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P0AFL5 (PPIA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase A

Short name=PPIase A
EC=5.2.1.8
Alternative name(s):
Cyclophilin A
Rotamase A
Gene names
Name:ppiA
Ordered Locus Names:Z4724, ECs4214
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

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

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 190166Peptidyl-prolyl cis-trans isomerase A
PRO_0000045120

Regions

Domain27 – 188162PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
P0AFL5 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 8B48535F36AA61A2

FASTA19020,431
        10         20         30         40         50         60 
MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP VSVQNFVDYV 

        70         80         90        100        110        120 
NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE ADNGLRNTRG TIAMARTADK 

       130        140        150        160        170        180 
DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPSKP 

       190 
VVILSAKVLP 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58471.1.
BA000007 Genomic DNA. Translation: BAB37637.1.
PIRC86001.
F91155.
RefSeqNP_289911.1. NC_002655.2.
NP_312241.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0AFL5.
SMRP0AFL5. Positions 25-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58471; AAG58471; Z4724.
BAB37637; BAB37637; BAB37637.
GeneID915930.
961533.
KEGGece:Z4724.
ecs:ECs4214.
PATRIC18357976. VBIEscCol44059_4155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065978.
KOK03767.
OMAGYFADWP.
OrthoDBEOG6S26C3.
ProtClustDBPRK10903.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4184-MONOMER.
ECOO157:PPIA-MONOMER.

Family and domain databases

InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPIA_ECO57
AccessionPrimary (citable) accession number: P0AFL5
Secondary accession number(s): P20752
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families