ID A0A0F7M2Z6_9GAMM Unreviewed; 324 AA.
AC A0A0F7M2Z6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=IMCC21906_00894 {ECO:0000313|EMBL:AKH68579.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68579.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH68579.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68579.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011477; AKH68579.1; -; Genomic_DNA.
DR RefSeq; WP_047011150.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7M2Z6; -.
DR STRING; 1620392.IMCC21906_00894; -.
DR KEGG; spoi:IMCC21906_00894; -.
DR PATRIC; fig|1620392.3.peg.944; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000035013; 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: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:UP000035013};
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 82..257
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 91..93
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 115
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 119..121
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 186
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ SEQUENCE 324 AA; 34575 MW; 2A543CBE372F5589 CRC64;
MTQETLIQLL ADGEFHSGEE AGSLLGVSRT AIWKQFKKLE LLGLPLEVQK GRGYRIAGGL
DLLDKQKILS LIPESISCAS AGFDIFDSIG STNAVAAEKA QQGGSHGYFC LAEQQTAGRG
RRGREWQSPY GRNVYLSMVW EFQSGAAALE GLSLSVGVAV ARALSDIGVS SARLKWPNDV
LCDNKKLAGI LLEMQGDPAG LCQVVVGVGV NVDMGKAQTT GISQPWIDAA SIVGCVDRNT
FTATLVSHLW NVLTEFSRRG FAELRDEWSS LDAYKDCEVM VQLGDKWVSG VASGVDSGGG
LVLNVDGVRQ VFKGGEVSVR SQTS
//
