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Q0WAP4 (PEPQ_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:
Xaa-Pro dipeptidase

Short name=X-Pro dipeptidase
EC=3.4.13.9
Alternative name(s):
Imidodipeptidase
Proline dipeptidase
Short name=Prolidase
Gene names
Name:pepQ
Ordered Locus Names:YPO3765, y0465, YP_3283
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Splits dipeptides with a prolyl residue in the C-terminal position By similarity. HAMAP-Rule MF_01279

Catalytic activity

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. HAMAP-Rule MF_01279

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01279

Sequence similarities

Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.

Sequence caution

The sequence AAM84054.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS63450.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Xaa-Pro dipeptidase HAMAP-Rule MF_01279
PRO_0000303879

Sites

Metal binding2461Manganese 2 By similarity
Metal binding2571Manganese 1 By similarity
Metal binding2571Manganese 2 By similarity
Metal binding3391Manganese 1 By similarity
Metal binding3841Manganese 1 By similarity
Metal binding4231Manganese 1 By similarity
Metal binding4231Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0WAP4 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 63FD90A35262F27E

FASTA44350,912
        10         20         30         40         50         60 
METLASLYNE HLSTLQQRTR DVLERHQLDA LLIHSGELQR LFLDDRDYPF KVNPQFKAWV 

        70         80         90        100        110        120 
PVTEVPNCWL WVDGVNTPKL WFYSPVDYWH SVEPLPDSFW TKNIDVQPLL NADDIAQQLP 

       130        140        150        160        170        180 
VQRERVAYIG YAQQRAQALG FSAENINPQP VLDYLHYYRS YKTDYELACM REAQKTAVVG 

       190        200        210        220        230        240 
HRAAYEAFQS GMSEFDINLA YLMATGHRDT DVPYDNIVAL NEHSAVLHYT ILQHQPPAEI 

       250        260        270        280        290        300 
RSFLIDAGAE YNGYAADLTR TYTADRDSDF AALISDLNTE QLALIDTIKS GERYTDYHVQ 

       310        320        330        340        350        360 
MHQRIAKLLR THNLVTGISE EAMVEQGITC PFLPHGLGHP LGLQVHDTAG FMQDDKGTNL 

       370        380        390        400        410        420 
NAPSKYPYLR CTRVLQPRMV LTIEPGLYFI DSLLAPWRIG EFSKHFNWDR IDALKPYGGI 

       430        440 
RIEDNIVIHD KRVENMTRDL KLA 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL22352.1.
AE009952 Genomic DNA. Translation: AAM84054.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS63450.1. Different initiation.
PIRAE0458.
RefSeqNP_667803.1. NC_004088.1.
NP_994573.1. NC_005810.1.
YP_002348644.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ0WAP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ0WAP4. 3 interactions.
STRING214092.YPO3765.

Protein family/group databases

MEROPSM24.003.

Proteomic databases

PRIDEQ0WAP4.

Protocols and materials databases

DNASU1145412.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM84054; AAM84054; y0465.
AAS63450; AAS63450; YP_3283.
GeneID1145412.
1176600.
2764609.
KEGGype:YPO3765.
ypk:y0465.
ypm:YP_3283.

Phylogenomic databases

eggNOGCOG0006.
HOGENOMHOG000290531.
KOK01271.
OMAMQDDTGT.
OrthoDBEOG6XHC3N.
ProtClustDBPRK13607.

Enzyme and pathway databases

BioCycYPES214092:GKDD-3737-MONOMER.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
HAMAPMF_01279. X_Pro_dipeptid.
InterProIPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
IPR022846. X_Pro_dipept.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. SSF55920. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEPQ_YERPE
AccessionPrimary (citable) accession number: Q0WAP4
Secondary accession number(s): Q74R11, Q8D1H7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 63 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

Peptidase families

Classification of peptidase families and list of entries