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P27028

- PPCE_ELIME

UniProt

P27028 - PPCE_ELIME

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Protein

Prolyl endopeptidase

Gene
f1pep1
Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei556 – 5561Charge relay system1 Publication
Active sitei675 – 6751Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type exopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl endopeptidase (EC:3.4.21.26)
Alternative name(s):
Post-proline cleaving enzyme
Proline-specific endopeptidase
Short name:
PE
Short name:
PSE
Gene namesi
Name:f1pep1
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 705685Prolyl endopeptidasePRO_0000027207Add
BLAST

Proteomic databases

PRIDEiP27028.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP27028.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9A family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERiPTHR11757. PTHR11757. 1 hit.
PfamiPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSiPR00862. PROLIGOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27028-1 [UniParc]FASTAAdd to Basket

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MKYNKLSVAV AAFAFAAVSA QNSNVLKYPE TKKVSHTDTY FGTQVSDPYR    50
WLEDDRAEDT KAWVQQEVKF TQDYLAQIPF RDQLKKQLMD IWNYEKISAP 100
FKKGKYTYFS KNDGLQAQSV LYRKDAAGKT EVFLDPNKFS EKGTTSLASV 150
SFNKKGTLVA YSISEGGSDW NKIIILDAET KKQLDETLLD VKFSGISWLG 200
DEGFFYSSYD KPKEGSVLSG MTDKHKVYFH KLGTKQSQDE LIIGGDKFPR 250
RYIGAYVTDD QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFDSNVN 300
VADTDGDTLY LFTDKDAPNK RLVKTTIQNP KAETWKDVIA ETSEPLEINT 350
GGGYFFATYM KDAIDQVKQY DKNGKLVRAI KLPGSGNASG FGGEKTEKDL 400
YYSFTNYITP PTIFKYNVTT GNSEVYQKPK VKFNPENYVS EQVFYTSSDG 450
TKIPMMISYK KGLKKDGKNP TILYSYGGFN ISLQPAFSVV NAIWMENGGI 500
YAVPNIRGGG EYGKKWHDAG TKMQKKNVFN DFIAAGEYLQ KNGYTSKEYM 550
ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD 600
YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK 650
FGSELQAKQS CKNPILIRIE TNAGHGAGRS TEQVVAENAD LLSFALYEMG 700
IKSLK 705
Length:705
Mass (Da):78,707
Last modified:August 1, 1992 - v1
Checksum:iBC0EDCBABB328256
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101S → C AA sequence 1 Publication
Sequence conflicti587 – 5871R → A AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10980 Genomic DNA. Translation: BAA01755.1.
X63674 Genomic DNA. Translation: CAA45213.1.
PIRiJX0194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10980 Genomic DNA. Translation: BAA01755.1 .
X63674 Genomic DNA. Translation: CAA45213.1 .
PIRi JX0194.

3D structure databases

ProteinModelPortali P27028.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P27028.
ChEMBLi CHEMBL6043.

Proteomic databases

PRIDEi P27028.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view ]
PANTHERi PTHR11757. PTHR11757. 1 hit.
Pfami PF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view ]
PRINTSi PR00862. PROLIGOPTASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiPPCE_ELIME
AccessioniPrimary (citable) accession number: P27028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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