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Database: UniProt
Entry: A0A3P5XKK1_9BACL
LinkDB: A0A3P5XKK1_9BACL
Original site: A0A3P5XKK1_9BACL 
ID   A0A3P5XKK1_9BACL        Unreviewed;       327 AA.
AC   A0A3P5XKK1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ECO:0000313|EMBL:VDC29161.1};
GN   ORFNames=FILTAD_02001 {ECO:0000313|EMBL:VDC29161.1};
OS   Filibacter tadaridae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Filibacter.
OX   NCBI_TaxID=2483811 {ECO:0000313|EMBL:VDC29161.1, ECO:0000313|Proteomes:UP000270468};
RN   [1] {ECO:0000313|EMBL:VDC29161.1, ECO:0000313|Proteomes:UP000270468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATB-66 {ECO:0000313|EMBL:VDC29161.1};
RA   Criscuolo A.;
RL   Submitted (NOV-2018) 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}.
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; UXAV01000042; VDC29161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P5XKK1; -.
DR   OrthoDB; 9807064at2; -.
DR   Proteomes; UP000270468; Unassembled WGS sequence.
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:UP000270468};
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         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   327 AA;  35928 MW;  6DE7F827255E6842 CRC64;
     MNSTVKNELL KRLFEAKGEP VSGQEIADHF GLSRTAIWKY VKDLEKDGFE IGTIRKKGYY
     LIASPDRVNE ANVQKHLTTK RYGRRIHYFD TCGSTQVIGH DEAQNGAPDG TVILSEEQTS
     GKGRMSRPWS SVGGKGIWMS IVLRPSLTPQ QAPQMTLVAA VSVTRAIQEV TGIEPDIKWP
     NDILVGGKKV TGILTELQAD PDRVKAIIIG IGINVNQVET DFPEELNPIA TSLRQVLGKP
     VDRAELIAKI LSFLELFTGL YEKHGFGPIK LLWESYSNTT GKQVRAVMLN ETIVGTAMGI
     SDEGVLELKL ADGSIRGIYS ADIELPK
//
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