PGPC_ECOLI
ID PGPC_ECOLI Reviewed; 211 AA.
AC P0AD42; P30133; Q2MAH0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphatidylglycerophosphatase C;
DE EC=3.1.3.27;
DE AltName: Full=Phosphatidylglycerolphosphate phosphatase C;
DE Short=PGP phosphatase C;
GN Name=pgpC; Synonyms=yfhB; OrderedLocusNames=b2560, JW5408;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NWL37;
RX PubMed=1602968; DOI=10.1111/j.1365-2958.1992.tb01540.x;
RA Poulsen L.K., Larsen N.W., Molin S., Andersson P.;
RT "Analysis of an Escherichia coli mutant strain resistant to the cell-
RT killing function encoded by the gef gene family.";
RL Mol. Microbiol. 6:895-905(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP GENE NAME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=21148555; DOI=10.1074/jbc.m110.199265;
RA Lu Y.H., Guan Z., Zhao J., Raetz C.R.;
RT "Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of
RT Escherichia coli.";
RL J. Biol. Chem. 286:5506-5518(2011).
CC -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
CC {ECO:0000269|PubMed:21148555}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC Evidence={ECO:0000269|PubMed:21148555};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21148555};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:21148555}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21148555}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Simultaneous deletion of
CC pgpC and pgpA increases phosphatidylglycerophosphate (PGP) levels
CC almost hundredfold relative to wild-type. In constrast, simultaneous
CC deletion of pgpC and pgpB leads to a twofold increase of PGP levels.
CC Lethal when combined with deletion of both pgpA and pgpB.
CC {ECO:0000269|PubMed:21148555}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79822.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA10910.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA51063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X72336; CAA51063.1; ALT_INIT; Genomic_DNA.
DR EMBL; D64044; BAA10910.1; ALT_INIT; Genomic_DNA.
DR EMBL; U36841; AAA79822.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75613.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76736.1; -; Genomic_DNA.
DR PIR; S20973; S20973.
DR RefSeq; NP_417055.4; NC_000913.3.
DR RefSeq; WP_000190655.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0AD42; -.
DR SMR; P0AD42; -.
DR BioGRID; 4261368; 7.
DR STRING; 511145.b2560; -.
DR jPOST; P0AD42; -.
DR PaxDb; P0AD42; -.
DR PRIDE; P0AD42; -.
DR DNASU; 947026; -.
DR EnsemblBacteria; AAC75613; AAC75613; b2560.
DR EnsemblBacteria; BAE76736; BAE76736; BAE76736.
DR GeneID; 66673552; -.
DR GeneID; 947026; -.
DR KEGG; ecj:JW5408; -.
DR KEGG; eco:b2560; -.
DR PATRIC; fig|511145.12.peg.2662; -.
DR EchoBASE; EB1345; -.
DR eggNOG; COG0560; Bacteria.
DR HOGENOM; CLU_112917_0_0_6; -.
DR OMA; GTFMRYL; -.
DR PhylomeDB; P0AD42; -.
DR BioCyc; EcoCyc:EG11371-MON; -.
DR BioCyc; MetaCyc:EG11371-MON; -.
DR UniPathway; UPA00084; UER00504.
DR PRO; PR:P0AD42; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IMP:EcoCyc.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006435; HAD-SF_hydro_IF_YfhB.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01545; YfhB_g-proteo; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Magnesium; Membrane; Metal-binding;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Phosphatidylglycerophosphatase C"
FT /id="PRO_0000169247"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..211
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 211 AA; 24439 MW; 908E95FE54A3AA2D CRC64;
MATHERRVVF FDLDGTLHQQ DMFGSFLRYL LRRQPLNALL VLPLLPIIAI ALLIKGRAAR
WPMSLLLWGC TFGHSEARLQ TLQADFVRWF RDNVTAFPLV QERLTTYLLS SDADIWLITG
SPQPLVEAVY FDTPWLPRVN LIASQIQRGY GGWVLTMRCL GHEKVAQLER KIGTPLRLYS
GYSDSNQDNP LLYFCQHRWR VTPRGELQQL E
