(data stored in ACNUC7421 zone)

SWISSPROT: B7UJ80_ECO27

ID   B7UJ80_ECO27            Unreviewed;       341 AA.
AC   B7UJ80;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523};
DE   AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523,
GN   ECO:0000313|EMBL:CAS07732.1};
GN   OrderedLocusNames=E2348C_0184 {ECO:0000313|EMBL:CAS07732.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07732.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07732.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
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 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:0000256|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] +
CC         UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosamine; Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:71573, ChEBI:CHEBI:78474, ChEBI:CHEBI:78847;
CC         EC=2.3.1.191; Evidence={ECO:0000256|HAMAP-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:0000256|HAMAP-
CC       Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523,
CC       ECO:0000256|SAAS:SAAS00760705}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxD subfamily. {ECO:0000256|HAMAP-Rule:MF_00523,
CC       ECO:0000256|SAAS:SAAS00760707}.
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DR   EMBL; FM180568; CAS07732.1; -; Genomic_DNA.
DR   RefSeq; WP_000095071.1; NC_011601.1.
DR   EnsemblBacteria; CAS07732; CAS07732; E2348C_0184.
DR   KEGG; ecg:E2348C_0184; -.
DR   HOGENOM; HOG000294339; -.
DR   KO; K02536; -.
DR   OMA; GFGYAHT; -.
DR   BioCyc; ECOL574521:E2348C_RS00950-MONOMER; -.
DR   UniPathway; UPA00359; UER00479.
DR   Proteomes; UP000008205; 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-UniRule.
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_sf.
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; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJ80.
DR   SWISS-2DPAGE; B7UJ80.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760710, ECO:0000313|EMBL:CAS07732.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760688};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760725};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760733};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS01103315};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760702, ECO:0000313|EMBL:CAS07732.1}.
FT   DOMAIN       22     88       LpxD. {ECO:0000259|Pfam:PF04613}.
FT   COILED      316    341       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    239    239       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00523}.
SQ   SEQUENCE   341 AA;  35999 MW;  760600E93367C28E CRC64;
     MSSIRLADLA QQLDAELHGD GDIVITGVAS MQSAQTGHIT FMVNPKYREH LGLCQASAVV
     MTLDDLPFAK 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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