位置:首页 > 蛋白库 > PGPA_HAEIN
PGPA_HAEIN
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   03-AUG-2022, entry version 118.
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; Proteobacteria; 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   RefSeq; WP_005694464.1; 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   OMA; VWDEIAG; -.
DR   PhylomeDB; P44157; -.
DR   BioCyc; HINF71421:G1GJ1-1331-MON; -.
DR   UniPathway; UPA00084; UER00504.
DR   Proteomes; UP000000579; 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   CDD; cd06971; PgpA; 1.
DR   InterPro; IPR026037; PgpA.
DR   InterPro; IPR036681; PgpA-like_sf.
DR   InterPro; IPR007686; YutG/PgpA.
DR   PANTHER; PTHR36305; PTHR36305; 1.
DR   Pfam; PF04608; PgpA; 1.
DR   PIRSF; PIRSF006162; PgpA; 1.
DR   SUPFAM; SSF101307; SSF101307; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024