ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P27195


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PPCF_ELIMR
Primary accession number P27195
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name Prolyl endopeptidase [Precursor]
Synonyms EC 3.4.21.26
Proline-specific endopeptidase
PSE
PE
Post-proline cleaving enzyme
Gene name None
From
Elizabethkingia miricola (Chryseobacterium miricola) [TaxID: 172045] 
Taxonomy Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales; Flavobacteriaceae; Elizabethkingia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 33958;
PubMed=1569074 [NCBI, ExPASy, EBI, Israel, Japan]
Chevallier S., Goeltz P., Thibault P., Banville D., Gagnon J.;
"Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine.";
J. Biol. Chem. 267:8192-8199(1992).
Comments
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
M81461; AAA24925.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P23687; 1O6G. [HSSP ENTRY / PDB]
ModBase P27195.
Protein family/group databases
MEROPS S09.001; -.
Ontologies
GO
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 P27195.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Hydrolase; Periplasm; Protease; Serine protease; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   705  685     Prolyl endopeptidase. PRO_0000027208
ACT_SITE   556   556        Charge relay system. 
ACT_SITE   675   675        Charge relay system (By similarity). 
Sequence information
Length: 705 AA [This is the length of the unprocessed precursor] Molecular weight: 78790 Da [This is the MW of the unprocessed precursor] CRC64: 36925D9A8783E03A [This is a checksum on the sequence]
        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 

P27195 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!