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P23869 (PPIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase B

Short name=PPIase B
EC=5.2.1.8
Alternative name(s):
Rotamase B
Gene names
Name:ppiB
Ordered Locus Names:b0525, JW0514
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

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

Enzyme regulation

Inhibition by cyclosporin A with a Ki of 25 to 50 mu-mol, a concentration 100-fold higher than that required for eukaryotic PPIases.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from direct assay Ref.1. Source: GOC

   Cellular_componentcytosol

Inferred from direct assay Ref.1. Source: EcoCyc

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay Ref.1. Source: EcoCyc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rhsCP169184EBI-555935,EBI-546818

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptidyl-prolyl cis-trans isomerase B
PRO_0000064202

Regions

Domain1 – 162162PPIase cyclophilin-type

Experimental info

Sequence conflict1321V → E in AAA23453. Ref.1

Secondary structure

........................................ 164
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23869 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 4D5C7D2D8B02C810

FASTA16418,153
        10         20         30         40         50         60 
MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI QGGGFEPGMK 

        70         80         90        100        110        120 
QKATKEPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI NVVDNDFLNF SGESLQGWGY 

       130        140        150        160 
CVFAEVVDGM DVVDKIKGVA TGRSGMHQDV PKEDVIIESV TVSE 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55430 Genomic DNA. Translation: AAA23453.1.
U00096 Genomic DNA. Translation: AAC73627.1.
AP009048 Genomic DNA. Translation: BAE76302.1.
X59293 Genomic DNA. Translation: CAA41982.1.
PIRCSECB. D64784.
RefSeqNP_415058.1. NC_000913.3.
YP_488814.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LOPX-ray1.80A1-164[»]
2NULX-ray2.10A1-164[»]
2RS4NMR-A1-164[»]
ProteinModelPortalP23869.
SMRP23869. Positions 1-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10546N.
IntActP23869. 23 interactions.
MINTMINT-1289871.
STRING511145.b0525.

2D gel databases

SWISS-2DPAGEP23869.

Proteomic databases

PaxDbP23869.
PRIDEP23869.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73627; AAC73627; b0525.
BAE76302; BAE76302; BAE76302.
GeneID12933020.
949038.
KEGGecj:Y75_p0511.
eco:b0525.
PATRIC32116210. VBIEscCol129921_0546.

Organism-specific databases

EchoBASEEB0751.
EcoGeneEG10758. ppiB.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065978.
KOK03768.
OMAEDINICS.
OrthoDBEOG6S26C3.
PhylomeDBP23869.
ProtClustDBPRK10791.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP23869.

Family and domain databases

InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23869.
PROP23869.

Entry information

Entry namePPIB_ECOLI
AccessionPrimary (citable) accession number: P23869
Secondary accession number(s): P78052, Q2MBQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene