LIPL_LYSSC
ID LIPL_LYSSC Reviewed; 278 AA.
AC B1I022;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=Bsph_0948;
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 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; CP000817; ACA38560.1; -; Genomic_DNA.
DR RefSeq; WP_012292704.1; NC_010382.1.
DR AlphaFoldDB; B1I022; -.
DR SMR; B1I022; -.
DR EnsemblBacteria; ACA38560; ACA38560; Bsph_0948.
DR KEGG; lsp:Bsph_0948; -.
DR HOGENOM; CLU_067270_0_0_9; -.
DR OMA; VQIYLCI; -.
DR Proteomes; UP000002164; 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; Transferase.
FT CHAIN 1..278
FT /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT /id="PRO_0000410842"
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; 31520 MW; 670D34CC17D99536 CRC64;
MKSILQQPIW RYYDQSISAK QRSPLESFAT DDTLCQLVGQ LVSPPTIRTW VHEASVVLGI
QDHRLPYVQQ GMDLLESRGY QPIVRNSGGL AVVLDEGILN ISIVLSEQMD SLSINDGYDV
MVDLVKGLFP EVAEKIEAYE IVGSYCPGSY DLSIEGKKFA GISQRRLRQG VAVQIYLCIE
GSGSQRAALI RDFYEESLQQ EETKFNYPQI VPEVMASLSE LVDLHLTVEG VVIRLQQLLH
RLAGEVHPES FHDEELTLYG FYLKRVFERN AKMLERHE
