVWH SQEGNGIWMS LILRPDIPLQ KTPQLTLLAA VAVVQGIEAA AGIQTDIKWP
NDILINGKKT VGILTEMQAE EDRVRSVIIG IGINVNQQSD DFPDELKDIA TSLSQASGEK
IDRAGVIQHI LLCFEKRYRD YMTHGFTPIK LLWESYALGI GTNMRARTLN GTFYGKALGI
DDEGVLLLET QEGIKKIYSA DIELG
