Reviewed, UniProtKB/Swiss-Prot Q06903 (PPCE_AERHY)

Names and origin

Protein names	Recommended name:     Prolyl endopeptidase       Short name=PE     EC=3.4.21.26 Alternative name(s):     Post-proline cleaving enzyme
Organism	Aeromonas hydrophila
Taxonomic identifier	644 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Molecular function	Hydrolase Protease Serine protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 690	689	Prolyl endopeptidase		PRO_0000122399
Sites
	Active site	538	1	Charge relay system By similarity
	Active site	657	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06903-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 854677C4AE753EB6	FASTA	690	76,515
	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

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: 8370677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: AK-9.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D14005 Genomic DNA. Translation: BAA03105.1.
PIR	JN0585.
3D structure databases
HSSP	HSSP built from PDB template 1O6G based on UniProtKB P23687.
ModBase	Search...
Protein family/group databases
MEROPS	S09.001.
Enzyme and pathway databases
BRENDA	3.4.21.26. 3060.
Family and domain databases
InterPro	IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR002470. Peptidase_S9A. IPR004106. Peptidase_S9A_N. [Graphical view]
PANTHER	PTHR11757. Peptidase_S9A. 1 hit.
Pfam	PF00326. Peptidase_S9. 1 hit. PF02897. Peptidase_S9_N. 1 hit. [Graphical view]
PRINTS	PR00862. PROLIGOPTASE.
PROSITE	PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPCE_AERHY

Accession

Primary (citable) accession number: Q06903

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 20, 2009
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)