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P23869

- PPIB_ECOLI

UniProt

P23869 - PPIB_ECOLI

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Protein
Peptidyl-prolyl cis-trans isomerase B
Gene
ppiB, b0525, JW0514
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.

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

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.

Miscellaneous databases

EvolutionaryTraceiP23869.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 162162PPIase cyclophilin-type
Add
BLAST

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321V → E in AAA23453. 1 Publication

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

« 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. 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: June 11, 2014
This is version 124 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

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