Skip Header

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

Peptidyl-prolyl cis-trans isomerase A

Gene

ppiA

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 catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibition by cyclosporin A with a Ki of 25 to 50 mu-mol, a concentration 100-fold higher than that required for eukaryotic PPIases.

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciEcoCyc:EG10757-MONOMER.
ECOL316407:JW3326-MONOMER.
MetaCyc:EG10757-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase A (EC:5.2.1.8)
Short name:
PPIase A
Alternative name(s):
Cyclophilin A
Rotamase A
Gene namesi
Name:ppiA
Synonyms:rot, rotA
Ordered Locus Names:b3363, JW3326
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10757. ppiA.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi136 – 1361F → W: Enhances susceptibility to CSA inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 190166Peptidyl-prolyl cis-trans isomerase APRO_0000025497Add
BLAST

Proteomic databases

PaxDbiP0AFL3.

2D gel databases

SWISS-2DPAGEP0AFL3.

Interactioni

Protein-protein interaction databases

DIPiDIP-48080N.
STRINGi511145.b3363.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 356Combined sources
Beta strandi38 – 447Combined sources
Turni46 – 483Combined sources
Helixi50 – 6112Combined sources
Turni62 – 676Combined sources
Beta strandi69 – 746Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 847Combined sources
Helixi101 – 1033Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi127 – 1326Combined sources
Helixi135 – 1373Combined sources
Beta strandi148 – 1547Combined sources
Helixi156 – 1638Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi173 – 1797Combined sources
Beta strandi182 – 1887Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLHNMR-A25-190[»]
1J2AX-ray1.80A25-190[»]
1V9TX-ray1.70A/B25-190[»]
1VAIX-ray1.80A/B25-190[»]
ProteinModelPortaliP0AFL3.
SMRiP0AFL3. Positions 25-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFL3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 188162PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated
Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065978.
InParanoidiP0AFL3.
KOiK03767.
OMAiTIKIELF.
OrthoDBiEOG6S26C3.
PhylomeDBiP0AFL3.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AFL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP
60 70 80 90 100
VSVQNFVDYV NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE
110 120 130 140 150
ADNGLRNTRG TIAMARTADK DSATSQFFIN VADNAFLDHG QRDFGYAVFG
160 170 180 190
KVVKGMDVAD KISQVPTHDV GPYQNVPSKP VVILSAKVLP
Length:190
Mass (Da):20,431
Last modified:December 20, 2005 - v1
Checksum:i8B48535F36AA61A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55429 Genomic DNA. Translation: AAA23451.1.
M28363 Genomic DNA. Translation: AAA23772.1.
U18997 Genomic DNA. Translation: AAA58160.1.
U00096 Genomic DNA. Translation: AAC76388.1.
AP009048 Genomic DNA. Translation: BAE77927.1.
M32354 Genomic DNA. Translation: AAA24261.1.
PIRiA37964. CSECA.
RefSeqiNP_417822.1. NC_000913.3.
WP_000477225.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76388; AAC76388; b3363.
BAE77927; BAE77927; BAE77927.
GeneIDi947870.
KEGGieco:b3363.
PATRICi32122160. VBIEscCol129921_3457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55429 Genomic DNA. Translation: AAA23451.1.
M28363 Genomic DNA. Translation: AAA23772.1.
U18997 Genomic DNA. Translation: AAA58160.1.
U00096 Genomic DNA. Translation: AAC76388.1.
AP009048 Genomic DNA. Translation: BAE77927.1.
M32354 Genomic DNA. Translation: AAA24261.1.
PIRiA37964. CSECA.
RefSeqiNP_417822.1. NC_000913.3.
WP_000477225.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLHNMR-A25-190[»]
1J2AX-ray1.80A25-190[»]
1V9TX-ray1.70A/B25-190[»]
1VAIX-ray1.80A/B25-190[»]
ProteinModelPortaliP0AFL3.
SMRiP0AFL3. Positions 25-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48080N.
STRINGi511145.b3363.

2D gel databases

SWISS-2DPAGEP0AFL3.

Proteomic databases

PaxDbiP0AFL3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76388; AAC76388; b3363.
BAE77927; BAE77927; BAE77927.
GeneIDi947870.
KEGGieco:b3363.
PATRICi32122160. VBIEscCol129921_3457.

Organism-specific databases

EchoBASEiEB0750.
EcoGeneiEG10757. ppiA.

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065978.
InParanoidiP0AFL3.
KOiK03767.
OMAiTIKIELF.
OrthoDBiEOG6S26C3.
PhylomeDBiP0AFL3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10757-MONOMER.
ECOL316407:JW3326-MONOMER.
MetaCyc:EG10757-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFL3.
PROiP0AFL3.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells."
    Hayano T., Takahashi N., Kato S., Maki N., Suzuki M.
    Biochemistry 30:3041-3048(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli."
    Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T.
    J. Bacteriol. 171:4525-4529(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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. "Chromosomal organization and expression of Escherichia coli pabA."
    Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.
    J. Bacteriol. 172:397-410(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-190.
  6. "Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A."
    Liu J., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 87:4028-4032(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, FUNCTION, PROTEIN SEQUENCE OF 25-36.
  7. "Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases."
    Compton L.A., Davis J.M., Macdonald J.R., Baechinger H.P.
    Eur. J. Biochem. 206:927-934(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue."
    Liu J., Chen C.-M., Walsh C.T.
    Biochemistry 30:2306-2310(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-136.
  9. "Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin."
    Clubb R.T., Ferguson S.B., Walsh C.T., Wagner G.
    Biochemistry 33:2761-2772(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin."
    Fejzo J., Etzkorn F.A., Clubb R.T., Shi Y., Walsh C.T., Wagner G.
    Biochemistry 33:5711-5720(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANT TRP-136.

Entry informationi

Entry nameiPPIA_ECOLI
AccessioniPrimary (citable) accession number: P0AFL3
Secondary accession number(s): P20752, Q2M729
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 22, 2015
This is version 81 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

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.