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Protein

Phospholipase A1

Gene

pldA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.
Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per monomer. In the dimeric form the Ca2+ is bound by different amino acids with binding of each Ca2+ shared with ligands coming from each monomer (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other). The Ca2+ ion may have a role in catalysis.1 Publication

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi126Calcium 1; via carbonyl oxygen; in dimeric form1
Active sitei162Proton acceptorCurated1
Active sitei164Nucleophile1 Publication1
Metal bindingi167Calcium 2; via carbonyl oxygen; in dimeric form1
Metal bindingi172Calcium 2; in dimeric form1
Metal bindingi204Calcium 3; in monomeric form1

GO - Molecular functioni

  • 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
  • calcium ion binding Source: UniProtKB
  • phosphatidylcholine 1-acylhydrolase activity Source: UniProtKB
  • phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
  • phospholipase A2 activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
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
Short name:
OMPLA
Phosphatidylcholine 1-acylhydrolase
Gene namesi
Name:pldA
Ordered Locus Names:b3821, JW3794
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10738. pldA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 52PeriplasmicAdd BLAST32
Transmembranei53 – 65Beta strandedAdd BLAST13
Topological domaini66 – 84ExtracellularAdd BLAST19
Transmembranei85 – 99Beta strandedAdd BLAST15
Topological domaini100 – 105Periplasmic6
Transmembranei106 – 118Beta strandedAdd BLAST13
Topological domaini119 – 128Extracellular10
Transmembranei129 – 148Beta strandedAdd BLAST20
Topological domaini149 – 150Periplasmic2
Transmembranei151 – 164Beta strandedAdd BLAST14
Topological domaini165 – 173Extracellular9
Transmembranei174 – 186Beta strandedAdd BLAST13
Topological domaini187 – 188Periplasmic2
Transmembranei189 – 198Beta stranded10
Topological domaini199 – 216ExtracellularAdd BLAST18
Transmembranei217 – 223Beta stranded7
Topological domaini224 – 225Periplasmic2
Transmembranei226 – 234Beta stranded9
Topological domaini235 – 241Extracellular7
Transmembranei242 – 250Beta stranded9
Topological domaini251 – 255Periplasmic5
Transmembranei256 – 265Beta stranded10
Topological domaini266 – 274Extracellular9
Transmembranei275 – 286Beta strandedAdd BLAST12
Topological domaini287 – 289Periplasmic3

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of cell outer membrane Source: EcoCyc
  • intrinsic component of cell outer membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172S → F: Inactive protein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
ChainiPRO_000002198321 – 289Phospholipase A1Add BLAST269

Proteomic databases

PaxDbiP0A921.
PRIDEiP0A921.

Interactioni

Subunit structurei

Homodimer; dimerization is reversible, and the dimeric form is the active one.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi4259303. 272 interactors.
IntActiP0A921. 12 interactors.
STRINGi511145.b3821.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 43Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi59 – 67Combined sources9
Turni70 – 75Combined sources6
Helixi77 – 81Combined sources5
Beta strandi84 – 99Combined sources16
Turni100 – 102Combined sources3
Beta strandi106 – 118Combined sources13
Helixi123 – 125Combined sources3
Beta strandi129 – 148Combined sources20
Beta strandi151 – 164Combined sources14
Beta strandi169 – 171Combined sources3
Beta strandi174 – 186Combined sources13
Beta strandi189 – 200Combined sources12
Helixi208 – 212Combined sources5
Beta strandi214 – 223Combined sources10
Beta strandi226 – 234Combined sources9
Turni236 – 238Combined sources3
Beta strandi241 – 252Combined sources12
Beta strandi255 – 265Combined sources11
Helixi269 – 271Combined sources3
Beta strandi275 – 285Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP0A921.
SMRiP0A921.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A921.

Family & Domainsi

Sequence similaritiesi

Belongs to the phospholipase A1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105HDD. Bacteria.
COG2829. LUCA.
HOGENOMiHOG000288150.
InParanoidiP0A921.
KOiK01058.
OMAiVEFGYNH.
PhylomeDBiP0A921.

Family and domain databases

CDDicd00541. OMPLA. 1 hit.
Gene3Di2.40.230.10. 1 hit.
InterProiIPR003187. PLipase_A1.
[Graphical view]
PfamiPF02253. PLA1. 1 hit.
[Graphical view]
PRINTSiPR01486. PHPHLIPASEA1.
SUPFAMiSSF56931. SSF56931. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLQGWLLP VFMLPMAVYA QEATVKEVHD APAVRGSIIA NMLQEHDNPF
60 70 80 90 100
TLYPYDTNYL IYTQTSDLNK EAIASYDWAE NARKDEVKFQ LSLAFPLWRG
110 120 130 140 150
ILGPNSVLGA SYTQKSWWQL SNSEESSPFR ETNYEPQLFL GFATDYRFAG
160 170 180 190 200
WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT RLMAENGNWL VEVKPWYVVG
210 220 230 240 250
NTDDNPDITK YMGYYQLKIG YHLGDAVLSA KGQYNWNTGY GGAELGLSYP
260 270 280
ITKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDLF
Length:289
Mass (Da):33,163
Last modified:July 19, 2005 - v1
Checksum:iA688AD32AA60F218
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15LP → FA in AAA67617 (PubMed:1379743).Curated2
Sequence conflicti30 – 33DAPA → MTRQ (PubMed:6383820).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA22133. PSECA1.
RefSeqiNP_418265.1. NC_000913.3.
WP_001259700.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76824; AAC76824; b3821.
BAE77480; BAE77480; BAE77480.
GeneIDi948307.
KEGGiecj:JW3794.
eco:b3821.
PATRICi32123143. VBIEscCol129921_3937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA22133. PSECA1.
RefSeqiNP_418265.1. NC_000913.3.
WP_001259700.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP0A921.
SMRiP0A921.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259303. 272 interactors.
IntActiP0A921. 12 interactors.
STRINGi511145.b3821.

Proteomic databases

PaxDbiP0A921.
PRIDEiP0A921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76824; AAC76824; b3821.
BAE77480; BAE77480; BAE77480.
GeneIDi948307.
KEGGiecj:JW3794.
eco:b3821.
PATRICi32123143. VBIEscCol129921_3937.

Organism-specific databases

EchoBASEiEB0731.
EcoGeneiEG10738. pldA.

Phylogenomic databases

eggNOGiENOG4105HDD. Bacteria.
COG2829. LUCA.
HOGENOMiHOG000288150.
InParanoidiP0A921.
KOiK01058.
OMAiVEFGYNH.
PhylomeDBiP0A921.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A921.
PROiP0A921.

Family and domain databases

CDDicd00541. OMPLA. 1 hit.
Gene3Di2.40.230.10. 1 hit.
InterProiIPR003187. PLipase_A1.
[Graphical view]
PfamiPF02253. PLA1. 1 hit.
[Graphical view]
PRINTSiPR01486. PHPHLIPASEA1.
SUPFAMiSSF56931. SSF56931. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPA1_ECOLI
AccessioniPrimary (citable) accession number: P0A921
Secondary accession number(s): P00631, Q2M8C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2005
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.