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P0A921 (PA1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Outer membrane phospholipase A
Short name=OM PLA
Short name=OMPLA
Phosphatidylcholine 1-acylhydrolase
Gene names
Name:pldA
Ordered Locus Names:b3821, JW3794
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins.

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 (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other). The calcium ion may have a role in catalysis. Ref.13

Enzyme regulation

By membrane damage, for example, by phage-induced lysis or temperature shock. The protein is inactive in the monomeric form and active in the dimeric form; calcium is essential for dimer stability. Ref.11 Ref.12

Subunit structure

Homodimer; dimerization is reversible, and the dimeric form is the active one. Ref.11 Ref.12 Ref.13

Subcellular location

Cell outer membrane; Multi-pass membrane protein. Note: One of the very few enzymes located there. Ref.8

Sequence similarities

Belongs to the phospholipase A1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

yhjCP376411EBI-1119179,EBI-849303

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1 Ref.5
Chain21 – 289269Phospholipase A1
PRO_0000021983

Regions

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

Sites

Active site1621Proton acceptor Probable
Active site1641Nucleophile Ref.10
Metal binding1261Calcium 1; via carbonyl oxygen; in dimeric form
Metal binding1671Calcium 2; via carbonyl oxygen; in dimeric form
Metal binding1721Calcium 2; in dimeric form
Metal binding2041Calcium 3; in monomeric form

Experimental info

Mutagenesis1721S → F: Inactive protein. Ref.9
Sequence conflict14 – 152LP → FA in AAA67617. Ref.2
Sequence conflict30 – 334DAPA → MTRQ Ref.6

Secondary structure

............................................ 289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A921 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: A688AD32AA60F218

FASTA28933,163
        10         20         30         40         50         60 
MRTLQGWLLP VFMLPMAVYA QEATVKEVHD APAVRGSIIA NMLQEHDNPF TLYPYDTNYL 

        70         80         90        100        110        120 
IYTQTSDLNK EAIASYDWAE NARKDEVKFQ LSLAFPLWRG ILGPNSVLGA SYTQKSWWQL 

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

       190        200        210        220        230        240 
RLMAENGNWL VEVKPWYVVG NTDDNPDITK YMGYYQLKIG YHLGDAVLSA KGQYNWNTGY 

       250        260        270        280 
GGAELGLSYP ITKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDLF 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence encoding pldA gene, the structural gene for detergent-resistant phospholipase A of E. coli."
Homma H., Kobayashi T., Chiba N., Karasawa K., Mizushima H., Kudo I., Inoue K., Ikeda H., Sekiguchi M., Nojima S.
J. Biochem. 96:1655-1664(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-30.
Strain: K12.
[2]"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 14-15.
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"In vitro folding of Escherichia coli outer-membrane phospholipase A."
Dekker N., Merck K., Tommassen J., Verheij H.M.
Eur. J. Biochem. 232:214-219(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-24.
Strain: K12.
[6]"The pro- and mature forms of the E. coli K-12 outer membrane phospholipase A are identical."
de Geus P., Verheij H.M., Riegman N.H., Hoekstra W.P.M., de Haas G.H.
EMBO J. 3:1799-1802(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-289.
Strain: K12.
[7]"The recQ gene of Escherichia coli K12: primary structure and evidence for SOS regulation."
Irino N., Nakayama K., Nakayama H.
Mol. Gen. Genet. 205:298-304(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-289.
Strain: K12.
[8]"Characteristics of detergent-resistant phospholipase A overproduced in E. coli cells bearing its cloned structural gene."
Homma H., Chiba N., Kobayashi T., Kudo I., Inoue K., Ikeda H., Sekiguchi M., Nojima S.
J. Biochem. 96:1645-1653(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12.
[9]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-172.
[10]"Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active-site serine."
Horrevoets A.J.G., Verheij H.M., de Haas G.H.
Eur. J. Biochem. 198:247-253(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE SER-164, PARTIAL PROTEIN SEQUENCE.
[11]"Dimerization regulates the enzymatic activity of Escherichia coli outer membrane phospholipase A."
Dekker N., Tommassen J., Lustig A., Rosenbusch J.P., Verheij H.M.
J. Biol. Chem. 272:3179-3184(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, ENZYME REGULATION.
[12]"Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo."
Dekker N., Tommassen J., Verheij H.M.
J. Bacteriol. 181:3281-3283(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, ENZYME REGULATION.
[13]"Structural evidence for dimerization-regulated activation of an integral membrane phospholipase."
Snijder H.J., Ubarretxena-Belandia I., Blaauw M., Kalk K.H., Verheij H.M., Egmond M.R., Dekker N., Dijkstra B.W.
Nature 401:717-721(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-289 IN MONOMERIC AND DIMERIC FORM, COFACTOR, SUBUNIT.
[14]"Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli."
Snijder H.J., Kingma R.L., Kalk K.H., Dekker N., Egmond M.R., Dijkstra B.W.
J. Mol. Biol. 309:477-489(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-289 IN MONOMERIC AND DIMERIC FORM IN THE PRESENCE AND ABSENCE OF CALCIUM.
[15]"Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad."
Snijder H.J., Van Eerde J.H., Kingma R.L., Kalk K.H., Dekker N., Egmond M.R., Dijkstra B.W.
Protein Sci. 10:1962-1969(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 21-289 OF MUTANT ALA-156.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02143 Genomic DNA. Translation: CAA26081.1.
M87049 Genomic DNA. Translation: AAA67617.1.
U00096 Genomic DNA. Translation: AAC76824.1.
AP009048 Genomic DNA. Translation: BAE77480.1.
M30198 Genomic DNA. Translation: AAA24516.1.
PIRPSECA1. A22133.
RefSeqNP_418265.1. NC_000913.3.
YP_491621.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FW2X-ray2.60A21-289[»]
1FW3X-ray2.80A/B21-289[»]
1ILDX-ray2.80A21-289[»]
1ILZX-ray2.50A21-289[»]
1IM0X-ray2.98A21-289[»]
1QD5X-ray2.17A21-289[»]
1QD6X-ray2.10A/B33-45[»]
C/D50-289[»]
ProteinModelPortalP0A921.
SMRP0A921. Positions 33-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A921. 12 interactions.
STRING511145.b3821.

Proteomic databases

PaxDbP0A921.
PRIDEP0A921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76824; AAC76824; b3821.
BAE77480; BAE77480; BAE77480.
GeneID12930309.
948307.
KEGGecj:Y75_p3357.
eco:b3821.
PATRIC32123143. VBIEscCol129921_3937.

Organism-specific databases

EchoBASEEB0731.
EcoGeneEG10738. pldA.

Phylogenomic databases

eggNOGCOG2829.
HOGENOMHOG000288150.
KOK01058.
OMAYNHRQTR.
OrthoDBEOG6HQSN6.
ProtClustDBPRK10763.

Enzyme and pathway databases

BioCycEcoCyc:MONOMER0-341.
ECOL316407:JW3794-MONOMER.
MetaCyc:MONOMER0-341.

Gene expression databases

GenevestigatorP0A921.

Family and domain databases

Gene3D2.40.230.10. 1 hit.
InterProIPR003187. PLipase_A1.
[Graphical view]
PfamPF02253. PLA1. 1 hit.
[Graphical view]
PRINTSPR01486. PHPHLIPASEA1.
SUPFAMSSF56931. SSF56931. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A921.
PROP0A921.

Entry information

Entry namePA1_ECOLI
AccessionPrimary (citable) accession number: P0A921
Secondary accession number(s): P00631, Q2M8C6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene