Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A921

- PA1_ECOLI

UniProt

P0A921 - PA1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phospholipase A1

Gene

pldA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other). The Ca(2+) 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Calcium 1; via carbonyl oxygen; in dimeric form
Active sitei162 – 1621Proton acceptorCurated
Active sitei164 – 1641Nucleophile1 Publication
Metal bindingi167 – 1671Calcium 2; via carbonyl oxygen; in dimeric form
Metal bindingi172 – 1721Calcium 2; in dimeric form
Metal bindingi204 – 2041Calcium 3; in monomeric form

GO - Molecular functioni

  1. 1-acyl-2-lysophosphatidylserine acylhydrolase activity Source: UniProtKB-EC
  2. calcium ion binding Source: UniProtKB
  3. phosphatidylcholine 1-acylhydrolase activity Source: UniProtKB
  4. phosphatidylserine 1-acylhydrolase activity Source: UniProtKB-EC
  5. phospholipase A2 activity Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10738. pldA.

Subcellular locationi

Cell outer membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: One of the very few enzymes located there.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 5232PeriplasmicAdd
BLAST
Transmembranei53 – 6513Beta strandedAdd
BLAST
Topological domaini66 – 8419ExtracellularAdd
BLAST
Transmembranei85 – 9915Beta strandedAdd
BLAST
Topological domaini100 – 1056Periplasmic
Transmembranei106 – 11813Beta strandedAdd
BLAST
Topological domaini119 – 12810Extracellular
Transmembranei129 – 14820Beta strandedAdd
BLAST
Topological domaini149 – 1502Periplasmic
Transmembranei151 – 16414Beta strandedAdd
BLAST
Topological domaini165 – 1739Extracellular
Transmembranei174 – 18613Beta strandedAdd
BLAST
Topological domaini187 – 1882Periplasmic
Transmembranei189 – 19810Beta stranded
Topological domaini199 – 21618ExtracellularAdd
BLAST
Transmembranei217 – 2237Beta stranded
Topological domaini224 – 2252Periplasmic
Transmembranei226 – 2349Beta stranded
Topological domaini235 – 2417Extracellular
Transmembranei242 – 2509Beta stranded
Topological domaini251 – 2555Periplasmic
Transmembranei256 – 26510Beta stranded
Topological domaini266 – 2749Extracellular
Transmembranei275 – 28612Beta strandedAdd
BLAST
Topological domaini287 – 2893Periplasmic

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721S → F: Inactive protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 289269Phospholipase A1PRO_0000021983Add
BLAST

Proteomic databases

PaxDbiP0A921.
PRIDEiP0A921.

Expressioni

Gene expression databases

GenevestigatoriP0A921.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
yhjCP376411EBI-1119179,EBI-849303

Protein-protein interaction databases

IntActiP0A921. 12 interactions.
STRINGi511145.b3821.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 436Combined sources
Beta strandi52 – 543Combined sources
Beta strandi59 – 679Combined sources
Turni70 – 756Combined sources
Helixi77 – 815Combined sources
Beta strandi84 – 9916Combined sources
Turni100 – 1023Combined sources
Beta strandi106 – 11813Combined sources
Helixi123 – 1253Combined sources
Beta strandi129 – 14820Combined sources
Beta strandi151 – 16414Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi174 – 18613Combined sources
Beta strandi189 – 20012Combined sources
Helixi208 – 2125Combined sources
Beta strandi214 – 22310Combined sources
Beta strandi226 – 2349Combined sources
Turni236 – 2383Combined sources
Beta strandi241 – 25212Combined sources
Beta strandi255 – 26511Combined sources
Helixi269 – 2713Combined sources
Beta strandi275 – 28511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 33-289.
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

eggNOGiCOG2829.
HOGENOMiHOG000288150.
InParanoidiP0A921.
KOiK01058.
OMAiWNRVYAR.
OrthoDBiEOG6HQSN6.
PhylomeDBiP0A921.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152LP → FA in AAA67617. (PubMed:1379743)Curated
Sequence conflicti30 – 334DAPA → MTRQ(PubMed:6383820)Curated

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.
YP_491621.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76824; AAC76824; b3821.
BAE77480; BAE77480; BAE77480.
GeneIDi12930309.
948307.
KEGGiecj:Y75_p3357.
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 .
PIRi A22133. PSECA1.
RefSeqi NP_418265.1. NC_000913.3.
YP_491621.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P0A921.
SMRi P0A921. Positions 33-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A921. 12 interactions.
STRINGi 511145.b3821.

Proteomic databases

PaxDbi P0A921.
PRIDEi P0A921.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76824 ; AAC76824 ; b3821 .
BAE77480 ; BAE77480 ; BAE77480 .
GeneIDi 12930309.
948307.
KEGGi ecj:Y75_p3357.
eco:b3821.
PATRICi 32123143. VBIEscCol129921_3937.

Organism-specific databases

EchoBASEi EB0731.
EcoGenei EG10738. pldA.

Phylogenomic databases

eggNOGi COG2829.
HOGENOMi HOG000288150.
InParanoidi P0A921.
KOi K01058.
OMAi WNRVYAR.
OrthoDBi EOG6HQSN6.
PhylomeDBi P0A921.

Enzyme and pathway databases

BioCyci EcoCyc:MONOMER0-341.
ECOL316407:JW3794-MONOMER.
MetaCyc:MONOMER0-341.

Miscellaneous databases

EvolutionaryTracei P0A921.
PROi P0A921.

Gene expression databases

Genevestigatori P0A921.

Family and domain databases

Gene3Di 2.40.230.10. 1 hit.
InterProi IPR003187. PLipase_A1.
[Graphical view ]
Pfami PF02253. PLA1. 1 hit.
[Graphical view ]
PRINTSi PR01486. PHPHLIPASEA1.
SUPFAMi SSF56931. SSF56931. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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 26, 2014
This is version 78 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

External Data

Dasty 3