NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1840588 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimoto T., Kanatani A., Shimoda T., Inaoka T., Kokubo T., Tsuru D.;
"Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene.";
J. Biochem. 110:873-878(1991).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1007/BF00170434; PubMed=7764331 [NCBI, ExPASy, EBI, Israel, Japan]
Diefenthal T., Dargatz H., Witte V., Reipen G., Svendsen I.;
"Cloning of proline-specific endopeptidase gene from Flavobacterium meningosepticum: expression in Escherichia coli and purification of the heterologous protein.";
Appl. Microbiol. Biotechnol. 40:90-97(1993).

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: Monomer.
SUBCELLULAR LOCATION: Periplasm.
SIMILARITY: Belongs to the peptidase S9A family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D10980; BAA01755.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X63674; CAA45213.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0194; JX0194.

3D structure databases

HSSP

P23687; 1O6G. [HSSP ENTRY / PDB]

ModBase

P27028.

Protein family/group databases

MEROPS

S09.001; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002470; Peptidase_S9A.
IPR004106; Peptidase_S9A_N.
Graphical view of domain structure.

PANTHER

PTHR11757; Peptidase_S9A; 1.

Pfam

PF00326; Peptidase_S9; 1.
PF02897; Peptidase_S9_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00862; PROLIGOPTASE.

PROSITE

PS00708; PRO_ENDOPEP_SER; 1.

ProtoNet

P27028.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Periplasm; Protease; Serine protease; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 705`	`685`	`Prolyl endopeptidase.`	`PRO_0000027207`
`ACT_SITE`	`556 556`		`Charge relay system.`
`ACT_SITE`	`675 675`		`Charge relay system (By similarity).`
`CONFLICT`	`110 110`		`S -> C (in Ref. 2; AA sequence).`
`CONFLICT`	`587 587`		`R -> A (in Ref. 2; AA sequence).`

Sequence information

Length: 705 AA [This is the length of the unprocessed precursor]

Molecular weight: 78707 Da [This is the MW of the unprocessed precursor]

CRC64: BC0EDCBABB328256 [This is a checksum on the sequence]

        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

P27028 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools