ID   LIPM_CLOD6              Reviewed;         271 AA.
AC   Q189T1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Octanoyltransferase LipM {ECO:0000255|HAMAP-Rule:MF_02118};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_02118};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02118};
GN   Name=lipM {ECO:0000255|HAMAP-Rule:MF_02118}; OrderedLocusNames=CD630_07330;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an
CC       intermediate carrier during protein lipoylation. {ECO:0000255|HAMAP-
CC       Rule:MF_02118}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02118};
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_02118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02118}.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC       acid is attached via an amide linkage to the epsilon-amino group of a
CC       specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC       The reaction proceeds via an octanoyl-thioester enzyme intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_02118}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC       {ECO:0000255|HAMAP-Rule:MF_02118}.
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DR   EMBL; AM180355; CAJ67567.1; -; Genomic_DNA.
DR   RefSeq; WP_003436933.1; NZ_CP010905.2.
DR   RefSeq; YP_001087210.1; NC_009089.1.
DR   AlphaFoldDB; Q189T1; -.
DR   SMR; Q189T1; -.
DR   STRING; 272563.CD630_07330; -.
DR   DNASU; 4914197; -.
DR   EnsemblBacteria; CAJ67567; CAJ67567; CD630_07330.
DR   KEGG; cdf:CD630_07330; -.
DR   KEGG; pdc:CDIF630_00849; -.
DR   PATRIC; fig|272563.120.peg.754; -.
DR   eggNOG; COG0095; Bacteria.
DR   OMA; YAYLDDW; -.
DR   PhylomeDB; Q189T1; -.
DR   BioCyc; PDIF272563:G12WB-844-MON; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
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_02118; LipM; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024898; LipM.
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..271
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000410855"
FT   DOMAIN          31..242
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        144
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT   SITE            159
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ   SEQUENCE   271 AA;  31220 MW;  BD04598FB00BD527 CRC64;
     MNQWRVIHNK SYEGAMNMAI DEAIFTAYKK GHNKPTLRFY TWEPACLSIG YFQKLEDEID
     LDKCRCMNID YTRRITGGRA VLHDNELTYS IIIGEDNPLI DKSINLSYRY ISEGLVKGLN
     LSGIETDNLN RGERISRENL SAACFNAHAS YEVTINNKKV IGSAQSRKDG VLLQHGSIIL
     DFDVEKLFKL IKTKTPELKE RAMKFTAKKA SGIENEIGRK IDIDILQKNI VKGLAEQFNV
     EFVEGDLTDY EKQLVKELYE KYKNEEYNKK R