BIRA_BACSU
ID BIRA_BACSU Reviewed; 325 AA.
AC P0CI75; P42975;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE EC=6.3.4.15 {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin--protein ligase {ECO:0000255|HAMAP-Rule:MF_00978};
DE AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000255|HAMAP-Rule:MF_00978};
GN Name=birA {ECO:0000255|HAMAP-Rule:MF_00978}; OrderedLocusNames=BSU22440;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-23; TRP-38 AND
RP GLY-58.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7730294; DOI=10.1128/jb.177.9.2572-2575.1995;
RA Bower S., Perkins J.P., Yocum R.R., Serror P., Sorokin A.V., Rahaim P.,
RA Howitt C.L., Prasad N., Ehrlich S.D., Pero J.;
RT "Cloning and characterization of the Bacillus subtilis birA gene encoding a
RT repressor of the biotin operon.";
RL J. Bacteriol. 177:2572-2575(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a
CC repressor. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00978};
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00978}.
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DR EMBL; L38424; AAA92879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L47709; AAB38447.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14160.1; -; Genomic_DNA.
DR PIR; A69595; A69595.
DR RefSeq; NP_390125.1; NC_000964.3.
DR RefSeq; WP_003230650.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P0CI75; -.
DR SMR; P0CI75; -.
DR STRING; 224308.BSU22440; -.
DR jPOST; P0CI75; -.
DR PaxDb; P0CI75; -.
DR PRIDE; P0CI75; -.
DR EnsemblBacteria; CAB14160; CAB14160; BSU_22440.
DR GeneID; 939028; -.
DR KEGG; bsu:BSU22440; -.
DR PATRIC; fig|224308.179.peg.2448; -.
DR eggNOG; COG0340; Bacteria.
DR eggNOG; COG1654; Bacteria.
DR InParanoid; P0CI75; -.
DR OMA; AVWKHIE; -.
DR PhylomeDB; P0CI75; -.
DR BioCyc; BSUB:BSU22440-MON; -.
DR BRENDA; 6.3.4.15; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF08279; HTH_11; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50037; SSF50037; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR TIGRFAMs; TIGR00122; birA_repr_reg; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; DNA-binding; Ligase; Nucleotide-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..325
FT /note="Bifunctional ligase/repressor BirA"
FT /id="PRO_0000064931"
FT DOMAIN 74..262
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT DNA_BIND 23..42
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 118
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 122..124
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT BINDING 189
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00978"
FT MUTAGEN 23
FT /note="G->S: Deregulation of biotin synthesis."
FT /evidence="ECO:0000269|PubMed:7730294"
FT MUTAGEN 38
FT /note="W->R: Deregulation of biotin synthesis."
FT /evidence="ECO:0000269|PubMed:7730294"
FT MUTAGEN 58
FT /note="G->E: Deregulation of biotin synthesis."
FT /evidence="ECO:0000269|PubMed:7730294"
SQ SEQUENCE 325 AA; 36182 MW; 69088BB2CAD09221 CRC64;
MRSTLRKDLI ELFSQAGNEF ISGQKISDAL GCSRTAVWKH IEELRKEGYE VEAVRRKGYR
LIKKPGKLSE SEIRFGLKTE VMGQHLIYHD VLSSTQKTAH ELANNNAPEG TLVVADKQTA
GRGRMSRVWH SQEGNGVWMS LILRPDIPLQ KTPQLTLLAA VAVVQGIEEA AGIQTDIKWP
NDILINGKKT VGILTEMQAE EDRVRSVIIG IGINVNQQPN DFPDELKDIA TSLSQAAGEK
IDRAGVIQHI LLCFEKRYRD YMTHGFTPIK LLWESYALGI GTNMRARTLN GTFYGKALGI
DDEGVLLLET NEGIKKIYSA DIELG
