SubmitCancel

Skip Header

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

P0AFL3

- PPIA_ECOLI

UniProt

P0AFL3 - PPIA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Peptidyl-prolyl cis-trans isomerase A
Gene
ppiA, rot, rotA, b3363, JW3326
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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

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

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
  2. protein peptidyl-prolyl isomerization Source: GOC
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10757. ppiA.

Subcellular locationi

GO - Cellular componenti

  1. 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 Publication
Add
BLAST
Chaini25 – 190166Peptidyl-prolyl cis-trans isomerase A
PRO_0000025497Add
BLAST

Proteomic databases

PaxDbiP0AFL3.

2D gel databases

SWISS-2DPAGEP0AFL3.

Expressioni

Gene expression databases

GenevestigatoriP0AFL3.

Interactioni

Protein-protein interaction databases

DIPiDIP-48080N.
STRINGi511145.b3363.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0AFL3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 188162PPIase cyclophilin-type
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065978.
KOiK03767.
OMAiTTPIVIQ.
OrthoDBiEOG6S26C3.
PhylomeDBiP0AFL3.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
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

MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP    50
VSVQNFVDYV NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE 100
ADNGLRNTRG TIAMARTADK DSATSQFFIN VADNAFLDHG QRDFGYAVFG 150
KVVKGMDVAD KISQVPTHDV GPYQNVPSKP VVILSAKVLP 190
Length:190
Mass (Da):20,431
Last modified:December 20, 2005 - v1
Checksum:i8B48535F36AA61A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_492068.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76388; AAC76388; b3363.
BAE77927; BAE77927; BAE77927.
GeneIDi12932091.
947870.
KEGGiecj:Y75_p3812.
eco:b3363.
PATRICi32122160. VBIEscCol129921_3457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A37964. CSECA.
RefSeqi NP_417822.1. NC_000913.3.
YP_492068.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CLH NMR - A 25-190 [» ]
1J2A X-ray 1.80 A 25-190 [» ]
1V9T X-ray 1.70 A/B 25-190 [» ]
1VAI X-ray 1.80 A/B 25-190 [» ]
ProteinModelPortali P0AFL3.
SMRi P0AFL3. Positions 25-190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48080N.
STRINGi 511145.b3363.

2D gel databases

SWISS-2DPAGE P0AFL3.

Proteomic databases

PaxDbi P0AFL3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76388 ; AAC76388 ; b3363 .
BAE77927 ; BAE77927 ; BAE77927 .
GeneIDi 12932091.
947870.
KEGGi ecj:Y75_p3812.
eco:b3363.
PATRICi 32122160. VBIEscCol129921_3457.

Organism-specific databases

EchoBASEi EB0750.
EcoGenei EG10757. ppiA.

Phylogenomic databases

eggNOGi COG0652.
HOGENOMi HOG000065978.
KOi K03767.
OMAi TTPIVIQ.
OrthoDBi EOG6S26C3.
PhylomeDBi P0AFL3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10757-MONOMER.
ECOL316407:JW3326-MONOMER.
MetaCyc:EG10757-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AFL3.
PROi P0AFL3.

Gene expression databases

Genevestigatori P0AFL3.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 72 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