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P0AFL3

- PPIA_ECOLI

UniProt

P0AFL3 - PPIA_ECOLI

Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

ppiA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    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

    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

    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.
    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

    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 1, 2014
    This is version 73 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