Peptidyl-prolyl cis-trans isomerase B - Escherichia coli (strain K12)

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P23869 (PPIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 164

164

Peptidyl-prolyl cis-trans isomerase B

PRO_0000064202

Regions

Domain

1 – 162

162

PPIase cyclophilin-type

Experimental info

Sequence conflict

132

V → E in AAA23453. Ref.1

Secondary structure

164

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23869 [UniParc].

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

164

18,153

        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' referencesShow '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 277:1453-1474(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.

PIR

CSECB. D64784.

RefSeq

NP_415058.1. NC_000913.2.
YP_488814.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P23869.

SMR

P23869. Positions 1-164.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10546N.

IntAct

P23869. 23 interactions.

MINT

MINT-1289871.

STRING

511145.b0525.

2D gel databases

SWISS-2DPAGE

P23869.

Proteomic databases

PaxDb

P23869.

PRIDE

P23869.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73627; AAC73627; b0525.
BAE76302; BAE76302; BAE76302.

GeneID

12933020.
949038.

KEGG

ecj:Y75_p0511.
eco:b0525.

PATRIC

32116210. VBIEscCol129921_0546.

Organism-specific databases

EchoBASE

EB0751.

EcoGene

EG10758. ppiB.

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000065978.

K03768.

OMA

EDINICS.

ProtClustDB

PRK10791.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P23869.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23869.

Entry information

Entry name

PPIB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents