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Database: UniProt
Entry: Q03YT9_LEUMM
LinkDB: Q03YT9_LEUMM
Original site: Q03YT9_LEUMM 
ID   Q03YT9_LEUMM            Unreviewed;       325 AA.
AC   Q03YT9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=LEUM_0518 {ECO:0000313|EMBL:ABJ61633.1};
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61633.1, ECO:0000313|Proteomes:UP000000362};
RN   [1] {ECO:0000313|EMBL:ABJ61633.1, ECO:0000313|Proteomes:UP000000362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC   523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC   {ECO:0000313|Proteomes:UP000000362};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ61633.1; -; Genomic_DNA.
DR   RefSeq; WP_011679350.1; NC_008531.1.
DR   AlphaFoldDB; Q03YT9; -.
DR   EnsemblBacteria; ABJ61633; ABJ61633; LEUM_0518.
DR   KEGG; lme:LEUM_0518; -.
DR   eggNOG; COG0340; Bacteria.
DR   eggNOG; COG1654; Bacteria.
DR   HOGENOM; CLU_051096_0_1_9; -.
DR   Proteomes; UP000000362; 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; 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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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          5..58
FT                   /note="Helix-turn-helix type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08279"
FT   DOMAIN          83..212
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03099"
FT   DOMAIN          272..315
FT                   /note="Biotin protein ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02237"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         88..90
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         113
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
FT   BINDING         185
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00978"
SQ   SEQUENCE   325 AA;  35840 MW;  6EA99C71834A4D25 CRC64;
     MKTTDQLLKY FLKHEGEYLS GETLANRLGV SRAAIWKAVQ KLNEDGHQID SQHRKGYRYK
     ETGVLSVPAI KALIATNWDI QVFDQLDSSN SYAKEALAAG KIVHPTVIIA DQQNAAYGRF
     RRSFVAPEKT GLYLSIALPV MNDRVLEPGL LTTATAVIVR HVIASSLGYQ LSFKWVNDLI
     FNDKKVGGIL TEGVLDIESQ SLTSLVVGIG LNLIQPINLP DQLDKKVGGI VSDLVFSRNM
     MIAKLVDEFA DMINQYQTGK YLPEYRAHNI VLGHEVVVQY AGQKIHGKAV EISNQGALIL
     VTFAGEKITI SSGEITKLNV NGKEY
//
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