ID W0I340_9GAMM Unreviewed; 319 AA.
AC W0I340;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:AHF78900.1};
GN ORFNames=Sant_3937 {ECO:0000313|EMBL:AHF78900.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF78900.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF78900.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF78900.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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; CP006569; AHF78900.1; -; Genomic_DNA.
DR RefSeq; WP_025424021.1; NZ_CP006569.1.
DR AlphaFoldDB; W0I340; -.
DR KEGG; sod:Sant_3937; -.
DR PATRIC; fig|1239307.3.peg.4350; -.
DR HOGENOM; CLU_051096_4_0_6; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000019028; 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; 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 NCBIfam; TIGR00121; birA_ligase; 1.
DR NCBIfam; TIGR00122; birA_repr_reg; 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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW 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:UP000019028};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00978};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00978};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00978}.
FT DOMAIN 66..254
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT DNA_BIND 22..41
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 89..91
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"
FT BINDING 183
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ SEQUENCE 319 AA; 34674 MW; 5542043793A37488 CRC64;
MKDVTIPLKL ISLLADGEFH SGEQFGAALG MSRAAINKHV QTVRDWGVDV FTVPGKGYRL
HAPLQLLDEA AIRSRLPSGR LAVLPVIDST NQYLIERIGT LAPGDACVAE YQAQGRGRRG
RQWISPFGNN LYLSLYWRLE QGPAAAGGLS LMVGIVMAEV LQRLGAEGVR VKWPNDLYLN
DRKLAGILVE INGKAGDAAH VVIGAGINLA MREPAAGMID QGWINLQEAG IVIDRNALVA
ELTATLRQAL RQFEGEGFAP FVARWQALDN FFDRPVKLLI GDREIRGIAR GIDAQGALLL
EQDGERHAYL GGEISLRGL
//
