ID   A0A0Q5PT85_9SPHN        Unreviewed;       252 AA.
AC   A0A0Q5PT85;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=ASG07_05660 {ECO:0000313|EMBL:KQR84291.1};
OS   Sphingomonas sp. Leaf343.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR84291.1, ECO:0000313|Proteomes:UP000051323};
RN   [1] {ECO:0000313|EMBL:KQR84291.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR84291.1,
RC   ECO:0000313|Proteomes:UP000051323};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR84291.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR84291.1,
RC   ECO:0000313|Proteomes:UP000051323};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQR84291.1}.
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DR   EMBL; LMPG01000010; KQR84291.1; -; Genomic_DNA.
DR   RefSeq; WP_055843997.1; NZ_LMPG01000010.1.
DR   AlphaFoldDB; A0A0Q5PT85; -.
DR   STRING; 1736345.ASG07_05660; -.
DR   Proteomes; UP000051323; 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   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; 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:KQR84291.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051323}.
FT   DOMAIN          1..187
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   252 AA;  26506 MW;  5DE0F87B4961F58D CRC64;
     MTQHRTVAET GSTNADLVLL AKAGAAEGFW LRAERQTAGR GRQGRAWVSP PGNVYASTLV
     RLRGSDPQAA TLALVAAVAL EEAVAVFLGA SPSPVRRSAP PALSRREGEL VLKWPNDLLL
     DGAKLSGILL DRVDDAVIVG IGVNLAHHPD LPDRATTSLA AHGVGVDPAA FLDVLAEAFA
     RWVGLWRGEG IAAVRARWLE RAHPVGTALT ARLADGIVID GLFDGLDPDG ALTLRLASGE
     RRVIHAADVF LL
//