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

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P0ADY1 (PPID_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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-562001,EBI-562001

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 623

623

Peptidyl-prolyl cis-trans isomerase D

PRO_0000193423

Regions

Topological domain

1 – 15

Cytoplasmic Potential

Transmembrane

16 – 36

Helical; Potential

Topological domain

37 – 623

587

Periplasmic Potential

Domain

266 – 355

PpiC

Experimental info

Mutagenesis

312

G → A or R: Loss of activity.

Mutagenesis

313

G → A or R: Loss of activity.

Mutagenesis

347

G → A: Loss of activity.

Mutagenesis

350

I → A or F: Loss of activity.

Secondary structure

623

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ADY1 [UniParc].

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

FASTA

623

68,150

        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' referencesShow '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 277:1453-1474(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]	"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.

PIR

A64774.

RefSeq

NP_414975.1. NC_000913.2.
YP_488733.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KGJ	NMR	-	A	264-357	[»]

ProteinModelPortal

P0ADY1.

SMR

P0ADY1. Positions 86-422.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39902N.

IntAct

P0ADY1. 8 interactions.

STRING

511145.b0441.

Proteomic databases

PaxDb

P0ADY1.

PRIDE

P0ADY1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73544; AAC73544; b0441.
BAE76221; BAE76221; BAE76221.

GeneID

12931738.
946056.

KEGG

ecj:Y75_p0429.
eco:b0441.

PATRIC

32116035. VBIEscCol129921_0459.

Organism-specific databases

EchoBASE

EB3038.

EcoGene

EG13249. ppiD.

Phylogenomic databases

eggNOG

COG0760.

HOGENOM

HOG000276975.

K03770.

OMA

QNIRDNS.

ProtClustDB

PRK10788.

Enzyme and pathway databases

BioCyc

EcoCyc:G6242-MONOMER.
ECOL316407:JW0431-MONOMER.

Gene expression databases

Genevestigator

P0ADY1.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]

Pfam

PF13145. Rotamase_2. 1 hit.
[Graphical view]

SUPFAM

SSF109998. Trigger_fac_C_bac. 1 hit.

PROSITE

PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ADY1.

Entry information

Entry name

PPID_ECOLI

Accession

Primary (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:	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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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