SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27195

- PPCF_ELIMR

UniProt

P27195 - PPCF_ELIMR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Prolyl endopeptidase
Gene
N/A
Organism
Elizabethkingia miricola (Chryseobacterium miricola)
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 system
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
OrganismiElizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifieri172045 [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 – 2020
Add
BLAST
Chaini21 – 705685Prolyl endopeptidase
PRO_0000027208Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP27195.

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.

P27195-1 [UniParc]FASTAAdd to Basket

« Hide

MKYKKLSVAV AAFAFAAVSA QNSNSLKYPE TKKVNHTDTY FGNQVSDPYR    50
WLEDDRAEDT KAWVQQEVKF TQDYLAQIPF RGQIKKQLLD IWNYEKISAP 100
FKKGKYTYFY KNDGLQAQSV LYRKDASGKT EVFLDPNKFS DKGTTSLANL 150
SFNKKGTLVA YSISEGGSDW NKIIILDAET KKQIDETLLD VKFSGISWLG 200
DEGFFYSSYD KPKDGSVLSG MTDKHKVYFH KLGTKQSQDE LIIGGDKFPR 250
RYLSGYVTED QRYLVVSAAN ATNGNELYIK DLKNKTDFIP IITGFESNVG 300
LVDTDGDTLF LHTDKNAPNM RMVKTTIQNP KPETWKDVIA ETSEPMRVNS 350
GGGYFFATYM KDALSQIKQY DKTGKLVREI KLPGSGTAGG FGGEKTEKEL 400
YYSFTNYITP PTIFKFSIDS GKSEVYQKPK VKFNPENYVS EQVFYTSADG 450
TKIPMMISNK KGLKKDGKNP TILYSYGGFN ISLQPAFSVV NAIWMENGGI 500
YAVPNIRGGG EYGKKWHDAG TKQQKKNVFN DFIAAGEYLQ KNGYTSKDYM 550
ALSGRSNGGL LVGATMTMRP DLAKVAFPGV GVLDMLRYNK FTAGAGWAYD 600
YGTAEDSKEM FEYLKSYSPV HNVKAGTCYP STMVITSDHD DRVVPAHSFK 650
FGAELQAKQA CKNPVLIRIE TNAGHGAGRS TEQVVMENAD LLSFALYEMG 700
IKNLK 705
Length:705
Mass (Da):78,790
Last modified:August 1, 1992 - v1
Checksum:i36925D9A8783E03A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81461 Genomic DNA. Translation: AAA24925.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81461 Genomic DNA. Translation: AAA24925.1 .

3D structure databases

ProteinModelPortali P27195.
ModBasei Search...
MobiDBi Search...

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. "Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine."
    Chevallier S., Goeltz P., Thibault P., Banville D., Gagnon J.
    J. Biol. Chem. 267:8192-8199(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 33958.

Entry informationi

Entry nameiPPCF_ELIMR
AccessioniPrimary (citable) accession number: P27195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 77 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

Similar proteinsi