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P0AFL3

- PPIA_ECOLI

UniProt

P0AFL3 - PPIA_ECOLI

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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

ppiA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

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

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
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 PublicationAdd
BLAST
Chaini25 – 190166Peptidyl-prolyl cis-trans isomerase APRO_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

1
190
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.
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.
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

        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:
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.
InParanoidi P0AFL3.
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: October 29, 2014
This is version 74 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