(data stored in ACNUC7421 zone)

SWISSPROT: LIPB_ECO27

ID   LIPB_ECO27              Reviewed;         213 AA.
AC   B7UKS0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN   Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013};
GN   OrderedLocusNames=E2348C_0530;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic
CC       acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of
CC       lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate
CC       although octanoyl-ACP is likely to be the physiological substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] +
CC         N(6)-octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665,
CC         Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:78809;
CC         EC=2.3.1.181; Evidence={ECO:0000255|HAMAP-Rule:MF_00013};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of
CC       octanoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00013}.
DR   EMBL; FM180568; CAS08078.1; -; Genomic_DNA.
DR   RefSeq; WP_000284027.1; NC_011601.1.
DR   SMR; B7UKS0; -.
DR   EnsemblBacteria; CAS08078; CAS08078; E2348C_0530.
DR   KEGG; ecg:E2348C_0530; -.
DR   KO; K03801; -.
DR   OMA; GEVTYHC; -.
DR   BioCyc; ECOL574521:E2348C_RS02790-MONOMER; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102555; F:octanoyl transferase activity (acting on glycine-cleavage complex H protein); IEA:UniProtKB-EC.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   CDD; cd16444; LipB; 1.
DR   HAMAP; MF_00013; LipB; 1.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKS0.
DR   SWISS-2DPAGE; B7UKS0.
KW   Acyltransferase; Complete proteome; Cytoplasm; Transferase.
FT   CHAIN         1    213       Octanoyltransferase.
FT                                /FTId=PRO_1000116545.
FT   DOMAIN       32    207       BPL/LPL catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01067}.
FT   REGION       71     78       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00013}.
FT   REGION      138    140       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00013}.
FT   REGION      151    153       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00013}.
FT   ACT_SITE    169    169       Acyl-thioester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00013}.
FT   SITE        135    135       Lowers pKa of active site Cys.
FT                                {ECO:0000255|HAMAP-Rule:MF_00013}.
SQ   SEQUENCE   213 AA;  23883 MW;  56EE2BB105F99EAD CRC64;
     MYQDKILVRQ LGLQPYEPIS QAMHEFTDTR DDSTLDEIWL VEHYPVFTQG QAGKAEHILM
     PGDIPVIQSD RGGQVTYHGP GQQVMYVLLN LKRRKLGVRE LVTLLEQTVV NTLAELGIEA
     HPRADAPGVY VGEKKICSLG LRIRRGCSFH GLALNVNMDL SPFLRINPCG YAGMEMAKIS
     QWKPEATTNN IAPRLLENIL ALLNNPDFEY ITA
//

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