ID   LIPL_STAA8              Reviewed;         278 AA.
AC   Q2G0I9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE            EC=2.3.1.204 {ECO:0000255|HAMAP-Rule:MF_02119};
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN   Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119};
GN   OrderedLocusNames=SAOUHSC_00575;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02119}.
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC       {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD29718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000253; ABD29718.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000362357.1; NZ_LS483365.1.
DR   RefSeq; YP_499143.1; NC_007795.1.
DR   AlphaFoldDB; Q2G0I9; -.
DR   SMR; Q2G0I9; -.
DR   STRING; 1280.SAXN108_0645; -.
DR   EnsemblBacteria; ABD29718; ABD29718; SAOUHSC_00575.
DR   GeneID; 3920616; -.
DR   KEGG; sao:SAOUHSC_00575; -.
DR   PATRIC; fig|93061.5.peg.518; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_067270_0_0_9; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..278
FT                   /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT                   /id="PRO_0000410845"
FT   DOMAIN          41..247
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        146
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT   SITE            158
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   278 AA;  31735 MW;  33F38C1749A029A2 CRC64;
     MDLASKYFNG VNWRYIDHSS GLEPMQSFAF DDTFCESVGK DISDNVVRTW IHQHTVILGI
     HDSRLPFLKD GIDYLTNEIG YNAIVRNSGG LGVVLDQGVL NISLMFKGQT ETTIDEAFTV
     MYLLISKMFE NENVDIDTME IEHSYCPGKF DLSIDGKKFA GISQRRVRGG IAVQIYLCVE
     GSGSERALMM QTFYEHALKG EVTKFKYPEI EPSCMASLET LLNKTITVQD VMFLLLYAIK
     DLGGVLNMTP ITQEEWQRYD TYFDKMIERN KKMIDQMQ