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Protein

Peptidyl-prolyl cis-trans isomerase C

Gene

ppiC

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

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

GO - Biological processi

  1. protein peptidyl-prolyl isomerization Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciEcoCyc:EG12352-MONOMER.
ECOL316407:JW3748-MONOMER.
MetaCyc:EG12352-MONOMER.
BRENDAi5.2.1.8. 2026.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12352. ppiC.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 – 1411Combined sources
Helixi15 – 2713Combined sources
Helixi31 – 399Combined sources
Turni42 – 465Combined sources
Helixi47 – 493Combined sources
Beta strandi52 – 543Combined sources
Beta strandi55 – 584Combined sources
Helixi60 – 689Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 806Combined sources
Beta strandi83 – 908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNSNMR-A2-93[»]
1JNTNMR-A2-93[»]
SMRiP0A9L5. Positions 2-93.
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.
InParanoidiP0A9L5.
KOiK03769.
OMAiLAQKHST.
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

        10         20         30         40         50
MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL
60 70 80 90
GEFRQGQMVP AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN
Length:93
Mass (Da):10,232
Last modified:January 23, 2007 - v2
Checksum:i678A1BF2CBEA969B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNSNMR-A2-93[»]
1JNTNMR-A2-93[»]
SMRiP0A9L5. Positions 2-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A9L5.
PRIDEiP0A9L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB2256.
EcoGeneiEG12352. ppiC.

Phylogenomic databases

eggNOGiCOG0760.
HOGENOMiHOG000275329.
InParanoidiP0A9L5.
KOiK03769.
OMAiLAQKHST.
OrthoDBiEOG690MCF.
PhylomeDBiP0A9L5.

Enzyme and pathway databases

BioCyciEcoCyc:EG12352-MONOMER.
ECOL316407:JW3748-MONOMER.
MetaCyc:EG12352-MONOMER.
BRENDAi5.2.1.8. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A9L5.
PROiP0A9L5.

Gene expression databases

GenevestigatoriP0A9L5.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.