ID Q1N281_9GAMM Unreviewed; 330 AA.
AC Q1N281;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
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 ORFNames=RED65_15628 {ECO:0000313|EMBL:EAT12283.1};
OS Bermanella marisrubri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bermanella.
OX NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT12283.1, ECO:0000313|Proteomes:UP000004263};
RN [1] {ECO:0000313|EMBL:EAT12283.1, ECO:0000313|Proteomes:UP000004263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RED65 {ECO:0000313|EMBL:EAT12283.1,
RC ECO:0000313|Proteomes:UP000004263};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-2006) 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: 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:EAT12283.1}.
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DR EMBL; AAQH01000008; EAT12283.1; -; Genomic_DNA.
DR RefSeq; WP_007018334.1; NZ_CP051183.1.
DR AlphaFoldDB; Q1N281; -.
DR STRING; 207949.RED65_15628; -.
DR HOGENOM; CLU_051096_4_0_6; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000004263; 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:UP000004263};
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 65..259
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT DNA_BIND 17..36
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 88..90
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 112
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 116..118
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ SEQUENCE 330 AA; 36182 MW; F5F38AC76EA217E4 CRC64;
MKQALLDILA DGQFHSGEEI GEALGVSRAA VWKQLKKLEA LDIPLHSVKG KGYRLPEPVG
LLSLSKLEQH GLTQDYFDSI DLALSLDSTN SAMMRLAETQ PGGRHLIFAE MQTQGRGRRG
RQWVSPFARN LYFSVLWTFE QGIAAIQGLS LAVGLSIYHT LKRYGLESHG LKWPNDILVA
KDADTFAKLG GILIEITGDV SDQCQVVIGV GLNLDIQTRD LAHIDQLATG LRQQGIEFDR
NELAATLLMD LSDTLNGFSQ HGFSPLQQHW NEADALHGHK VNLILPSSEL TGIARGVNAI
GELQLEIDGQ LQVYNGGEVT LRSQGKHHEA
//
