EC 3.1.1.32
EC 3.1.1.4
Detergent-resistant phospholipase A
DR-phospholipase A
Phosphatidylcholine 1-acylhydrolase
Outer membrane phospholipase A
OM PLA

Gene name

	Name:	pldA
	OrderedLocusNames:	STY3602, t3340

From

Salmonella typhi

[TaxID: 601]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CT18;
DOI=10.1038/35101607; PubMed=11677608 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.";
Nature 413:848-852(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700931 / Ty2;
DOI=10.1128/JB.185.7.2330-2337.2003; PubMed=12644504 [NCBI, ExPASy, EBI, Israel, Japan]
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.";
J. Bacteriol. 185:2330-2337(2003).

Comments

FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities (By similarity).
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 2-acylglycerophosphocholine + a carboxylate.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Calcium (By similarity).
SUBCELLULAR LOCATION: Cell outer membrane (By similarity). Note=One of the very few enzymes located there (By similarity).
SIMILARITY: Belongs to the phospholipase A1 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AL627278; CAD07935.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014613; AAO70868.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_457794.1; -.
NP_807008.1; -.

3D structure databases

HSSP

P00631; 1QD6. [HSSP ENTRY / PDB]

SMR

P0A232; 28-289.

ModBase

P0A232.

Enzyme and pathway databases

BioCyc

SENT209261:T3340-MON; -.
SENT220341:STY3602-MON; -.

Ontologies

GO:0009279;	Cellular component: cell outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008970;	Molecular function: phospholipase A1 activity (inferred from electronic annotation from EC).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from EC).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003187; PLA1.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.230.10; PLA1; 1.

Pfam

PF02253; PLA1; 1.
Pfam graphical view of domain structure.

PRINTS

PR01486; PHPHLIPASEA1.

Genome annotation databases

GeneID

1071539; -.
1249857; -.

GenomeReviews

AE014613_GR; t3340.
AL513382_GR; STY3602.

KEGG

stt:t3340; -.
sty:STY3602; -.

Phylogenomic databases

HOGENOM

P0A232; -.

Genome annotation databases

CMR

P0A232; STY3602.

Other

ProtoNet

P0A232.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Cell membrane; Cell outer membrane; Complete proteome; Hydrolase; Lipid degradation; Membrane; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`By similarity.`
`CHAIN`	`21 289`	`269`	`Phospholipase A1.`	`PRO_0000021988`
`ACT_SITE`	`164 164`		`By similarity.`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 32967 Da [This is the MW of the unprocessed precursor]

CRC64: DA97F5E1651C49C6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRAILRGLLP ATLLPLAAYA QEATIKEVHD APAVRGSIIA NMLQEHDNPF TLYPYDTNYL 

        70         80         90        100        110        120 
IYTNTSDLNK EAISTYNWSE NARKDEVKFQ LSLAFPLWRG ILGPNSVLGA SYTQKSWWQL 

       130        140        150        160        170        180 
SNSKESSPFR ETNYEPQLFL GFATDYRFAG WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT 

       190        200        210        220        230        240 
RLMAENGNWL VEVKPWYVIG STDDNPDITK YMGYYQLKIG YHLGEAVLSA KGQYNWNTGY 

       250        260        270        280 
GGAEVGLSYP VTKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDIF

P0A232 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools