(data stored in ACNUC7421 zone)

SWISSPROT: LPXD_ECO57

ID   LPXD_ECO57              Reviewed;         341 AA.
AC   P65323; P58610;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   05-JUL-2017, entry version 81.
DE   RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE   AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523};
GN   OrderedLocusNames=Z0191, ECs0181;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC       (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP
CC       as the acyl donor. Is involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to
CC       the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY: (3R)-3-hydroxytetradecanoyl-[acyl-carrier-
CC       protein] + UDP-3-O-((3R)-hydroxytetradecanoyl)-alpha-D-glucosamine
CC       = UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine
CC       + a holo-[acyl-carrier-protein]. {ECO:0000255|HAMAP-
CC       Rule:MF_00523}.
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxD subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
DR   EMBL; AE005174; AAG54481.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33604.1; -; Genomic_DNA.
DR   PIR; E85502; E85502.
DR   PIR; E90651; E90651.
DR   RefSeq; NP_308208.1; NC_002695.1.
DR   RefSeq; WP_001139282.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P65323; -.
DR   SMR; P65323; -.
DR   STRING; 155864.Z0191; -.
DR   EnsemblBacteria; AAG54481; AAG54481; Z0191.
DR   EnsemblBacteria; BAB33604; BAB33604; BAB33604.
DR   GeneID; 913891; -.
DR   KEGG; ece:Z0191; -.
DR   KEGG; ecs:ECs0181; -.
DR   PATRIC; fig|386585.9.peg.284; -.
DR   eggNOG; ENOG4105D7M; Bacteria.
DR   eggNOG; COG1044; LUCA.
DR   HOGENOM; HOG000294339; -.
DR   KO; K02536; -.
DR   UniPathway; UPA00359; UER00479.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043764; F:UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03352; LbH_LpxD; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   PANTHER; PTHR43378; PTHR43378; 1.
DR   Pfam; PF00132; Hexapep; 3.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 4.
PE   3: Inferred from homology;
DR   PRODOM; P65323.
DR   SWISS-2DPAGE; P65323.
KW   Acyltransferase; Complete proteome; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Repeat; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    341       UDP-3-O-(3-hydroxymyristoyl)glucosamine
FT                                N-acyltransferase.
FT                                /FTId=PRO_0000059671.
FT   ACT_SITE    239    239       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00523}.
SQ   SEQUENCE   341 AA;  36024 MW;  10ADFECAB17478FB CRC64;
     MPSIRLADLA QQLDAELHGD GDIVITGVAS MQSAQTGHIT FMVNPKYREH LGLCQASAVV
     MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI APSAVIDATA KLGNNVSIGA
     NAVIESGVEL GDNVIIGAGC FVGKNSKIGA GSRLWANVTI YHEIQIGQNC LIQSGTVVGA
     DGFGYANDRG NWVKIPQIGR VIIGDRVEIG ACTTIDRGAL DDTVIGNGVI IDNQCQIAHN
     VVIGDNTAVA GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
     YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KSLERKVNQQ D
//

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