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Database: UniProt
Entry: W9AR91_9BACI
LinkDB: W9AR91_9BACI
Original site: W9AR91_9BACI 
ID   W9AR91_9BACI            Unreviewed;       280 AA.
AC   W9AR91;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
DE            EC=2.3.1.204 {ECO:0000256|HAMAP-Rule:MF_02119};
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000256|HAMAP-Rule:MF_02119};
GN   Name=lipL {ECO:0000256|HAMAP-Rule:MF_02119,
GN   ECO:0000313|EMBL:CDO05101.1};
GN   ORFNames=BN988_03684 {ECO:0000313|EMBL:CDO05101.1};
OS   Oceanobacillus picturae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO05101.1, ECO:0000313|Proteomes:UP000028863};
RN   [1] {ECO:0000313|EMBL:CDO05101.1, ECO:0000313|Proteomes:UP000028863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1 {ECO:0000313|EMBL:CDO05101.1,
RC   ECO:0000313|Proteomes:UP000028863};
RA   Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated from
RT   human gut.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDO05101.1, ECO:0000313|Proteomes:UP000028863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S1 {ECO:0000313|EMBL:CDO05101.1,
RC   ECO:0000313|Proteomes:UP000028863};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC       moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC         Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC         Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02119};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC       {ECO:0000256|HAMAP-Rule:MF_02119}.
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:CDO05101.1}.
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DR   EMBL; CCAX010000004; CDO05101.1; -; Genomic_DNA.
DR   RefSeq; WP_036578542.1; NZ_QWLU01000002.1.
DR   AlphaFoldDB; W9AR91; -.
DR   STRING; 171693.BN988_03684; -.
DR   eggNOG; COG0095; Bacteria.
DR   OrthoDB; 2080934at2; -.
DR   Proteomes; UP000028863; Unassembled WGS sequence.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16443; LplA; 1.
DR   HAMAP; MF_02119; LipL; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024897; LipL.
DR   PANTHER; PTHR43679:SF3; OCTANOYL-[GCVH]:PROTEIN N-OCTANOYLTRANSFERASE; 1.
DR   PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028863};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02119, ECO:0000313|EMBL:CDO05101.1}.
FT   DOMAIN          48..232
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   ACT_SITE        152
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
FT   SITE            164
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   280 AA;  31588 MW;  862048E518000516 CRC64;
     MKNWKDIIRH QTFRYIDHSN QPTFHGEPYT AMTSFAIDDA LALSVSDEQS PPAVRLWVHD
     ETIVLGIPDG KLPYIAEGIA YLQQAEKQVV IRNSGGLAVA LDKGVLNISL ILPGVKQLSI
     QDCYEAMVSF VQYMLHDLTD AIEAYEIVQS YCPGDYDLSI NGRKFAGISQ RRVKDGAAIQ
     IYLDVEGNSK ERATLIQQFY KIGKKNEETS FSYPNVDPSV MGSLSELLGI DLTVQDMKQR
     VTQALAVFSE NVVTMDFSDE EISHFEKRLK QMQKRNEKIQ
//
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