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Reviewed, UniProtKB/Swiss-Prot P0A231 (PA1_SALTY)

Last modified February 9, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
    Phosphatidylcholine 1-acylhydrolase
    Outer membrane phospholipase A
      Short name=OM PLA
Gene names
Name: pldA
Ordered Locus Names: STM3957
ORF Names: STMD1.33
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.

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.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentCell membrane
Cell outer membrane
Membrane
   DomainSignal
Transmembrane
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase A1 activity

Inferred from electronic annotation. Source: EC

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 289269Phospholipase A1
PRO_0000021989

Regions

Topological domain21 – 5232Periplasmic By similarity
Transmembrane53 – 6513 By similarity
Topological domain66 – 8419Extracellular By similarity
Transmembrane85 – 9915 By similarity
Topological domain100 – 1056Periplasmic By similarity
Transmembrane106 – 11813 By similarity
Topological domain119 – 12810Extracellular By similarity
Transmembrane129 – 14820 By similarity
Topological domain149 – 1502Periplasmic By similarity
Transmembrane151 – 16414 By similarity
Topological domain165 – 1739Extracellular By similarity
Transmembrane174 – 18613 By similarity
Topological domain187 – 1882Periplasmic By similarity
Transmembrane189 – 19810 By similarity
Topological domain199 – 21618Extracellular By similarity
Transmembrane217 – 2237 By similarity
Topological domain224 – 2252Periplasmic By similarity
Transmembrane226 – 2349 By similarity
Topological domain235 – 2417Extracellular By similarity
Transmembrane242 – 2509 By similarity
Topological domain251 – 2555Periplasmic By similarity
Transmembrane256 – 26510 By similarity
Topological domain266 – 2749Extracellular By similarity
Transmembrane275 – 28612 By similarity
Topological domain287 – 2893Periplasmic By similarity

Sites

Active site1621Proton acceptor By similarity
Active site1641Nucleophile By similarity
Metal binding1261Calcium 1; via carbonyl oxygen; in dimeric form By similarity
Metal binding1671Calcium 2; via carbonyl oxygen; in dimeric form By similarity
Metal binding1721Calcium 2; in active dimeric form By similarity
Metal binding2041Calcium 3; in inactive monomeric form By similarity

Experimental info

Sequence conflict1551D → H in CAA54222. Ref.1
Sequence conflict1741S → T in CAA54222. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P0A231-1 [UniParc].

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

FASTA28932,967
        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

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References

« Hide 'large scale' references
[1]"Molecular characterization of enterobacterial pldA genes encoding outer membrane phospholipase A."
Brok R.G.P.M., Brinkman E., van Boxtel R., Bekkers A.C.A.P., Verheij H.M., Tommassen J.
J. Bacteriol. 176:861-870(1994) [PubMed: 8300539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76900 Genomic DNA. Translation: CAA54222.1.
AF233324 Genomic DNA. Translation: AAF33435.1.
AE006468 Genomic DNA. Translation: AAL22801.1.
PIRA36971.
RefSeqNP_462842.1.

3D structure databases

SMRP0A231. Positions 28-289.
ModBaseSearch...

Proteomic databases

PRIDEP0A231.

Genome annotation databases

GeneID1255483.
GenomeReviewsGene locus STM3957 in contig AE006468_GR.
KEGGstm:STM3957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG564477.
OMAYTRLMAQ.

Enzyme and pathway databases

BioCycSTYP99287:STM3957-MONOMER.
BRENDA3.1.1.32. 2.
3.1.1.4. 2.

Family and domain databases

InterProIPR003187. PLA1.
[Graphical view]
Gene3DG3DSA:2.40.230.10. PLA1. 1 hit.
PfamPF02253. PLA1. 1 hit.
[Graphical view]
PRINTSPR01486. PHPHLIPASEA1.
ProtoNetSearch...

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Entry information

Entry namePA1_SALTY
AccessionPrimary (citable) accession number: P0A231
Secondary accession number(s): P37442, Q9L6N9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents