PA1_SHIFL
ID PA1_SHIFL Reviewed; 289 AA.
AC P0A923; P00631;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Short=OMPLA;
DE AltName: Full=Phosphatidylcholine 1-acylhydrolase;
DE Flags: Precursor;
GN Name=pldA; OrderedLocusNames=SF3899, S3856;
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: 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}.
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DR EMBL; AE005674; AAN45334.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18864.1; -; Genomic_DNA.
DR RefSeq; NP_709627.1; NC_004337.2.
DR RefSeq; WP_001259700.1; NZ_WPGW01000036.1.
DR AlphaFoldDB; P0A923; -.
DR SMR; P0A923; -.
DR STRING; 198214.SF3899; -.
DR EnsemblBacteria; AAN45334; AAN45334; SF3899.
DR EnsemblBacteria; AAP18864; AAP18864; S3856.
DR GeneID; 1023494; -.
DR GeneID; 66672271; -.
DR KEGG; sfl:SF3899; -.
DR KEGG; sfx:S3856; -.
DR PATRIC; fig|198214.7.peg.4599; -.
DR HOGENOM; CLU_045813_1_0_6; -.
DR OMA; WGGCRSV; -.
DR OrthoDB; 1546598at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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; Reference proteome; Signal;
KW Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..289
FT /note="Phospholipase A1"
FT /id="PRO_0000021985"
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; 33163 MW; A688AD32AA60F218 CRC64;
MRTLQGWLLP VFMLPMAVYA QEATVKEVHD APAVRGSIIA NMLQEHDNPF TLYPYDTNYL
IYTQTSDLNK EAIASYDWAE NARKDEVKFQ LSLAFPLWRG ILGPNSVLGA SYTQKSWWQL
SNSEESSPFR ETNYEPQLFL GFATDYRFAG WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT
RLMAENGNWL VEVKPWYVVG NTDDNPDITK YMGYYQLKIG YHLGDAVLSA KGQYNWNTGY
GGAELGLSYP ITKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDLF
