Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AFL3 (PPIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:rot, rotA
Ordered Locus Names:b3363, JW3326
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Ref.6

Catalytic activity

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

Enzyme regulation

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

Subcellular location

Periplasm.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.6
Chain25 – 190166Peptidyl-prolyl cis-trans isomerase A
PRO_0000025497

Regions

Domain27 – 188162PPIase cyclophilin-type

Experimental info

Mutagenesis1361F → W: Enhances susceptibility to CSA inhibition. Ref.8

Secondary structure

.................................. 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AFL3 [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

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRCSECA. A37964.
RefSeqNP_417822.1. NC_000913.3.
YP_492068.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLHNMR-A25-190[»]
1J2AX-ray1.80A25-190[»]
1V9TX-ray1.70A/B25-190[»]
1VAIX-ray1.80A/B25-190[»]
ProteinModelPortalP0AFL3.
SMRP0AFL3. Positions 25-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48080N.
STRING511145.b3363.

2D gel databases

SWISS-2DPAGEP0AFL3.

Proteomic databases

PaxDbP0AFL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76388; AAC76388; b3363.
BAE77927; BAE77927; BAE77927.
GeneID12932091.
947870.
KEGGecj:Y75_p3812.
eco:b3363.
PATRIC32122160. VBIEscCol129921_3457.

Organism-specific databases

EchoBASEEB0750.
EcoGeneEG10757. ppiA.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065978.
KOK03767.
OMAGYFADWP.
OrthoDBEOG6S26C3.
PhylomeDBP0AFL3.
ProtClustDBPRK10903.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0AFL3.

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...

Other

EvolutionaryTraceP0AFL3.
PROP0AFL3.

Entry information

Entry namePPIA_ECOLI
AccessionPrimary (citable) accession number: P0AFL3
Secondary accession number(s): P20752, Q2M729
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 70 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene