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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

ppiB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

  • peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc

GO - Biological processi

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10758. ppiB.

Subcellular locationi

GO - Cellular componenti

  • 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 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 – 65Combined sources
Beta strandi9 – 157Combined sources
Turni17 – 193Combined sources
Helixi21 – 3212Combined sources
Turni33 – 386Combined sources
Beta strandi43 – 453Combined sources
Turni46 – 483Combined sources
Beta strandi49 – 568Combined sources
Turni57 – 593Combined sources
Helixi72 – 743Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 963Combined sources
Beta strandi98 – 1036Combined sources
Helixi106 – 1083Combined sources
Beta strandi112 – 1143Combined sources
Turni115 – 1173Combined sources
Beta strandi122 – 1287Combined sources
Helixi130 – 1378Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi147 – 1537Combined sources
Beta strandi156 – 1627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP23869.
KOiK03768.
OMAiEDINICS.
OrthoDBiEOG6S26C3.
PhylomeDBiP23869.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
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

        10         20         30         40         50
MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI
60 70 80 90 100
QGGGFEPGMK QKATKEPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI
110 120 130 140 150
NVVDNDFLNF SGESLQGWGY CVFAEVVDGM DVVDKIKGVA TGRSGMHQDV
160
PKEDVIIESV TVSE
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC73627; AAC73627; b0525.
BAE76302; BAE76302; BAE76302.
GeneIDi949038.
KEGGiecj:Y75_p0511.
eco:b0525.
PATRICi32116210. VBIEscCol129921_0546.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

2D gel databases

SWISS-2DPAGEP23869.

Proteomic databases

PaxDbiP23869.
PRIDEiP23869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73627; AAC73627; b0525.
BAE76302; BAE76302; BAE76302.
GeneIDi949038.
KEGGiecj:Y75_p0511.
eco:b0525.
PATRICi32116210. VBIEscCol129921_0546.

Organism-specific databases

EchoBASEiEB0751.
EcoGeneiEG10758. ppiB.

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065978.
InParanoidiP23869.
KOiK03768.
OMAiEDINICS.
OrthoDBiEOG6S26C3.
PhylomeDBiP23869.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP23869.
PROiP23869.

Gene expression databases

GenevestigatoriP23869.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: May 27, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.