ID   PGPC_SHIFL              Reviewed;         211 AA.
AC   P0AD43; P30133;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SF2607, S2779;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC       phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN44104.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP17928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN44104.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP17928.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_708397.4; NC_004337.2.
DR   RefSeq; WP_000190655.1; NZ_WPGW01000021.1.
DR   AlphaFoldDB; P0AD43; -.
DR   SMR; P0AD43; -.
DR   STRING; 198214.SF2607; -.
DR   EnsemblBacteria; AAN44104; AAN44104; SF2607.
DR   EnsemblBacteria; AAP17928; AAP17928; S2779.
DR   GeneID; 1025660; -.
DR   GeneID; 66673552; -.
DR   KEGG; sfl:SF2607; -.
DR   KEGG; sfx:S2779; -.
DR   PATRIC; fig|198214.7.peg.3112; -.
DR   HOGENOM; CLU_112917_0_0_6; -.
DR   OrthoDB; 1472357at2; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
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_0000169248"
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