UniProtKB - P0A921 (PA1_ECOLI)
Protein
Phospholipase A1
Gene
pldA
Organism
Escherichia coli (strain K12)
Status
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
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+EC:3.1.1.32
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+EC:3.1.1.4
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
Activity 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 126 | Calcium 1; via carbonyl oxygen; in dimeric form | 1 | |
Active sitei | 162 | Proton acceptorCurated | 1 | |
Active sitei | 164 | Nucleophile1 Publication | 1 | |
Metal bindingi | 167 | Calcium 2; via carbonyl oxygen; in dimeric form | 1 | |
Metal bindingi | 172 | Calcium 2; in dimeric form | 1 | |
Metal bindingi | 204 | Calcium 3; in monomeric form | 1 |
GO - Molecular functioni
- 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
- calcium ion binding Source: UniProtKB
- lysophospholipase activity Source: EcoCyc
- phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
- phospholipase A1 activity Source: UniProtKB
- phospholipase A2 activity Source: EcoCyc
- phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
- phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
- phospholipase activity Source: EcoCyc
- protein homodimerization activity Source: UniProtKB
GO - Biological processi
- lipid catabolic process Source: UniProtKB-KW
- phosphatidylglycerol metabolic process Source: EcoCyc
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:MONOMER0-341 MetaCyc:MONOMER0-341 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pldA Ordered Locus Names:b3821, JW3794 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell outer membrane 1 Publication; Multi-pass membrane protein 1 Publication Note: One of the very few enzymes located there.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 21 – 52 | PeriplasmicAdd BLAST | 32 | |
Transmembranei | 53 – 65 | Beta strandedAdd BLAST | 13 | |
Topological domaini | 66 – 84 | ExtracellularAdd BLAST | 19 | |
Transmembranei | 85 – 99 | Beta strandedAdd BLAST | 15 | |
Topological domaini | 100 – 105 | Periplasmic | 6 | |
Transmembranei | 106 – 118 | Beta strandedAdd BLAST | 13 | |
Topological domaini | 119 – 128 | Extracellular | 10 | |
Transmembranei | 129 – 148 | Beta strandedAdd BLAST | 20 | |
Topological domaini | 149 – 150 | Periplasmic | 2 | |
Transmembranei | 151 – 164 | Beta strandedAdd BLAST | 14 | |
Topological domaini | 165 – 173 | Extracellular | 9 | |
Transmembranei | 174 – 186 | Beta strandedAdd BLAST | 13 | |
Topological domaini | 187 – 188 | Periplasmic | 2 | |
Transmembranei | 189 – 198 | Beta stranded | 10 | |
Topological domaini | 199 – 216 | ExtracellularAdd BLAST | 18 | |
Transmembranei | 217 – 223 | Beta stranded | 7 | |
Topological domaini | 224 – 225 | Periplasmic | 2 | |
Transmembranei | 226 – 234 | Beta stranded | 9 | |
Topological domaini | 235 – 241 | Extracellular | 7 | |
Transmembranei | 242 – 250 | Beta stranded | 9 | |
Topological domaini | 251 – 255 | Periplasmic | 5 | |
Transmembranei | 256 – 265 | Beta stranded | 10 | |
Topological domaini | 266 – 274 | Extracellular | 9 | |
Transmembranei | 275 – 286 | Beta strandedAdd BLAST | 12 | |
Topological domaini | 287 – 289 | Periplasmic | 3 |
GO - Cellular componenti
- cell outer membrane Source: EcoCyc
- integral component of cell outer membrane Source: EcoCyc
- intrinsic component of cell outer membrane Source: UniProtKB
Keywords - Cellular componenti
Cell outer membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 172 | S → F: Inactive protein. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03692, 1-Hexadecanosulfonyl-O-L-Serine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | 2 PublicationsAdd BLAST | 20 | |
ChainiPRO_0000021983 | 21 – 289 | Phospholipase A1Add BLAST | 269 |
Proteomic databases
jPOSTi | P0A921 |
PaxDbi | P0A921 |
PRIDEi | P0A921 |
Interactioni
Subunit structurei
Homodimer; dimerization is reversible, and the dimeric form is the active one.
