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P23869

- PPIB_ECOLI

UniProt

P23869 - PPIB_ECOLI

Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

ppiB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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.

    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
    2. protein binding Source: IntAct

    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:EG10758-MONOMER.
    ECOL316407:JW0514-MONOMER.
    MetaCyc:EG10758-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
    Short name:
    PPIase B
    Alternative name(s):
    Rotamase B
    Gene namesi
    Name:ppiB
    Ordered Locus Names:b0525, JW0514
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10758. ppiB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164Peptidyl-prolyl cis-trans isomerase BPRO_0000064202Add
    BLAST

    Proteomic databases

    PaxDbiP23869.
    PRIDEiP23869.

    2D gel databases

    SWISS-2DPAGEP23869.

    Expressioni

    Gene expression databases

    GenevestigatoriP23869.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rhsCP169184EBI-555935,EBI-546818

    Protein-protein interaction databases

    DIPiDIP-10546N.
    IntActiP23869. 23 interactions.
    MINTiMINT-1289871.
    STRINGi511145.b0525.

    Structurei

    Secondary structure

    1
    164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Beta strandi9 – 157
    Turni17 – 193
    Helixi21 – 3212
    Turni33 – 386
    Beta strandi43 – 453
    Turni46 – 483
    Beta strandi49 – 568
    Turni57 – 593
    Helixi72 – 743
    Beta strandi82 – 854
    Beta strandi88 – 903
    Beta strandi94 – 963
    Beta strandi98 – 1036
    Helixi106 – 1083
    Beta strandi112 – 1143
    Turni115 – 1173
    Beta strandi122 – 1287
    Helixi130 – 1378
    Beta strandi141 – 1444
    Beta strandi147 – 1537
    Beta strandi156 – 1627

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LOPX-ray1.80A1-164[»]
    2NULX-ray2.10A1-164[»]
    2RS4NMR-A1-164[»]
    ProteinModelPortaliP23869.
    SMRiP23869. Positions 1-164.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23869.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 162162PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.Curated
    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065978.
    KOiK03768.
    OMAiEDINICS.
    OrthoDBiEOG6S26C3.
    PhylomeDBiP23869.

    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.

    P23869-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI    50
    QGGGFEPGMK QKATKEPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI 100
    NVVDNDFLNF SGESLQGWGY CVFAEVVDGM DVVDKIKGVA TGRSGMHQDV 150
    PKEDVIIESV TVSE 164
    Length:164
    Mass (Da):18,153
    Last modified:November 1, 1997 - v2
    Checksum:i4D5C7D2D8B02C810
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321V → E in AAA23453. (PubMed:2007139)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55430 Genomic DNA. Translation: AAA23453.1.
    U00096 Genomic DNA. Translation: AAC73627.1.
    AP009048 Genomic DNA. Translation: BAE76302.1.
    X59293 Genomic DNA. Translation: CAA41982.1.
    PIRiD64784. CSECB.
    RefSeqiNP_415058.1. NC_000913.3.
    YP_488814.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73627; AAC73627; b0525.
    BAE76302; BAE76302; BAE76302.
    GeneIDi12933020.
    949038.
    KEGGiecj:Y75_p0511.
    eco:b0525.
    PATRICi32116210. VBIEscCol129921_0546.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55430 Genomic DNA. Translation: AAA23453.1 .
    U00096 Genomic DNA. Translation: AAC73627.1 .
    AP009048 Genomic DNA. Translation: BAE76302.1 .
    X59293 Genomic DNA. Translation: CAA41982.1 .
    PIRi D64784. CSECB.
    RefSeqi NP_415058.1. NC_000913.3.
    YP_488814.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LOP X-ray 1.80 A 1-164 [» ]
    2NUL X-ray 2.10 A 1-164 [» ]
    2RS4 NMR - A 1-164 [» ]
    ProteinModelPortali P23869.
    SMRi P23869. Positions 1-164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10546N.
    IntActi P23869. 23 interactions.
    MINTi MINT-1289871.
    STRINGi 511145.b0525.

    2D gel databases

    SWISS-2DPAGE P23869.

    Proteomic databases

    PaxDbi P23869.
    PRIDEi P23869.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73627 ; AAC73627 ; b0525 .
    BAE76302 ; BAE76302 ; BAE76302 .
    GeneIDi 12933020.
    949038.
    KEGGi ecj:Y75_p0511.
    eco:b0525.
    PATRICi 32116210. VBIEscCol129921_0546.

    Organism-specific databases

    EchoBASEi EB0751.
    EcoGenei EG10758. ppiB.

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065978.
    KOi K03768.
    OMAi EDINICS.
    OrthoDBi EOG6S26C3.
    PhylomeDBi P23869.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10758-MONOMER.
    ECOL316407:JW0514-MONOMER.
    MetaCyc:EG10758-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P23869.
    PROi P23869.

    Gene expression databases

    Genevestigatori P23869.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Cysteinyl-tRNA synthetase is a direct descendant of the first aminoacyl-tRNA synthetase."
      Avalos J., Corrochano L.M., Brenner S.
      FEBS Lett. 286:176-180(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
      Strain: K12.
    5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    6. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "The substrate-binding site in Escherichia coli cyclophilin A preferably recognizes a cis-proline isomer or a highly distorted form of the trans isomer."
      Konno M., Ito M., Hayano T., Takahashi N.
      J. Mol. Biol. 256:897-908(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiPPIB_ECOLI
    AccessioniPrimary (citable) accession number: P23869
    Secondary accession number(s): P78052, Q2MBQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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