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Database: UniProt
Entry: A0A3E0U2P6_9GAMM
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ID   A0A3E0U2P6_9GAMM        Unreviewed;       332 AA.
AC   A0A3E0U2P6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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   ECO:0000313|EMBL:REL30994.1};
GN   ORFNames=DXX94_09830 {ECO:0000313|EMBL:REL30994.1};
OS   Thalassotalea euphylliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL30994.1, ECO:0000313|Proteomes:UP000256899};
RN   [1] {ECO:0000313|Proteomes:UP000256899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|Proteomes:UP000256899};
RA   Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT   "Thalassotalea euphylliae genome.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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: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|ARBA:ARBA00000933,
CC         ECO:0000256|HAMAP-Rule:MF_00978};
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {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:REL30994.1}.
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DR   EMBL; QUOT01000001; REL30994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0U2P6; -.
DR   Proteomes; UP000256899; 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: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:UP000256899};
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..263
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         92..94
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         116
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         120..122
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         187
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ   SEQUENCE   332 AA;  36336 MW;  77E4B1D8DCDC9EB3 CRC64;
     MSKSVREKLI QALASGKFVS GQDIADELSV SRAAISKQVT VLQQMGLDIF KVRGKGYQLA
     KPLVLLDKVS ISDALEQLSA TNSVEVHTLI DSTNDYLLRK LPNQVEPGQA CIAEFQSQGR
     GRRGRQWISP FGSHLYLSYY RYLADGMSSA MGLSLLTALA ISDAINALYN VQVQLKWPND
     VYLDGVKLAG ILIDLEGQAS GACHSVIGIG LNLNMPEQAA NDIDQPWTDL QRHLSQSAES
     QIDRNQLAVA IIVALNQRLA QQESQGIETM LADWHQQDLF LNQPVRLITG DKEQQGICRG
     VNAQGALLFE QNGQVKPVHG GEVSLRGNNF ES
//
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