ID A0A158DSH8_9BURK Unreviewed; 295 AA.
AC A0A158DSH8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=biotin--[biotin carboxyl-carrier protein] ligase {ECO:0000256|ARBA:ARBA00024227};
DE EC=6.3.4.15 {ECO:0000256|ARBA:ARBA00024227};
GN ORFNames=AWB78_05547 {ECO:0000313|EMBL:SAK97528.1};
OS Caballeronia calidae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAK97528.1, ECO:0000313|Proteomes:UP000071859};
RN [1] {ECO:0000313|EMBL:SAK97528.1, ECO:0000313|Proteomes:UP000071859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29321 {ECO:0000313|EMBL:SAK97528.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000933};
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DR EMBL; FCOX02000036; SAK97528.1; -; Genomic_DNA.
DR RefSeq; WP_062609080.1; NZ_FCOX02000036.1.
DR AlphaFoldDB; A0A158DSH8; -.
DR OrthoDB; 9807064at2; -.
DR Proteomes; UP000071859; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR008988; Transcriptional_repressor_C.
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 SUPFAM; SSF50037; C-terminal domain of transcriptional repressors; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SAK97528.1}.
FT DOMAIN 14..225
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 295 AA; 31454 MW; EBB7350AC285F659 CRC64;
MNPTPFAPDA PWRIDRTRLA ALAERPARDW TIDIVDETGS TNADLMEQMR ASRHDSAPAP
IVRIAYSQTA GRGRRGRAWL AEPGNALLMS VGCVIGRPIE GLSGLSLAIG TAVLDALARL
PLTPSARAAL KWPNDVLLDD GKLAGILIET AWNTPEATAV VIGIGMNLHG AEQLAAQVDD
ASRLAASSVQ GTAPAALARA WPDANLTDTL AALLNALDTA LPRFEAEGFR PFRQRWLDMH
AWAGREVALI DQGMEVTRGI ASGVDDSGQL LIDTPEGPRA VTTGELTLRL TKERP
//