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Q8K987 (PPID_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:BUsg_462
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

PPIases accelerate the folding of proteins By similarity.

Catalytic activity

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

Subcellular location

Cell membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Contains 1 PpiC domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Peptidyl-prolyl cis-trans isomerase D
PRO_0000193421

Regions

Topological domain1 – 1010Cytoplasmic Potential
Transmembrane11 – 3121Helical; Potential
Topological domain32 – 621590Extracellular Potential
Domain228 – 355128PpiC

Sequences

Sequence LengthMass (Da)Tools
Q8K987 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 5B7A89B253144C7C

FASTA62174,140
        10         20         30         40         50         60 
MIKYLKSRLN IIIVKCILGI IILSLVFGTI NNYFNRDTTR YIAKVNGEEI SFITLQKMYI 

        70         80         90        100        110        120 
DERKKQEKIL GQDFEKIKKN KKFKEETYNY ILSQLINNIL LEQYTKRMNF NIQDNEIKKI 

       130        140        150        160        170        180 
IFNIPIFQEN NEFNKKKYLN YLSSKNLTHY EYVSLIRKKL NTTYLINAIS ETDFILDNEQ 

       190        200        210        220        230        240 
KKIIKLLSEK RIIKKAIIKI NPIINNQKVT EKEINNYFDQ HKNEFYTPEK FKISYIQLKP 

       250        260        270        280        290        300 
NKFKIQCSNE EIKNWYKKNI DKYSNQERRQ YSIIQTKTKN EALSILSELK KGEDFSKIAK 

       310        320        330        340        350        360 
EKSIDPFSSE QGGNIGWITK NFVPNEIKIA NLEKIDQISN IIKFNNNFLI IKLNKILPKK 

       370        380        390        400        410        420 
YKKISEVSDL IENEIKYQKS LNTYKKLKDK IAIIAKKNIN RFDLILKKTN ILPKETNWFD 

       430        440        450        460        470        480 
KDSVPKELQN PILKKIIFKK GLLDRQKKLK SHSGLIVLND HQSFLLSIKN FQKKRIKKLK 

       490        500        510        520        530        540 
DIKRNIVNKL KYIKAVEKTK NKLKKILFQL KIGNEHILKK ENIIFEEYET VSRYDKNPNI 

       550        560        570        580        590        600 
SVIFAMPHPK EEKNVYTMYQ NKNKNFVIAL LDKVYNEKFS NEEEKIIIKY LEKNNIDVTF 

       610        620 
QCFLQNLHRK ATILYNKTDN F 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM68005.1.
RefSeqNP_660794.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K987.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM68005; AAM68005; BUsg_462.
GeneID1005703.
KEGGbas:BUsg462.
PATRIC21247780. VBIBucAph100086_0489.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0760.
KOK03770.
OMANHEYINI.
OrthoDBEOG6M9DS4.
ProtClustDBCLSK315500.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-486-MONOMER.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF13145. Rotamase_2. 1 hit.
[Graphical view]
SUPFAMSSF109998. SSF109998. 2 hits.
PROSITEPS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPID_BUCAP
AccessionPrimary (citable) accession number: Q8K987
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 75 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names