LPXG_CHLPN
ID LPXG_CHLPN Reviewed; 320 AA.
AC Q9Z7X6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-2,3-diacylglucosamine pyrophosphatase LpxG {ECO:0000250|UniProtKB:O84467};
DE Short=UDP-DAGn pyrophosphatase {ECO:0000250|UniProtKB:O84467};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:O84467};
DE AltName: Full=UDP-2,3-diacylglucosamine hydrolase LpxG {ECO:0000250|UniProtKB:O84467};
DE Short=UDP-DAGn hydrolase {ECO:0000250|UniProtKB:O84467};
GN Name=lpxG {ECO:0000250|UniProtKB:O84467};
GN OrderedLocusNames=CPn_0578, CP_0170, CPj0578, CpB0602;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3-
CC diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate (lipid X)
CC and UMP by catalyzing the attack of water at the alpha-P atom. Involved
CC in the biosynthesis of lipid A, a phosphorylated glycolipid that
CC anchors the lipooligosaccharide (LOS) to the outer membrane of the
CC cell. {ECO:0000250|UniProtKB:O84467}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-2,3-diacyl-alpha-D-glucosamine = 2,3-diacyl-alpha-D-
CC glucosaminyl 1-phosphate + 2 H(+) + UMP; Xref=Rhea:RHEA:53328,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:137179, ChEBI:CHEBI:137180;
CC Evidence={ECO:0000250|UniProtKB:O84467};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O84467};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis.
CC {ECO:0000250|UniProtKB:O84467}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:O84467}; Single-pass membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:O84467}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE001363; AAD18717.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF73636.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98785.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98531.1; -; Genomic_DNA.
DR PIR; G72061; G72061.
DR PIR; G86562; G86562.
DR RefSeq; NP_224774.1; NC_000922.1.
DR RefSeq; WP_010883216.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7X6; -.
DR STRING; 115711.CP_0170; -.
DR EnsemblBacteria; AAD18717; AAD18717; CPn_0578.
DR EnsemblBacteria; AAF73636; AAF73636; CP_0170.
DR GeneID; 45050622; -.
DR KEGG; cpa:CP_0170; -.
DR KEGG; cpj:yaeI; -.
DR KEGG; cpn:CPn_0578; -.
DR KEGG; cpt:CpB0602; -.
DR PATRIC; fig|115713.3.peg.644; -.
DR eggNOG; COG1408; Bacteria.
DR HOGENOM; CLU_025443_3_2_0; -.
DR UniPathway; UPA00359; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Manganese; Membrane;
KW Metal-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxG"
FT /id="PRO_0000019223"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 36412 MW; FA67AF640E60F6E1 CRC64;
MLISISLATL PILAFSWASF IEPNWLRTTA IPWRLPKKHA HLHGLRIAQI SDLHFHKRVP
EKFLNKVSKS IKNFSPDLIV FCGDLLCRAR LEDKERLETF LNTLEAPLGV FAILGNHDYS
SYISRNTKGE ITCIPEEKSR PIQRAIIAVM QGLFSSPSYR YDPNLTPQEP HPDLLKLLKN
TPLTLLHNTT HVIPNTLNIV GLGDLFARQF HPEQAFKNYD PSLPGLLLSH NPDGITRLQQ
YPGDFVLSGH SHGPQVTLSW PKFARKFFER LSGLENPYLA RGYFVTKEGK QLYVNRGLGG
LKRIRFCSPP EICYITCSYD
