LPXG_CHLMU
ID LPXG_CHLMU Reviewed; 329 AA.
AC Q9PJT2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=TC_0746;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
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).
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; AE002160; AAF39553.1; -; Genomic_DNA.
DR PIR; B81669; B81669.
DR RefSeq; WP_010231421.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PJT2; -.
DR STRING; 243161.TC_0746; -.
DR EnsemblBacteria; AAF39553; AAF39553; TC_0746.
DR GeneID; 1246109; -.
DR KEGG; cmu:TC_0746; -.
DR eggNOG; COG1408; Bacteria.
DR HOGENOM; CLU_025443_3_2_0; -.
DR OMA; LGDYPAG; -.
DR OrthoDB; 1690667at2; -.
DR UniPathway; UPA00359; -.
DR Proteomes; UP000000800; 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..329
FT /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxG"
FT /id="PRO_0000019222"
FT TRANSMEM 2..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 37109 MW; 233246E55411992C CRC64;
MFVFVGSTVS LTAIVAAPVL TWIWANHLEP NLLKLTRLDW RLPKKFAHLH GLRIVQISDL
HLNQSTPDAF LKKISRKVSS LSPDMLVFTG DFICRAKVES SNKLKNFLCS LNAPLGCFAC
LGNHDYATYV SRDIHGKINT IPETSSRPLR RALTSVYQSL FSSSHNEFAE EFTPQDPNPH
LLSILHNTPF QLLHNQSVTL SDVVNIVGLG DFFAKQFDPK KAFTNYNPTL PGIILSHNPD
TIHYLKDYPG DVVFSGHSHG PQISLPWPKF ANTITNKLSG LENPELARGL FSFPQEKRLL
YVNRGLGGWK RIRFFSPPEI CIMRCLYEP
