Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P27195

- PPCF_ELIMR

UniProt

P27195 - PPCF_ELIMR

Protein

Prolyl endopeptidase

Gene
N/A
Organism
Elizabethkingia miricola (Chryseobacterium miricola)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 systemPROSITE-ProRule annotation

    GO - Molecular functioni

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

    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

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 705685Prolyl endopeptidasePRO_0000027208Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP27195.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    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: October 1, 2014
    This is version 78 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