ID   LPXH_ECO7I              Reviewed;         240 AA.
AC   B7NL16;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   02-NOV-2016, entry version 54.
DE   RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000255|HAMAP-Rule:MF_00575};
DE            EC=3.6.1.54 {ECO:0000255|HAMAP-Rule:MF_00575};
DE   AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000255|HAMAP-Rule:MF_00575};
GN   Name=lpxH {ECO:0000255|HAMAP-Rule:MF_00575};
GN   OrderedLocusNames=ECIAI39_0487;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the pyrophosphate bond of
CC       UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-
CC       phosphate (lipid X) and UMP. {ECO:0000255|HAMAP-Rule:MF_00575}.
CC   -!- CATALYTIC ACTIVITY: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-
CC       alpha-D-glucosamine + H(2)O = 2-N,3-O-bis((3R)-3-
CC       hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + UMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00575}.
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 4/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00575}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00575}.
CC   -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00575}.
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DR   EMBL; CU928164; CAR16625.1; -; Genomic_DNA.
DR   RefSeq; WP_000212239.1; NC_011750.1.
DR   RefSeq; YP_002406518.1; NC_011750.1.
DR   ProteinModelPortal; B7NL16; -.
DR   EnsemblBacteria; CAR16625; CAR16625; ECIAI39_0487.
DR   GeneID; 7152527; -.
DR   KEGG; ect:ECIAI39_0487; -.
DR   PATRIC; 18329524; VBIEscCol51957_0516.
DR   HOGENOM; HOG000261930; -.
DR   KO; K03269; -.
DR   OMA; FMHGNRD; -.
DR   UniPathway; UPA00359; UER00480.
DR   Proteomes; UP000000749; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.60.21.10; -; 2.
DR   HAMAP; MF_00575; LpxH; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR01854; lipid_A_lpxH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism.
FT   CHAIN         1    240       UDP-2,3-diacylglucosamine hydrolase.
FT                                /FTId=PRO_1000129519.
SQ   SEQUENCE   240 AA;  27007 MW;  7DA5C2F3F917FBFD CRC64;
     MATLFIADLH LCAEEPAITA GFLRFLAREA RKADALYILG DLFEAWIGDD DPNPLHRQMA
     AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE KVLELYGRRV LIMHGDTLCT
     DDIGYQAFRA KVHKPWLQTL FLALPLFVRK RIAARMRANS KEANSSKSLA IMDVNQNAVV
     SAMEKHQVQW LIHGHTHRPA VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
//