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P0ADY1

- PPID_ECOLI

UniProt

P0ADY1 - PPID_ECOLI

Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

ppiD

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 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr.

    Catalytic activityi

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciEcoCyc:G6242-MONOMER.
    ECOL316407:JW0431-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase D (EC:5.2.1.8)
    Short name:
    PPIase D
    Alternative name(s):
    Rotamase D
    Gene namesi
    Name:ppiD
    Synonyms:ybaU
    Ordered Locus Names:b0441, JW0431
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13249. ppiD.

    Subcellular locationi

    Cell inner membrane 1 Publication; Single-pass type II membrane protein 1 Publication; Periplasmic side 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi312 – 3121G → A or R: Loss of activity. 1 Publication
    Mutagenesisi313 – 3131G → A or R: Loss of activity. 1 Publication
    Mutagenesisi347 – 3471G → A: Loss of activity. 1 Publication
    Mutagenesisi350 – 3501I → A or F: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 623623Peptidyl-prolyl cis-trans isomerase DPRO_0000193423Add
    BLAST

    Proteomic databases

    PaxDbiP0ADY1.
    PRIDEiP0ADY1.

    Expressioni

    Inductioni

    By heat shock.

    Gene expression databases

    GenevestigatoriP0ADY1.

    Interactioni

    Subunit structurei

    Has been isolated as a homodimer and homotrimer from inner membrane preparations.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-562001,EBI-562001

    Protein-protein interaction databases

    DIPiDIP-39902N.
    IntActiP0ADY1. 8 interactions.
    STRINGi511145.b0441.

    Structurei

    Secondary structure

    1
    623
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi268 – 27811
    Helixi279 – 29113
    Helixi295 – 3017
    Helixi306 – 3094
    Turni310 – 3123
    Beta strandi313 – 3197
    Helixi325 – 3284
    Beta strandi338 – 3447
    Beta strandi347 – 35711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KGJNMR-A264-357[»]
    ProteinModelPortaliP0ADY1.
    SMRiP0ADY1. Positions 86-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADY1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini37 – 623587PeriplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini266 – 35590PpiCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PpiC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0760.
    HOGENOMiHOG000276975.
    KOiK03770.
    OMAiQNIRDNS.
    OrthoDBiEOG6M9DS4.
    PhylomeDBiP0ADY1.

    Family and domain databases

    InterProiIPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    IPR027304. Trigger_fact/SurA_dom.
    [Graphical view]
    PfamiPF13145. Rotamase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF109998. SSF109998. 2 hits.
    PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ADY1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI    50
    SRGQFENAFN SERNRMQQQL GDQYSELAAN EGYMKTLRQQ VLNRLIDEAL 100
    LDQYARELKL GISDEQVKQA IFATPAFQVD GKFDNSRYNG ILNQMGMTAD 150
    QYAQALRNQL TTQQLINGVA GTDFMLKGET DELAALVAQQ RVVREATIDV 200
    NALAAKQPVT EQEIASYYEQ NKNNFMTPEQ FRVSYIKLDA ATMQQPVSDA 250
    DIQSYYDQHQ DQFTQPQRTR YSIIQTKTED EAKAVLDELN KGGDFAALAK 300
    EKSADIISAR NGGDMGWLED ATIPDELKNA GLKEKGQLSG VIKSSVGFLI 350
    VRLDDIQPAK VKSLDEVRDD IAAKVKHEKA LDAYYALQQK VSDAASNDTE 400
    SLAGAEQAAG VKATQTGWFS KDNLPEELNF KPVADAIFNG GLVGENGAPG 450
    INSDIITVDG DRAFVLRISE HKPEAVKPLA DVQEQVKALV QHNKAEQQAK 500
    VDAEKLLVDL KAGKGAEAMQ AAGLKFGEPK TLSRSGRDPI SQAAFALPLP 550
    AKDKPSYGMA TDMQGNVVLL ALDEVKQGSM PEDQKKAMVQ GITQNNAQIV 600
    FEALMSNLRK EAKIKIGDAL EQQ 623
    Length:623
    Mass (Da):68,150
    Last modified:December 6, 2005 - v1
    Checksum:i0F646F687114A387
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82943 Genomic DNA. Translation: BAA11645.1.
    U82664 Genomic DNA. Translation: AAB40197.1.
    U00096 Genomic DNA. Translation: AAC73544.1.
    AP009048 Genomic DNA. Translation: BAE76221.1.
    PIRiA64774.
    RefSeqiNP_414975.1. NC_000913.3.
    YP_488733.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73544; AAC73544; b0441.
    BAE76221; BAE76221; BAE76221.
    GeneIDi12931738.
    946056.
    KEGGiecj:Y75_p0429.
    eco:b0441.
    PATRICi32116035. VBIEscCol129921_0459.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82943 Genomic DNA. Translation: BAA11645.1 .
    U82664 Genomic DNA. Translation: AAB40197.1 .
    U00096 Genomic DNA. Translation: AAC73544.1 .
    AP009048 Genomic DNA. Translation: BAE76221.1 .
    PIRi A64774.
    RefSeqi NP_414975.1. NC_000913.3.
    YP_488733.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KGJ NMR - A 264-357 [» ]
    ProteinModelPortali P0ADY1.
    SMRi P0ADY1. Positions 86-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-39902N.
    IntActi P0ADY1. 8 interactions.
    STRINGi 511145.b0441.

    Proteomic databases

    PaxDbi P0ADY1.
    PRIDEi P0ADY1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73544 ; AAC73544 ; b0441 .
    BAE76221 ; BAE76221 ; BAE76221 .
    GeneIDi 12931738.
    946056.
    KEGGi ecj:Y75_p0429.
    eco:b0441.
    PATRICi 32116035. VBIEscCol129921_0459.

    Organism-specific databases

    EchoBASEi EB3038.
    EcoGenei EG13249. ppiD.

    Phylogenomic databases

    eggNOGi COG0760.
    HOGENOMi HOG000276975.
    KOi K03770.
    OMAi QNIRDNS.
    OrthoDBi EOG6M9DS4.
    PhylomeDBi P0ADY1.

    Enzyme and pathway databases

    BioCyci EcoCyc:G6242-MONOMER.
    ECOL316407:JW0431-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ADY1.
    PROi P0ADY1.

    Gene expression databases

    Genevestigatori P0ADY1.

    Family and domain databases

    InterProi IPR000297. PPIase_PpiC.
    IPR023058. PPIase_PpiC_CS.
    IPR027304. Trigger_fact/SurA_dom.
    [Graphical view ]
    Pfami PF13145. Rotamase_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109998. SSF109998. 2 hits.
    PROSITEi PS01096. PPIC_PPIASE_1. 1 hit.
    PS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli."
      Dartigalongue C., Raina S.
      EMBO J. 17:3968-3980(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS.
    6. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.

    Entry informationi

    Entry nameiPPID_ECOLI
    AccessioniPrimary (citable) accession number: P0ADY1
    Secondary accession number(s): P77241, Q2MBY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 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, 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