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

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P0AFL3 (PPIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. 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 A
Short name=PPIase A
EC=5.2.1.8

Alternative name(s):
Cyclophilin A
Rotamase A

Gene names

Name:	ppiA
Synonyms:	rot, rotA
Ordered Locus Names:	b3363, JW3326

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	190 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Ref.6
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	Periplasm.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
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	outer membrane-bounded periplasmic space Inferred from direct assay Ref.6. Source: EcoCyc
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Ref.6

Chain

25 – 190

166

Peptidyl-prolyl cis-trans isomerase A

PRO_0000025497

Regions

Domain

27 – 188

162

PPIase cyclophilin-type

Experimental info

Mutagenesis

136

F → W: Enhances susceptibility to CSA inhibition. Ref.8

Secondary structure

190

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AFL3 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 8B48535F36AA61A2
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FASTA

190

20,431

        10         20         30         40         50         60 
MFKSTLAAMA AVFALSALSP AAMAAKGDPH VLLTTSAGNI ELELDKQKAP VSVQNFVDYV 

        70         80         90        100        110        120 
NSGFYNNTTF HRVIPGFMIQ GGGFTEQMQQ KKPNPPIKNE ADNGLRNTRG TIAMARTADK 

       130        140        150        160        170        180 
DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPSKP 

       190 
VVILSAKVLP

« 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]	"Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cyclic AMP in Escherichia coli." Kawamukai M., Matsuda H., Fujii W., Utsumi R., Komano T. J. Bacteriol. 171:4525-4529(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
[4]	"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.
[5]	"Chromosomal organization and expression of Escherichia coli pabA." Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P. J. Bacteriol. 172:397-410(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-190.
[6]	"Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A." Liu J., Walsh C.T. Proc. Natl. Acad. Sci. U.S.A. 87:4028-4032(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, FUNCTION, PROTEIN SEQUENCE OF 25-36.
[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]	"Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue." Liu J., Chen C.-M., Walsh C.T. Biochemistry 30:2306-2310(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-136.
[9]	"Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin." Clubb R.T., Ferguson S.B., Walsh C.T., Wagner G. Biochemistry 33:2761-2772(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"The mutant Escherichia coli F112W cyclophilin binds cyclosporin A in nearly identical conformation as human cyclophilin." Fejzo J., Etzkorn F.A., Clubb R.T., Shi Y., Walsh C.T., Wagner G. Biochemistry 33:5711-5720(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF MUTANT TRP-136.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55429 Genomic DNA. Translation: AAA23451.1.
M28363 Genomic DNA. Translation: AAA23772.1.
U18997 Genomic DNA. Translation: AAA58160.1.
U00096 Genomic DNA. Translation: AAC76388.1.
AP009048 Genomic DNA. Translation: BAE77927.1.
M32354 Genomic DNA. Translation: AAA24261.1.

PIR

CSECA. A37964.

RefSeq

NP_417822.1. NC_000913.2.
YP_492068.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CLH	NMR	-	A	25-190	[»]
1J2A	X-ray	1.80	A	25-190	[»]
1V9T	X-ray	1.70	A/B	25-190	[»]
1VAI	X-ray	1.80	A/B	25-190	[»]

ProteinModelPortal

P0AFL3.

SMR

P0AFL3. Positions 25-190.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48080N.

STRING

511145.b3363.

2D gel databases

SWISS-2DPAGE

P0AFL3.

Proteomic databases

PaxDb

P0AFL3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76388; AAC76388; b3363.
BAE77927; BAE77927; BAE77927.

GeneID

12932091.
947870.

KEGG

ecj:Y75_p3812.
eco:b3363.

PATRIC

32122160. VBIEscCol129921_3457.

Organism-specific databases

EchoBASE

EB0750.

EcoGene

EG10757. ppiA.

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000065978.

K03767.

OMA

GMDVADQ.

ProtClustDB

PRK10903.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10757-MONOMER.
ECOL316407:JW3326-MONOMER.
MetaCyc:EG10757-MONOMER.

Gene expression databases

Genevestigator

P0AFL3.

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

P0AFL3.

Entry information

Entry name

PPIA_ECOLI

Accession

Primary (citable) accession number: P0AFL3
Secondary accession number(s): P20752, Q2M729

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 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