LIPL_STAEQ
ID LIPL_STAEQ Reviewed; 279 AA.
AC Q5HRF6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=SERP0237;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53632.1; -; Genomic_DNA.
DR RefSeq; WP_002445773.1; NC_002976.3.
DR AlphaFoldDB; Q5HRF6; -.
DR SMR; Q5HRF6; -.
DR STRING; 176279.SERP0237; -.
DR EnsemblBacteria; AAW53632; AAW53632; SERP0237.
DR KEGG; ser:SERP0237; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_067270_0_0_9; -.
DR OMA; VQIYLCI; -.
DR OrthoDB; 871298at2; -.
DR Proteomes; UP000000531; 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..279
FT /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT /id="PRO_0000410846"
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 279 AA; 31976 MW; D24CF7E7DAB9B217 CRC64;
MDLATKYFNQ INWRYVDHSS GLEPMQSFAF DDTFSESVGK DLSCNVVRTW IHQHTVILGI
HDSRLPFLSD GIRFLTDEQG YNAIVRNSGG LGVVLDQGIL NISLIFKGQT ETTIDEAFTV
MYLLISKMFE DEDVSIDTKE IEQSYCPGKF DLSINDKKFA GISQRRVRGG IAVQIYLCIE
GSGSERALMM QQFYQRALKG QTTKFHYPDI DPSCMASLET LLNREIKVQD VMFLLLYALK
DLGANLNMDP ITEDEWTRYE GYYDKMLERN AKINEKLDF
