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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...

GO - Biological processi

    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 – 2020
    Add
    BLAST
    Chaini21 – 705685Prolyl endopeptidase
    PRO_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

    « Hide

    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...

    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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