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P27195 (PPCF_ELIMR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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:
Prolyl endopeptidase

EC=3.4.21.26
Alternative name(s):
Post-proline cleaving enzyme
Proline-specific endopeptidase
Short name=PE
Short name=PSE
OrganismElizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifier172045 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond.

Catalytic activity

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the peptidase S9A family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 705685Prolyl endopeptidase
PRO_0000027208

Sites

Active site5561Charge relay system
Active site6751Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
P27195 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 36925D9A8783E03A

FASTA70578,790
        10         20         30         40         50         60 
MKYKKLSVAV AAFAFAAVSA QNSNSLKYPE TKKVNHTDTY FGNQVSDPYR WLEDDRAEDT 

        70         80         90        100        110        120 
KAWVQQEVKF TQDYLAQIPF RGQIKKQLLD IWNYEKISAP FKKGKYTYFY KNDGLQAQSV 

       130        140        150        160        170        180 
LYRKDASGKT EVFLDPNKFS DKGTTSLANL SFNKKGTLVA YSISEGGSDW NKIIILDAET 

       190        200        210        220        230        240 
KKQIDETLLD VKFSGISWLG DEGFFYSSYD KPKDGSVLSG MTDKHKVYFH KLGTKQSQDE 

       250        260        270        280        290        300 
LIIGGDKFPR RYLSGYVTED QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFESNVG 

       310        320        330        340        350        360 
LVDTDGDTLF LHTDKNAPNM RMVKTTIQNP KPETWKDVIA ETSEPMRVNS GGGYFFATYM 

       370        380        390        400        410        420 
KDALSQIKQY DKTGKLVREI KLPGSGTAGG FGGEKTEKEL YYSFTNYITP PTIFKFSIDS 

       430        440        450        460        470        480 
GKSEVYQKPK VKFNPENYVS EQVFYTSADG TKIPMMISNK KGLKKDGKNP TILYSYGGFN 

       490        500        510        520        530        540 
ISLQPAFSVV NAIWMENGGI YAVPNIRGGG EYGKKWHDAG TKQQKKNVFN DFIAAGEYLQ 

       550        560        570        580        590        600 
KNGYTSKDYM ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD 

       610        620        630        640        650        660 
YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK FGAELQAKQA 

       670        680        690        700 
CKNPVLIRIE TNAGHGAGRS TEQVVMENAD LLSFALYEMG IKNLK 

« Hide

References

[1]"Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine."
Chevallier S., Goeltz P., Thibault P., Banville D., Gagnon J.
J. Biol. Chem. 267:8192-8199(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 33958.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81461 Genomic DNA. Translation: AAA24925.1.

3D structure databases

ProteinModelPortalP27195.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERPTHR11757. PTHR11757. 1 hit.
PfamPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSPR00862. PROLIGOPTASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPCF_ELIMR
AccessionPrimary (citable) accession number: P27195
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 77 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