位置:首页 > 蛋白库 > PA1_PROVU
PA1_PROVU
ID   PA1_PROVU               Reviewed;         289 AA.
AC   P37447;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phospholipase A1;
DE            EC=3.1.1.32;
DE            EC=3.1.1.4;
DE   AltName: Full=Detergent-resistant phospholipase A;
DE            Short=DR-phospholipase A;
DE   AltName: Full=Outer membrane phospholipase A;
DE            Short=OM PLA;
DE   AltName: Full=Phosphatidylcholine 1-acylhydrolase;
DE   Flags: Precursor;
GN   Name=pldA;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8300539; DOI=10.1128/jb.176.3.861-870.1994;
RA   Brok R.G.P.M., Brinkman E., van Boxtel R., Bekkers A.C.A.P., Verheij H.M.,
RA   Tommassen J.;
RT   "Molecular characterization of enterobacterial pldA genes encoding outer
RT   membrane phospholipase A.";
RL   J. Bacteriol. 176:861-870(1994).
CC   -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC
CC       3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is
CC       bound by different amino acids with binding of each Ca(2+) shared with
CC       ligands coming from each monomer. The Ca(2+) ion may have a role in
CC       catalysis. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric form is
CC       the active one. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=One of the very few enzymes
CC       located there. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
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; X76902; CAA54224.1; -; Genomic_DNA.
DR   PIR; C36971; C36971.
DR   AlphaFoldDB; P37447; -.
DR   SMR; P37447; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00541; OMPLA; 1.
DR   Gene3D; 2.40.230.10; -; 1.
DR   InterPro; IPR003187; PLipase_A1.
DR   InterPro; IPR036541; PLipase_A1_sf.
DR   PANTHER; PTHR40457; PTHR40457; 1.
DR   Pfam; PF02253; PLA1; 1.
DR   PRINTS; PR01486; PHPHLIPASEA1.
DR   SUPFAM; SSF56931; SSF56931; 1.
PE   3: Inferred from homology;
KW   Calcium; Cell outer membrane; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..289
FT                   /note="Phospholipase A1"
FT                   /id="PRO_0000021987"
FT   TOPO_DOM        21..52
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        53..65
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        66..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        85..99
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        100..105
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..118
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        119..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        129..148
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        149..150
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        151..164
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        165..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        174..186
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        187..188
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        189..198
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        199..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        217..223
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        224..225
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        226..234
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        235..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        242..250
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        251..255
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        256..265
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        266..274
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        275..286
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        287..289
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /note="in monomeric form"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32945 MW;  D75516CFFB406997 CRC64;
     MRTGPGWLLA AAALPFFACA QEATIDKVHD TPAVRGSIIA NMLQEHDNPF TLYPYESNYL
     LYTYTSDLNK KAIESYNWSD NANKDEVKFQ LSLAFPLWRG ILGDNSLLGA SYTQRSWWQL
     SNTGESAPFR ETNYEPQLFL GFATDYSVGD WTLRDAEFGY NHQSNGRSDP TSRSWNRLYS
     RLMAQNGNWL VEVKPWYVIG DTSDNKNITK YMGYYQLKIG YQLGEAVLSA KGQYNWNTGY
     GGAELGVSYP ITKHVRFYTQ VYSGYGESLI DYDFNQTRVG MGVMLNDLF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024