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P0A921

- PA1_ECOLI

UniProt

P0A921 - PA1_ECOLI

Protein

Phospholipase A1

Gene

pldA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    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

    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.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

    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.

    GO - Cellular componenti

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

    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 – 436
    Beta strandi52 – 543
    Beta strandi59 – 679
    Turni70 – 756
    Helixi77 – 815
    Beta strandi84 – 9916
    Turni100 – 1023
    Beta strandi106 – 11813
    Helixi123 – 1253
    Beta strandi129 – 14820
    Beta strandi151 – 16414
    Beta strandi169 – 1713
    Beta strandi174 – 18613
    Beta strandi189 – 20012
    Helixi208 – 2125
    Beta strandi214 – 22310
    Beta strandi226 – 2349
    Turni236 – 2383
    Beta strandi241 – 25212
    Beta strandi255 – 26511
    Helixi269 – 2713
    Beta strandi275 – 28511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 5232PeriplasmicAdd
    BLAST
    Topological domaini66 – 8419ExtracellularAdd
    BLAST
    Topological domaini100 – 1056Periplasmic
    Topological domaini119 – 12810Extracellular
    Topological domaini149 – 1502Periplasmic
    Topological domaini165 – 1739Extracellular
    Topological domaini187 – 1882Periplasmic
    Topological domaini199 – 21618ExtracellularAdd
    BLAST
    Topological domaini224 – 2252Periplasmic
    Topological domaini235 – 2417Extracellular
    Topological domaini251 – 2555Periplasmic
    Topological domaini266 – 2749Extracellular
    Topological domaini287 – 2893Periplasmic

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 6513Beta strandedAdd
    BLAST
    Transmembranei85 – 9915Beta strandedAdd
    BLAST
    Transmembranei106 – 11813Beta strandedAdd
    BLAST
    Transmembranei129 – 14820Beta strandedAdd
    BLAST
    Transmembranei151 – 16414Beta strandedAdd
    BLAST
    Transmembranei174 – 18613Beta strandedAdd
    BLAST
    Transmembranei189 – 19810Beta stranded
    Transmembranei217 – 2237Beta stranded
    Transmembranei226 – 2349Beta stranded
    Transmembranei242 – 2509Beta stranded
    Transmembranei256 – 26510Beta stranded
    Transmembranei275 – 28612Beta strandedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phospholipase A1 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane beta strand

    Phylogenomic databases

    eggNOGiCOG2829.
    HOGENOMiHOG000288150.
    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

    MRTLQGWLLP VFMLPMAVYA QEATVKEVHD APAVRGSIIA NMLQEHDNPF    50
    TLYPYDTNYL IYTQTSDLNK EAIASYDWAE NARKDEVKFQ LSLAFPLWRG 100
    ILGPNSVLGA SYTQKSWWQL SNSEESSPFR ETNYEPQLFL GFATDYRFAG 150
    WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT RLMAENGNWL VEVKPWYVVG 200
    NTDDNPDITK YMGYYQLKIG YHLGDAVLSA KGQYNWNTGY GGAELGLSYP 250
    ITKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDLF 289
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 76 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