pldA

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

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	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
Inferred from direct assayⁱ
- 11371166
phosphatidylcholine 1-acylhydrolase activity
Source: UniProtKB
Traceable author statementⁱ
- 11371166
phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
phospholipase A2 activity
Source: EcoCyc
Inferred from direct assayⁱ
- 2653433
phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine) Source: UniProtKB-EC
phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine) Source: UniProtKB-EC
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11371166

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

lipid catabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

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

BioCycⁱ

EcoCyc:MONOMER0-341
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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10738 pldA

EcoGeneⁱ

EG10738 pldA

Subcellular locationⁱ

Topology

Feature key	Position(s)	DescriptionActions	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
Inferred from direct assayⁱ
- 10806384
integral component of cell outer membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 6397463
intrinsic component of cell outer membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 11371166

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	172	S → F: Inactive protein. 1 Publication		1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03692 1-Hexadecanosulfonyl-O-L-Serine

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

PaxDbⁱ	P0A921
PRIDEⁱ	P0A921

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
Inferred from direct assayⁱ
- 11371166

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259303, 274 interactors
IntActⁱ	P0A921, 12 interactors
STRINGⁱ	316385.ECDH10B_4012

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	38 – 43	Combined sources	6
Beta strandⁱ	52 – 54	Combined sources	3
Beta strandⁱ	59 – 67	Combined sources	9
Turnⁱ	70 – 75	Combined sources	6
Helixⁱ	77 – 81	Combined sources	5
Beta strandⁱ	84 – 99	Combined sources	16
Turnⁱ	100 – 102	Combined sources	3
Beta strandⁱ	106 – 118	Combined sources	13
Helixⁱ	123 – 125	Combined sources	3
Beta strandⁱ	129 – 148	Combined sources	20
Beta strandⁱ	151 – 164	Combined sources	14
Beta strandⁱ	169 – 171	Combined sources	3
Beta strandⁱ	174 – 186	Combined sources	13
Beta strandⁱ	189 – 200	Combined sources	12
Helixⁱ	208 – 212	Combined sources	5
Beta strandⁱ	214 – 223	Combined sources	10
Beta strandⁱ	226 – 234	Combined sources	9
Turnⁱ	236 – 238	Combined sources	3
Beta strandⁱ	241 – 252	Combined sources	12
Beta strandⁱ	255 – 265	Combined sources	11
Helixⁱ	269 – 271	Combined sources	3
Beta strandⁱ	275 – 285	Combined sources	11

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A921
SMRⁱ	P0A921
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P0A921

EvolutionaryTraceⁱ

P0A921

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the phospholipase A1 family.Curated

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGⁱ	ENOG4105HDD Bacteria COG2829 LUCA
HOGENOMⁱ	HOG000288150
InParanoidⁱ	P0A921
KEGG Orthology (KO) More...KOⁱ	K01058
OMAⁱ	WGGCRSV
PhylomeDBⁱ	P0A921

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02253 PLA1, 1 hit
PRINTSⁱ	PR01486 PHPHLIPASEA1
SUPFAMⁱ	SSF56931 SSF56931, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0A921-1 [UniParc]FASTA Add 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 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
NCBI Reference Sequences More...RefSeqⁱ	NP_418265.1, NC_000913.3 WP_001259700.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76824; AAC76824; b3821 BAE77480; BAE77480; BAE77480
GeneIDⁱ	948307
KEGGⁱ	ecj:JW3794 eco:b3821
PATRICⁱ	fig\|1411691.4.peg.2886

Protein	Similar proteins		Species	Score	Length	Source
P0A921	Phospholipase A1		ECO57		289	UniRef100_P0A922
Phospholipase A1		SHIFL		289
Phospholipase A		Shigella flexneri 2a		289
Outer membrane phospholipase A		Escherichia coli NCCP15648		289
Phospholipase A(1)		Escherichia coli O145 str. RM9872		289
+126

Protein	Similar proteins		Species	Score	Length	Source
P0A921	Phospholipase A1		ECO57		289	UniRef90_P0A922
Phospholipase A1		SHIFL		289
Phospholipase A		Shigella flexneri 2a		289
Outer membrane phospholipase A		Escherichia coli NCCP15648		289
Phospholipase A(1)		Escherichia coli O145 str. RM9872		289
+520

Protein	Similar proteins		Species	Score	Length	Source
P0A921	Phospholipase A1		ECO57		289	UniRef50_P0A922
Phospholipase A1		SHIFL		289
Phospholipase A1		PROVU		289
Phospholipase A1		KLEPN		286
Phospholipase A		Shigella flexneri 2a		289
+1288

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:	September 12, 2018
	This is version 101 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, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

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UniRef

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Annotation systems

Supporting data

UniProtKB - P0A921 (PA1_ECOLI)

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Phospholipase A1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