LIPM_LYSSC
ID LIPM_LYSSC Reviewed; 276 AA.
AC B1HS22;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 67.
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=Bsph_3557;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACA41045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000817; ACA41045.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B1HS22; -.
DR SMR; B1HS22; -.
DR EnsemblBacteria; ACA41045; ACA41045; Bsph_3557.
DR KEGG; lsp:Bsph_3557; -.
DR HOGENOM; CLU_022986_5_0_9; -.
DR Proteomes; UP000002164; 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; Transferase.
FT CHAIN 1..276
FT /note="Octanoyltransferase LipM"
FT /id="PRO_0000410859"
FT DOMAIN 31..246
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 148
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT SITE 163
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ SEQUENCE 276 AA; 31373 MW; 3F77DE2855646EC2 CRC64;
MTTWYFLNSG KCSPSFNMAL DEALLDWHSE GLIPPVIRFY EWEPATLSIG YFQQAKKDIN
LDAVREQGLG FVRRPTGGRA VLHEHELTYS VIVTESYPDM PESVTEAYRV LSEGILQGFH
NLGMDAYFSV PDTEEKRADL KSPKSAVCFD APSWYELVVE GKKIAGSAQT RQKGVILQHG
AILLDLDQEK LLSVFNFSSE EAKDRMRRKL PEKAVAINSL VDEPVTVEQC VTAFRDGFAK
SLQIELKPFT LSEEQLEYVR ALEEKKYACD EWNFKK