ID Q67PK8_SYMTH Unreviewed; 335 AA.
AC Q67PK8;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=STH1400 {ECO:0000313|EMBL:BAD40385.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD40385.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD40385.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00978}.
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DR EMBL; AP006840; BAD40385.1; -; Genomic_DNA.
DR RefSeq; WP_011195530.1; NC_006177.1.
DR AlphaFoldDB; Q67PK8; -.
DR STRING; 292459.STH1400; -.
DR KEGG; sth:STH1400; -.
DR eggNOG; COG0340; Bacteria.
DR eggNOG; COG1654; Bacteria.
DR HOGENOM; CLU_051096_0_0_9; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000000417; 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:0016740; F:transferase activity; IEA:UniProt.
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:UP000000417};
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 71..262
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT DNA_BIND 23..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 94..96
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 118
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT BINDING 189
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ SEQUENCE 335 AA; 35980 MW; 26E88765F8FB3A60 CRC64;
MTSRTAPELL SLLTAAGGGW VSGAEISRRL GVSRTAIWKH IEALRLLGYE IEAAPRKGYR
LVARPDLLTP EEVRAGLATR RLGRVVEYRE TVGSTNDLAK EMARQGAPEG LLVLAEQQTA
GKGRLGRSWT TPPGAAIAMS LVLRPDLPPH AAPRITLAAA VAVTEAVREA AGVAAGIKWP
NDVQVNGRKL CGILTEMEAE MDRVAFVVLG IGLNVTLRRE QMDPSFRETA TSLALEGAPP
VRRAALVQAI LARFEAVYDE LLGDRFDRVL DRWRALSVTL GQAVRALGLD GQPVLEGVAE
EVDQEGALLV RDGAGQVHRV VSGEVSLRPA HAQDR
//
