Phospholipase A1 precursor - Salmonella typhi

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P0A232 (PA1_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phospholipase A1
EC=3.1.1.32
EC=3.1.1.4

Alternative name(s):
Detergent-resistant phospholipase A
Short name=DR-phospholipase A
Outer membrane phospholipase A
Short name=OM PLA
Phosphatidylcholine 1-acylhydrolase

Gene names

Name:	pldA
Ordered Locus Names:	STY3602, t3340

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (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. Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per monomer. In the dimeric form the calcium is bound by different amino acids with binding of each calcium shared with ligands coming from each monomer. The calcium ion may have a role in catalysis By similarity.
Subunit structure	Homodimer; dimerization is reversible, and the dimeric form is the active one By similarity.
Subcellular location	Cell outer membrane; Multi-pass membrane protein By similarity. Note: One of the very few enzymes located there By similarity.
Sequence similarities	Belongs to the phospholipase A1 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal Transmembrane Transmembrane beta strand
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-acyl-2-lysophosphatidylserine acylhydrolase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylcholine 1-acylhydrolase activity Inferred from electronic annotation. Source: EC phosphatidylserine 1-acylhydrolase activity Inferred from electronic annotation. Source: EC phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

By similarity

Chain

21 – 289

269

Phospholipase A1

PRO_0000021988

Regions

Topological domain

21 – 52

Periplasmic By similarity

Transmembrane

53 – 65

Beta stranded; By similarity

Topological domain

66 – 84

Extracellular By similarity

Transmembrane

85 – 99

Beta stranded; By similarity

Topological domain

100 – 105

Periplasmic By similarity

Transmembrane

106 – 118

Beta stranded; By similarity

Topological domain

119 – 128

Extracellular By similarity

Transmembrane

129 – 148

Beta stranded; By similarity

Topological domain

149 – 150

Periplasmic By similarity

Transmembrane

151 – 164

Beta stranded; By similarity

Topological domain

165 – 173

Extracellular By similarity

Transmembrane

174 – 186

Beta stranded; By similarity

Topological domain

187 – 188

Periplasmic By similarity

Transmembrane

189 – 198

Beta stranded; By similarity

Topological domain

199 – 216

Extracellular By similarity

Transmembrane

217 – 223

Beta stranded; By similarity

Topological domain

224 – 225

Periplasmic By similarity

Transmembrane

226 – 234

Beta stranded; By similarity

Topological domain

235 – 241

Extracellular By similarity

Transmembrane

242 – 250

Beta stranded; By similarity

Topological domain

251 – 255

Periplasmic By similarity

Transmembrane

256 – 265

Beta stranded; By similarity

Topological domain

266 – 274

Extracellular By similarity

Transmembrane

275 – 286

Beta stranded; By similarity

Topological domain

287 – 289

Periplasmic By similarity

Sites

Active site

162

Proton acceptor By similarity

Active site

164

Nucleophile By similarity

Metal binding

126

Calcium 1; via carbonyl oxygen; in dimeric form By similarity

Metal binding

167

Calcium 2; via carbonyl oxygen; in dimeric form By similarity

Metal binding

172

Calcium 2; in dimeric form By similarity

Metal binding

204

Calcium 3; in monomeric form By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A232 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: DA97F5E1651C49C6
Show »

FASTA

289

32,967

        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

« Hide

References

[1]	"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." 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. Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.
[2]	"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627278 Genomic DNA. Translation: CAD07935.1. AE014613 Genomic DNA. Translation: AAO70868.1.
RefSeq	NP_457794.1. NC_003198.1. NP_807008.1. NC_004631.1.
3D structure databases
ProteinModelPortal	P0A232.
SMR	P0A232. Positions 28-289.
ModBase	Search...
Proteomic databases
PRIDE	P0A232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1071539. 1249857.
GenomeReviews	Gene locus t3340 in contig AE014613_GR. Gene locus STY3602 in contig AL513382_GR.
KEGG	stt:t3340. sty:STY3602.
PATRIC	18545314. VBISalEnt120419_3671.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG564477.
OMA	YNWNSGY.
ProtClustDB	PRK10763.
Enzyme and pathway databases
BioCyc	SENT209261:T3340-MONOMER. SENT220341:STY3602-MONOMER.
Family and domain databases
InterPro	IPR003187. PLipase_A1. [Graphical view]
Gene3D	G3DSA:2.40.230.10. PLA1. 1 hit.
KO	K01058.
Pfam	PF02253. PLA1. 1 hit. [Graphical view]
PRINTS	PR01486. PHPHLIPASEA1.
SUPFAM	SSF56931. PLA1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PA1_SALTI

Accession

Primary (citable) accession number: P0A232
Secondary accession number(s): P37442, Q9L6N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents