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P0A9L5

- PPIC_ECOLI

UniProt

P0A9L5 - PPIC_ECOLI

Protein

Peptidyl-prolyl cis-trans isomerase C

Gene

ppiC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
    2. protein binding Source: EcoCyc

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. protein peptidyl-prolyl isomerization Source: GOC

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12352-MONOMER.
    ECOL316407:JW3748-MONOMER.
    MetaCyc:EG12352-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase C (EC:5.2.1.8)
    Short name:
    PPIase C
    Alternative name(s):
    Par10
    Parvulin
    Rotamase C
    Gene namesi
    Name:ppiC
    Synonyms:parVA
    Ordered Locus Names:b3775, JW3748
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12352. ppiC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 9392Peptidyl-prolyl cis-trans isomerase CPRO_0000193415Add
    BLAST

    Proteomic databases

    PaxDbiP0A9L5.
    PRIDEiP0A9L5.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9L5.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48081N.
    IntActiP0A9L5. 13 interactions.
    MINTiMINT-1225694.
    STRINGi511145.b3775.

    Structurei

    Secondary structure

    1
    93
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1411
    Helixi15 – 2713
    Helixi31 – 399
    Turni42 – 465
    Helixi47 – 493
    Beta strandi52 – 543
    Beta strandi55 – 584
    Helixi60 – 689
    Beta strandi71 – 733
    Beta strandi75 – 806
    Beta strandi83 – 908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JNSNMR-A2-93[»]
    1JNTNMR-A2-93[»]
    ProteinModelPortaliP0A9L5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9L5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 9190PpiCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PpiC/parvulin rotamase family.Curated
    Contains 1 PpiC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0760.
    HOGENOMiHOG000275329.
    KOiK03769.
    OMAiSCELLKP.
    OrthoDBiEOG690MCF.
    PhylomeDBiP0A9L5.

    Family and domain databases

    InterProiIPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    [Graphical view]
    PfamiPF00639. Rotamase. 1 hit.
    [Graphical view]
    PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A9L5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL   50
    GEFRQGQMVP AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN 93
    Length:93
    Mass (Da):10,232
    Last modified:January 23, 2007 - v2
    Checksum:i678A1BF2CBEA969B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S73874 Genomic DNA. Translation: AAB32054.1.
    M87049 Genomic DNA. Translation: AAA67578.1.
    U00096 Genomic DNA. Translation: AAC76780.1.
    AP009048 Genomic DNA. Translation: BAE77522.1.
    PIRiS48658.
    RefSeqiNP_418223.1. NC_000913.3.
    YP_491663.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76780; AAC76780; b3775.
    BAE77522; BAE77522; BAE77522.
    GeneIDi12934320.
    948285.
    KEGGiecj:Y75_p3400.
    eco:b3775.
    PATRICi32123045. VBIEscCol129921_3892.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S73874 Genomic DNA. Translation: AAB32054.1 .
    M87049 Genomic DNA. Translation: AAA67578.1 .
    U00096 Genomic DNA. Translation: AAC76780.1 .
    AP009048 Genomic DNA. Translation: BAE77522.1 .
    PIRi S48658.
    RefSeqi NP_418223.1. NC_000913.3.
    YP_491663.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JNS NMR - A 2-93 [» ]
    1JNT NMR - A 2-93 [» ]
    ProteinModelPortali P0A9L5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48081N.
    IntActi P0A9L5. 13 interactions.
    MINTi MINT-1225694.
    STRINGi 511145.b3775.

    Proteomic databases

    PaxDbi P0A9L5.
    PRIDEi P0A9L5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76780 ; AAC76780 ; b3775 .
    BAE77522 ; BAE77522 ; BAE77522 .
    GeneIDi 12934320.
    948285.
    KEGGi ecj:Y75_p3400.
    eco:b3775.
    PATRICi 32123045. VBIEscCol129921_3892.

    Organism-specific databases

    EchoBASEi EB2256.
    EcoGenei EG12352. ppiC.

    Phylogenomic databases

    eggNOGi COG0760.
    HOGENOMi HOG000275329.
    KOi K03769.
    OMAi SCELLKP.
    OrthoDBi EOG690MCF.
    PhylomeDBi P0A9L5.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12352-MONOMER.
    ECOL316407:JW3748-MONOMER.
    MetaCyc:EG12352-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9L5.
    PROi P0A9L5.

    Gene expression databases

    Genevestigatori P0A9L5.

    Family and domain databases

    InterProi IPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    [Graphical view ]
    Pfami PF00639. Rotamase. 1 hit.
    [Graphical view ]
    PROSITEi PS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin."
      Rahfeld J.-U., Ruecknagel K.P., Schelbert B., Ludwig B., Hacker J., Mann K., Fischer G.
      FEBS Lett. 352:180-184(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-93.
    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.
      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. "A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli."
      Rahfeld J.-U., Schierhorn A., Mann K., Fischer G.
      FEBS Lett. 343:65-69(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22, CHARACTERIZATION.
    6. "Conserved sequence motifs in bacterial and bacteriophage chaperonins."
      Rudd K.E., Sofia H.J., Koonin E.V., Plunkett G. III, Lazar S., Rouviere P.E.
      Trends Biochem. Sci. 20:14-15(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    7. "Solution structure of Escherichia coli Par10: the prototypic member of the parvulin family of peptidyl-prolyl cis/trans isomerases."
      Kuhlewein A., Voll G., Hernandez Alvarez B., Kessler H., Fischer G., Rahfeld J.-U., Gemmecker G.
      Protein Sci. 13:2378-2387(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiPPIC_ECOLI
    AccessioniPrimary (citable) accession number: P0A9L5
    Secondary accession number(s): P39159, Q2M884
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 76 of the entry and version 2 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