ID   LIPM_BACCR              Reviewed;         278 AA.
AC   Q818P0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BC_4209;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP11124.1; -; Genomic_DNA.
DR   RefSeq; NP_833923.1; NC_004722.1.
DR   RefSeq; WP_000514081.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q818P0; -.
DR   SMR; Q818P0; -.
DR   STRING; 226900.BC_4209; -.
DR   EnsemblBacteria; AAP11124; AAP11124; BC_4209.
DR   GeneID; 67508847; -.
DR   KEGG; bce:BC4209; -.
DR   PATRIC; fig|226900.8.peg.4348; -.
DR   HOGENOM; CLU_022986_5_0_9; -.
DR   OMA; YAYLDDW; -.
DR   Proteomes; UP000001417; 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..278
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000410850"
FT   DOMAIN          33..248
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT   SITE            165
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ   SEQUENCE   278 AA;  32105 MW;  20EA1C56003E2A05 CRC64;
     MGKEKWCYIN SGQCSPAFNM ALDECLLNWQ SEKKMPPTIR FYEWEVPTLT VGYFQRVEKD
     INMDVVNEKK YGFVRRQTGG RGVLHDKELT YSVIVSEDHP NMPKTVTEAY RVISQGLLDG
     FKALGLEAYY AVPKTEADRE NLKNPRSGVC FDAPSWYEIV VEGRKIAGSA QTRQKGVILQ
     HGSIPLEIDL DELYDLFLFP NERVKERMKS MFSSKAVAIN ELTDRTFTIE QLIKAFEVGF
     EKGLDVELVP YELTEEQLHE VQTLAKEKYE SNEWNYKK