ID PGPA_HAEIN Reviewed; 163 AA. AC P44157; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Phosphatidylglycerophosphatase A; DE EC=3.1.3.27; DE AltName: Full=Phosphatidylglycerolphosphate phosphatase A; DE Short=PGP phosphatase A; GN Name=pgpA; OrderedLocusNames=HI_1306; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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}; Multi-pass CC membrane protein {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22953.1; -; Genomic_DNA. DR PIR; D64025; D64025. DR RefSeq; NP_439457.1; NC_000907.1. DR AlphaFoldDB; P44157; -. DR STRING; 71421.HI_1306; -. DR EnsemblBacteria; AAC22953; AAC22953; HI_1306. DR KEGG; hin:HI_1306; -. DR PATRIC; fig|71421.8.peg.1358; -. DR eggNOG; COG1267; Bacteria. DR HOGENOM; CLU_103734_0_1_6; -. DR OrthoDB; 9804091at2; -. DR PhylomeDB; P44157; -. DR BioCyc; HINF71421:G1GJ1-1331-MONOMER; -. DR UniPathway; UPA00084; UER00504. DR Proteomes; UP000000579; Chromosome. 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 CDD; cd06971; PgpA; 1. DR InterPro; IPR026037; PgpA. DR InterPro; IPR036681; PgpA-like_sf. DR InterPro; IPR007686; YutG/PgpA. DR PANTHER; PTHR36305; PHOSPHATIDYLGLYCEROPHOSPHATASE A; 1. DR PANTHER; PTHR36305:SF1; PHOSPHATIDYLGLYCEROPHOSPHATASE A; 1. DR Pfam; PF04608; PgpA; 1. DR PIRSF; PIRSF006162; PgpA; 1. DR SUPFAM; SSF101307; YutG-like; 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..163 FT /note="Phosphatidylglycerophosphatase A" FT /id="PRO_0000058360" FT TRANSMEM 10..28 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 35..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 92..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 137..157 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 163 AA; 18035 MW; 77CC4D4FC550937B CRC64; MTENNPLKKI SLLNPIHLLA VGFGSGLIHP APGTWGSLAG TILGVILLSL LGVKIFLIFT ALCFLLGCYL CQKTTADMGV HDHGSIVWDE FVGVFIVLAA IPSLSWQWIL AAFALFRFFD ILKPFPIRYF DEKLENGFGI MIDDVLAAIY AVIVVFAIQY WML //