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Q06903 (PPCE_AERHY) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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

Short name=PE
EC=3.4.21.26
Alternative name(s):
Post-proline cleaving enzyme
OrganismAeromonas hydrophila
Taxonomic identifier644 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length690 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.

Sequence similarities

Belongs to the peptidase S9A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 690689Prolyl endopeptidase
PRO_0000122399

Sites

Active site5381Charge relay system By similarity
Active site6571Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06903 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 854677C4AE753EB6

FASTA69076,515
        10         20         30         40         50         60 
MSGKARLHYP VTRQSEQLDH YFGQAVADPY RWLEDDRSPE TEAWVKAQNR VTQDYLAQIP 

        70         80         90        100        110        120 
FRDAIKGKLA TSWNYAKEGA PFREGRYHYF FKNDGLQNQN VLCGQLAGKP AEVFLDPNLL 

       130        140        150        160        170        180 
SPDGTTALDQ LSFSRDGKTL AYSLSLAGSD WREIHLMDVE SKQPLETPLR DVKFSGISWL 

       190        200        210        220        230        240 
GNEGFFYSSY DKPDGSELSA RTDQHKLYFH RLGTAQEEDR LVFGAIPAQR HRYVGATVTE 

       250        260        270        280        290        300 
DDRYLLISAA DSTSGNRLYV KDLTREGAPL LTVQGDLAAD VSLVDNKGSR LYLLTNRDAP 

       310        320        330        340        350        360 
NRRLVTVEAD NPGPEQWRDL IPERQQVLTV HSGGGYLFAE YMVDATARVE QFDHDGKRVR 

       370        380        390        400        410        420 
EVGLPGLGSV SGFNGKQDDP ALYFGFENYA QPPTLYKFEP NSGAISLYRA SAAPFKPEDY 

       430        440        450        460        470        480 
VSEQRFYRSK DGTRVPLIIS YRKGLKLDGS NPTILYGYGG FDVSLTPSFS VSVANWLDLG 

       490        500        510        520        530        540 
GVYAVANLRG GGEYGQAWHL AGTRMNKQNV FDDFIAAAEY LKAEGYTRTD RLAIRGGSNG 

       550        560        570        580        590        600 
GLLVGAVMTQ RPDLMRVACQ AVGVLDMLRY HTFTAGAGWA YDYGTSADSE AMFDYLKGYS 

       610        620        630        640        650        660 
PLHSVRAGVS YPSTLVTTAD HDDRVVPAHS FKFAATLQAD DAGPHPQLIR IETNAGHGAG 

       670        680        690 
TPVAKLIEQS ADIYAFTLFE MGYRQLPRQP 

« Hide

References

[1]"Prolyl endopeptidase from Aeromonas hydrophila: cloning, sequencing, and expression of the enzyme gene, and characterization of the expressed enzyme."
Kanatani A., Yoshimoto T., Kitazono A., Kokubo T., Tsuru D.
J. Biochem. 113:790-796(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: AK-9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14005 Genomic DNA. Translation: BAA03105.1.
PIRJN0585.

3D structure databases

ProteinModelPortalQ06903.
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 namePPCE_AERHY
AccessionPrimary (citable) accession number: Q06903
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 69 of the entry and version 2 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