Reviewed, UniProtKB/Swiss-Prot P27028 (PPCE_FLAME)

Names and origin

Protein names

Recommended name:
    Prolyl endopeptidase
    EC=3.4.21.26
Alternative name(s):
    Proline-specific endopeptidase
      Short name=PSE
      Short name=PE
    Post-proline cleaving enzyme

Gene names

Name:

f1pep1

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	705 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.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the peptidase S9A family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 20	20
	Chain	21 – 705	685	Prolyl endopeptidase		PRO_0000027207
Sites
	Active site	556	1	Charge relay system Ref.1
	Active site	675	1	Charge relay system By similarity
Experimental info
	Sequence conflict	110	1	S → C AA sequence Ref.2
	Sequence conflict	587	1	R → A AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P27028-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: BC0EDCBABB328256	FASTA	705	78,707
	10 20 30 40 50 60 MKYNKLSVAV AAFAFAAVSA QNSNVLKYPE TKKVSHTDTY FGTQVSDPYR WLEDDRAEDT 70 80 90 100 110 120 KAWVQQEVKF TQDYLAQIPF RDQLKKQLMD IWNYEKISAP FKKGKYTYFS KNDGLQAQSV 130 140 150 160 170 180 LYRKDAAGKT EVFLDPNKFS EKGTTSLASV SFNKKGTLVA YSISEGGSDW NKIIILDAET 190 200 210 220 230 240 KKQLDETLLD VKFSGISWLG DEGFFYSSYD KPKEGSVLSG MTDKHKVYFH KLGTKQSQDE 250 260 270 280 290 300 LIIGGDKFPR RYIGAYVTDD QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFDSNVN 310 320 330 340 350 360 VADTDGDTLY LFTDKDAPNK RLVKTTIQNP KAETWKDVIA ETSEPLEINT GGGYFFATYM 370 380 390 400 410 420 KDAIDQVKQY DKNGKLVRAI KLPGSGNASG FGGEKTEKDL YYSFTNYITP PTIFKYNVTT 430 440 450 460 470 480 GNSEVYQKPK VKFNPENYVS EQVFYTSSDG TKIPMMISYK KGLKKDGKNP TILYSYGGFN 490 500 510 520 530 540 ISLQPAFSVV NAIWMENGGI YAVPNIRGGG EYGKKWHDAG TKMQKKNVFN DFIAAGEYLQ 550 560 570 580 590 600 KNGYTSKEYM ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD 610 620 630 640 650 660 YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK FGSELQAKQS 670 680 690 700 CKNPILIRIE TNAGHGAGRS TEQVVAENAD LLSFALYEMG IKSLK

References

[1]	"Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene." Yoshimoto T., Kanatani A., Shimoda T., Inaoka T., Kokubo T., Tsuru D. J. Biochem. 110:873-878(1991) [PubMed: 1840588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Cloning of proline-specific endopeptidase gene from Flavobacterium meningosepticum: expression in Escherichia coli and purification of the heterologous protein." Diefenthal T., Dargatz H., Witte V., Reipen G., Svendsen I. Appl. Microbiol. Biotechnol. 40:90-97(1993) [PubMed: 7764331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10980 Genomic DNA. Translation: BAA01755.1. X63674 Genomic DNA. Translation: CAA45213.1.
PIR	JX0194.
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. 39124.
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_FLAME

Accession

Primary (citable) accession number: P27028

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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