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P0ADY1 (PPID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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 D

Short name=PPIase D
EC=5.2.1.8
Alternative name(s):
Rotamase D
Gene names
Name:ppiD
Synonyms:ybaU
Ordered Locus Names:b0441, JW0431
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr.

Catalytic activity

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

Subunit structure

Has been isolated as a homodimer and homotrimer from inner membrane preparations. Ref.6

Subcellular location

Cell inner membrane; Single-pass type II membrane protein; Periplasmic side Ref.6.

Induction

By heat shock.

Sequence similarities

Contains 1 PpiC domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-562001,EBI-562001

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623Peptidyl-prolyl cis-trans isomerase D
PRO_0000193423

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 623587Periplasmic Potential
Domain266 – 35590PpiC

Experimental info

Mutagenesis3121G → A or R: Loss of activity.
Mutagenesis3131G → A or R: Loss of activity.
Mutagenesis3471G → A: Loss of activity.
Mutagenesis3501I → A or F: Loss of activity.

Secondary structure

................ 623
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADY1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 0F646F687114A387

FASTA62368,150
        10         20         30         40         50         60 
MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI SRGQFENAFN 

        70         80         90        100        110        120 
SERNRMQQQL GDQYSELAAN EGYMKTLRQQ VLNRLIDEAL LDQYARELKL GISDEQVKQA 

       130        140        150        160        170        180 
IFATPAFQVD GKFDNSRYNG ILNQMGMTAD QYAQALRNQL TTQQLINGVA GTDFMLKGET 

       190        200        210        220        230        240 
DELAALVAQQ RVVREATIDV NALAAKQPVT EQEIASYYEQ NKNNFMTPEQ FRVSYIKLDA 

       250        260        270        280        290        300 
ATMQQPVSDA DIQSYYDQHQ DQFTQPQRTR YSIIQTKTED EAKAVLDELN KGGDFAALAK 

       310        320        330        340        350        360 
EKSADIISAR NGGDMGWLED ATIPDELKNA GLKEKGQLSG VIKSSVGFLI VRLDDIQPAK 

       370        380        390        400        410        420 
VKSLDEVRDD IAAKVKHEKA LDAYYALQQK VSDAASNDTE SLAGAEQAAG VKATQTGWFS 

       430        440        450        460        470        480 
KDNLPEELNF KPVADAIFNG GLVGENGAPG INSDIITVDG DRAFVLRISE HKPEAVKPLA 

       490        500        510        520        530        540 
DVQEQVKALV QHNKAEQQAK VDAEKLLVDL KAGKGAEAMQ AAGLKFGEPK TLSRSGRDPI 

       550        560        570        580        590        600 
SQAAFALPLP AKDKPSYGMA TDMQGNVVLL ALDEVKQGSM PEDQKKAMVQ GITQNNAQIV 

       610        620 
FEALMSNLRK EAKIKIGDAL EQQ 

« Hide

References

« Hide 'large scale' references
[1]Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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 277:1453-1462(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]"A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli."
Dartigalongue C., Raina S.
EMBO J. 17:3968-3980(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS.
[6]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D82943 Genomic DNA. Translation: BAA11645.1.
U82664 Genomic DNA. Translation: AAB40197.1.
U00096 Genomic DNA. Translation: AAC73544.1.
AP009048 Genomic DNA. Translation: BAE76221.1.
PIRA64774.
RefSeqNP_414975.1. NC_000913.3.
YP_488733.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KGJNMR-A264-357[»]
ProteinModelPortalP0ADY1.
SMRP0ADY1. Positions 86-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-39902N.
IntActP0ADY1. 8 interactions.
STRING511145.b0441.

Proteomic databases

PaxDbP0ADY1.
PRIDEP0ADY1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73544; AAC73544; b0441.
BAE76221; BAE76221; BAE76221.
GeneID12931738.
946056.
KEGGecj:Y75_p0429.
eco:b0441.
PATRIC32116035. VBIEscCol129921_0459.

Organism-specific databases

EchoBASEEB3038.
EcoGeneEG13249. ppiD.

Phylogenomic databases

eggNOGCOG0760.
HOGENOMHOG000276975.
KOK03770.
OMAQNIRDNS.
OrthoDBEOG6M9DS4.
PhylomeDBP0ADY1.
ProtClustDBPRK10788.

Enzyme and pathway databases

BioCycEcoCyc:G6242-MONOMER.
ECOL316407:JW0431-MONOMER.

Gene expression databases

GenevestigatorP0ADY1.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF13145. Rotamase_2. 1 hit.
[Graphical view]
SUPFAMSSF109998. SSF109998. 2 hits.
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADY1.
PROP0ADY1.

Entry information

Entry namePPID_ECOLI
AccessionPrimary (citable) accession number: P0ADY1
Secondary accession number(s): P77241, Q2MBY5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 71 of the entry and version 1 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