LPXG_CHLTR
ID LPXG_CHLTR Reviewed; 329 AA.
AC O84467;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=UDP-2,3-diacylglucosamine pyrophosphatase LpxG {ECO:0000303|PubMed:27006461};
DE Short=UDP-DAGn pyrophosphatase {ECO:0000303|PubMed:27006461};
DE EC=3.6.1.- {ECO:0000269|PubMed:27006461};
DE AltName: Full=UDP-2,3-diacylglucosamine hydrolase LpxG {ECO:0000303|PubMed:27006461};
DE Short=UDP-DAGn hydrolase {ECO:0000303|PubMed:27006461};
GN Name=lpxG {ECO:0000303|PubMed:27006461}; OrderedLocusNames=CT_461;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-59.
RX PubMed=27006461; DOI=10.1128/mbio.00090-16;
RA Young H.E., Zhao J., Barker J.R., Guan Z., Valdivia R.H., Zhou P.;
RT "Discovery of the elusive UDP-diacylglucosamine hydrolase in the Lipid A
RT biosynthetic pathway in Chlamydia trachomatis.";
RL MBio 7:E00090-E00090(2016).
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. Can functionally complement lpxH deficiency in E.coli.
CC Overexpression of LpxG results in toxic accumulation of lipid X and
CC profoundly reduces the infectivity of C.trachomatis. Can utilize UDP-2-
CC N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine as substrate
CC in vitro, but the substrate is likely UDP-2-N-((3R)-3-
CC hydroxyicosanoyl),3-O-(tetradecanoyl)-alpha-D-glucosamine in vivo.
CC {ECO:0000269|PubMed:27006461}.
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:0000269|PubMed:27006461};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:27006461};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis.
CC {ECO:0000269|PubMed:27006461}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:27006461}; Single-pass membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000305|PubMed:27006461}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. LpxG
CC family. {ECO:0000305}.
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DR EMBL; AE001273; AAC68061.1; -; Genomic_DNA.
DR PIR; A71511; A71511.
DR RefSeq; NP_219974.1; NC_000117.1.
DR RefSeq; WP_009871819.1; NC_000117.1.
DR AlphaFoldDB; O84467; -.
DR STRING; 813.O172_02520; -.
DR EnsemblBacteria; AAC68061; AAC68061; CT_461.
DR GeneID; 884234; -.
DR KEGG; ctr:CT_461; -.
DR PATRIC; fig|272561.5.peg.499; -.
DR HOGENOM; CLU_025443_3_2_0; -.
DR InParanoid; O84467; -.
DR OMA; LGDYPAG; -.
DR BioCyc; MetaCyc:MON-20143; -.
DR UniPathway; UPA00359; -.
DR Proteomes; UP000000431; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008758; F:UDP-2,3-diacylglucosamine hydrolase activity; IDA:UniProtKB.
DR GO; GO:0009245; P:lipid A biosynthetic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Manganese; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..329
FT /note="UDP-2,3-diacylglucosamine pyrophosphatase LpxG"
FT /id="PRO_0000019224"
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"
FT MUTAGEN 59
FT /note="D->A: Loss of catalytic activity. Overexpression of
FT this mutant does not result in a significant reduction of
FT bacterial infectivity."
FT /evidence="ECO:0000269|PubMed:27006461"
SQ SEQUENCE 329 AA; 36955 MW; 6CADB6B536694779 CRC64;
MFVSVGITAS LTTILAAPVL TWVWANHLEP NLLRVTRLNW NLPKKFAHLH GLRIVQISDL
HLNHSTPDAF LKKVSRKISS LSPDILVFTG DFVCRAKVET PERLKHFLCS LHAPLGCFAC
LGNHDYATYV SRDIHGKINT ISAMNSRPLK RAFTSVYQSL FASSRNEFAD TLNPQIPNPH
LVSILRNTPF QLLHNQSATL SDTINIVGLG DFFAKQFDPK KAFTDYNPTL PGIILSHNPD
TIHHLQDYPG DVVFSGHSHG PQISLPWPKF ANTITNKLSG LENPELARGL FSFPEESRLL
YVNRGLGGWK RIRFCSPPEI CLMRCLYEP
