ID   LIPL_MACCJ              Reviewed;         274 AA.
AC   B9E8M1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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}; OrderedLocusNames=MCCL_1832;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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}.
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DR   EMBL; AP009484; BAH18539.1; -; Genomic_DNA.
DR   RefSeq; WP_015912331.1; NC_011999.1.
DR   AlphaFoldDB; B9E8M1; -.
DR   SMR; B9E8M1; -.
DR   STRING; 458233.MCCL_1832; -.
DR   EnsemblBacteria; BAH18539; BAH18539; MCCL_1832.
DR   KEGG; mcl:MCCL_1832; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_067270_0_0_9; -.
DR   OMA; VQIYLCI; -.
DR   OrthoDB; 871298at2; -.
DR   Proteomes; UP000001383; 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..274
FT                   /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT                   /id="PRO_0000410843"
FT   DOMAIN          37..242
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        141
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT   SITE            153
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   274 AA;  30942 MW;  7B713940C9807640 CRC64;
     MTGSIFEGKW QYVDHTTGLQ PMQSFSFDDM YCHLVGQGND AVVRTWVHNH VVILGIHDAR
     LPYLAEGIEY LNNKGYGAIV RNSGGLGVVL DAGVLNISLI FKGDISFSID AGYEYMYELV
     QEMFASYGKR IEAKEITRSY CPGSYDLSID GKKFAGISQR RVKGGIAVQI YLCIEGSGSE
     RAELMRQFYD IALRGEVTKF HYPDIDSSCM ASLEELLETE LSVEEVLFKL LFAMKTLGAT
     LSNNEMTNDM WTLYNIYFER MIERNSKLKI NQEG