3 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 4259303, 274 interactors |
IntActi | P0A921, 12 interactors |
STRINGi | 511145.b3821 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A921 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A921 |
Family & Domainsi
Sequence similaritiesi
Belongs to the phospholipase A1 family.Curated
Keywords - Domaini
Signal, Transmembrane, Transmembrane beta strandPhylogenomic databases
eggNOGi | COG2829, Bacteria |
HOGENOMi | CLU_045813_1_0_6 |
InParanoidi | P0A921 |
PhylomeDBi | P0A921 |
Family and domain databases
CDDi | cd00541, OMPLA, 1 hit |
Gene3Di | 2.40.230.10, 1 hit |
InterProi | View protein in InterPro IPR003187, PLipase_A1 IPR036541, PLipase_A1_sf |
PANTHERi | PTHR40457, PTHR40457, 1 hit |
Pfami | View protein in Pfam PF02253, PLA1, 1 hit |
PRINTSi | PR01486, PHPHLIPASEA1 |
SUPFAMi | SSF56931, SSF56931, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A921-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 14 – 15 | LP → FA in AAA67617 (PubMed:1379743).Curated | 2 | |
Sequence conflicti | 30 – 33 | DAPA → MTRQ (PubMed:6383820).Curated | 4 |
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 |
PIRi | A22133, PSECA1 |
RefSeqi | NP_418265.1, NC_000913.3 WP_001259700.1, NZ_SSZK01000046.1 |
Genome annotation databases
EnsemblBacteriai | AAC76824; AAC76824; b3821 BAE77480; BAE77480; BAE77480 |
GeneIDi | 48723712 948307 |
KEGGi | ecj:JW3794 eco:b3821 |
PATRICi | fig|1411691.4.peg.2886 |
Similar proteinsi
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 |
PIRi | A22133, PSECA1 |
RefSeqi | NP_418265.1, NC_000913.3 WP_001259700.1, NZ_SSZK01000046.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FW2 | X-ray | 2.60 | A | 21-289 | [»] | |
1FW3 | X-ray | 2.80 | A/B | 21-289 | [»] | |
1ILD | X-ray | 2.80 | A | 21-289 | [»] | |
1ILZ | X-ray | 2.50 | A | 21-289 | [»] | |
1IM0 | X-ray | 2.98 | A | 21-289 | [»] | |
1QD5 | X-ray | 2.17 | A | 21-289 | [»] | |
1QD6 | X-ray | 2.10 | A/B | 33-45 | [»] | |
C/D | 50-289 | [»] | ||||
SMRi | P0A921 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259303, 274 interactors |
IntActi | P0A921, 12 interactors |
STRINGi | 511145.b3821 |
Chemistry databases
DrugBanki | DB03692, 1-Hexadecanosulfonyl-O-L-Serine |
Proteomic databases
jPOSTi | P0A921 |
PaxDbi | P0A921 |
PRIDEi | P0A921 |
Genome annotation databases
EnsemblBacteriai | AAC76824; AAC76824; b3821 BAE77480; BAE77480; BAE77480 |
GeneIDi | 48723712 948307 |
KEGGi | ecj:JW3794 eco:b3821 |
PATRICi | fig|1411691.4.peg.2886 |
Organism-specific databases
EchoBASEi | EB0731 |
Phylogenomic databases
eggNOGi | COG2829, Bacteria |
HOGENOMi | CLU_045813_1_0_6 |
InParanoidi | P0A921 |
PhylomeDBi | P0A921 |
Enzyme and pathway databases
BioCyci | EcoCyc:MONOMER0-341 MetaCyc:MONOMER0-341 |
Miscellaneous databases
EvolutionaryTracei | P0A921 |
PROi | PR:P0A921 |
Family and domain databases
CDDi | cd00541, OMPLA, 1 hit |
Gene3Di | 2.40.230.10, 1 hit |
InterProi | View protein in InterPro IPR003187, PLipase_A1 IPR036541, PLipase_A1_sf |
PANTHERi | PTHR40457, PTHR40457, 1 hit |
Pfami | View protein in Pfam PF02253, PLA1, 1 hit |
PRINTSi | PR01486, PHPHLIPASEA1 |
SUPFAMi | SSF56931, SSF56931, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PA1_ECOLI | |
Accessioni | P0A921Primary (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: | December 2, 2020 | |
This is version 115 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families