ID B3EI43_CHLL2 Unreviewed; 330 AA.
AC B3EI43;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Clim_2431 {ECO:0000313|EMBL:ACD91452.1};
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD91452.1, ECO:0000313|Proteomes:UP000008841};
RN [1] {ECO:0000313|EMBL:ACD91452.1, ECO:0000313|Proteomes:UP000008841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330
RC {ECO:0000313|Proteomes:UP000008841};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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}.
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DR EMBL; CP001097; ACD91452.1; -; Genomic_DNA.
DR RefSeq; WP_012467317.1; NC_010803.1.
DR AlphaFoldDB; B3EI43; -.
DR STRING; 290315.Clim_2431; -.
DR KEGG; cli:Clim_2431; -.
DR eggNOG; COG0340; Bacteria.
DR eggNOG; COG1654; Bacteria.
DR HOGENOM; CLU_051096_0_0_10; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000008841; 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 CDD; cd00090; HTH_ARSR; 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; IPR011991; ArsR-like_HTH.
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 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..259
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 188
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ SEQUENCE 330 AA; 36189 MW; 2B265EF02094FDE2 CRC64;
MNDLTYGILS RLHGASGYLS GEDLCREFGI TRSAVWKHIG QLRDAGCRID AVSGSGYRLL
ALSGVPVAGE VDLFLATRTA GRIFHYQKET ESTNLEAKKL AAEGVPEGAV IVADSQRAGR
GRLGRTWVSP AGKNLYFSLI LRPSVVSLRI PQITLLVAAA IHQAICDLFP CIDTGVKWPN
DILAGGRKLC GVLCEMQSEP GMTHFVVVGI GINVNQDDFP EELRDKATSL KLETGEWFSR
SRLLATVLNR FEELYLNWLQ EDDLGFILPY LERYSLLQGK DVCIDQFSRQ ITGTVCGIAR
GGELVLQTED GTELKISSGE ASLRKAYTHL
//
