(data stored in SCRATCH zone)

SWISSPROT: C5BHH1_EDWI9

ID   C5BHH1_EDWI9            Unreviewed;       309 AA.
AC   C5BHH1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Lipid A biosynthesis lauroyltransferase {ECO:0000256|HAMAP-Rule:MF_01942};
DE            EC=2.3.1.241 {ECO:0000256|HAMAP-Rule:MF_01942};
DE   AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase {ECO:0000256|HAMAP-Rule:MF_01942};
GN   Name=lpxL {ECO:0000256|HAMAP-Rule:MF_01942};
GN   OrderedLocusNames=NT01EI_0537 {ECO:0000313|EMBL:ACR67770.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67770.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67770.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67770.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
CC   -!- FUNCTION: Catalyzes the transfer of laurate from lauroyl-acyl
CC       carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-
CC       (lauroyl)-lipid IV(A). {ECO:0000256|HAMAP-Rule:MF_01942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + dodecanoyl-
CC         [ACP] = dodecanoyl-(Kdo)2-lipid IVA + holo-[ACP];
CC         Xref=Rhea:RHEA:28442, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:60365, ChEBI:CHEBI:61524, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:65264; EC=2.3.1.241; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01942};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01942}.
CC   -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis;
CC       KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
CC       IV(A): step 3/4. {ECO:0000256|HAMAP-Rule:MF_01942}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01942}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01942}.
CC   -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family.
CC       {ECO:0000256|HAMAP-Rule:MF_01942}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001600; ACR67770.1; -; Genomic_DNA.
DR   RefSeq; WP_015869970.1; NC_012779.2.
DR   EnsemblBacteria; ACR67770; ACR67770; NT01EI_0537.
DR   GeneID; 7961562; -.
DR   KEGG; eic:NT01EI_0537; -.
DR   PATRIC; fig|634503.3.peg.487; -.
DR   eggNOG; ENOG4105D1S; Bacteria.
DR   eggNOG; COG1560; LUCA.
DR   HOGENOM; HOG000265960; -.
DR   KO; K02517; -.
DR   OMA; ILCLPYP; -.
DR   OrthoDB; 1106624at2; -.
DR   BioCyc; EICT634503:G1GVC-500-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00360; UER00485.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008913; F:lauroyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07984; LPLAT_LABLAT-like; 1.
DR   HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1.
DR   InterPro; IPR004960; LipA_acyltrans.
DR   InterPro; IPR011920; Lipid_A_LpxL_LpxP.
DR   PANTHER; PTHR30606; PTHR30606; 1.
DR   Pfam; PF03279; Lip_A_acyltrans; 1.
DR   PIRSF; PIRSF026649; MsbB; 1.
DR   TIGRFAMs; TIGR02207; lipid_A_htrB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHH1.
DR   SWISS-2DPAGE; C5BHH1.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01942,
KW   ECO:0000313|EMBL:ACR67770.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01942};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01942};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01942,
KW   ECO:0000313|EMBL:ACR67770.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01942};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01942}.
FT   TRANSMEM     20     40       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01942}.
FT   MOTIF       135    140       HXXXXD motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01942}.
SQ   SEQUENCE   309 AA;  36082 MW;  1836F43401E663B0 CRC64;
     MSDNHVYPQF QRSMLHPRYW LTWLGIGIFY LMMLLPYPWL YRLGKMLGKT AMRFMKTRVE
     VTRRNLALCF PQMPEAQREA WVIQNFESVG MALVETGMAW FWPDWRIRRW CRLEGEENMR
     QAKQTGKGIL LIGLHFLTLE LGARIFGMHN PGVGVYRPND NPVLDWLQTW GRLRSNKYML
     DRRDVKGMIR ALKEGEIVWY APDHDYGPRS SVFVPLFAVA QAATTTGTYI LARMGKPTIL
     PFMPLRNADG SGYTLHIQPM LQDVPLDDQT ATAAYMNRVV EREIMLAPTQ YMWLHRRFKT
     CPPGIASRY
//

If you have problems or comments...

PBIL Back to PBIL home page