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Database: UniProt
Entry: A0A0B0ICL7_9BACI
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ID   A0A0B0ICL7_9BACI        Unreviewed;       327 AA.
AC   A0A0B0ICL7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Bifunctional ligase/repressor BirA {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   ORFNames=LQ50_09945 {ECO:0000313|EMBL:KHF40308.1};
OS   Halalkalibacter okhensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF40308.1, ECO:0000313|Proteomes:UP000030832};
RN   [1] {ECO:0000313|EMBL:KHF40308.1, ECO:0000313|Proteomes:UP000030832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA   Prakash J.S.;
RT   "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a
CC       repressor. {ECO:0000256|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: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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00978}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHF40308.1}.
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DR   EMBL; JRJU01000010; KHF40308.1; -; Genomic_DNA.
DR   RefSeq; WP_034628455.1; NZ_JRJU01000010.1.
DR   AlphaFoldDB; A0A0B0ICL7; -.
DR   STRING; 333138.LQ50_09945; -.
DR   eggNOG; COG0340; Bacteria.
DR   eggNOG; COG1654; Bacteria.
DR   OrthoDB; 9807064at2; -.
DR   Proteomes; UP000030832; Unassembled WGS sequence.
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:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd16442; BPL; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; 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   NCBIfam; TIGR00121; birA_ligase; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|HAMAP-Rule:MF_00978};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00978};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00978};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030832};
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          67..258
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   DNA_BIND        19..38
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         114
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         185
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ   SEQUENCE   327 AA;  36512 MW;  B7A06B2019727E2F CRC64;
     MKEQLLKIFA EHSGEFVSGE MISQQLGCSR TAIWKHIDEL RKNGYQLESA PRKGYRLVSK
     GDGIHPHEVK VGLSTKRLGQ ELTYFDATDS TQFTAHKLAQ EGATEGHVVI ANEQTAGKGR
     LGRDWYSRKG TSVSISMILR PDLPPQKTPQ LTLLTAVAVV RAIKNIVGIE CDIKWPNDIL
     LKGKKLVGIL TEMQADPDRV HSIIIGIGIN VNQRSDDFDP SIRDLATSLA IEKGKTVERA
     QVISAVLNEF EHLYDLYLNE GFTPIRSLWE VYSISVGTYI YARTMREVIY GYAKGITNDG
     VLLLEDEKGQ EHKIYSADIE IASQVEE
//
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