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P29068

- CBPT_THEVU

UniProt

P29068 - CBPT_THEVU

Protein

Carboxypeptidase T

Gene

cpt

Organism
Thermoactinomyces vulgaris
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Able to split off hydrophobic and basic amino acids with comparable efficiency.

    Catalytic activityi

    Releases a C-terminal residue, which may be hydrophobic or positively charged.

    Cofactori

    Binds 1 zinc ion per subunit.

    Enzyme regulationi

    Binds four calcium ions which seem to play an important role in the thermostability of the enzyme.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi167 – 1671Zinc
    Metal bindingi170 – 1701Zinc
    Metal bindingi302 – 3021Zinc
    Active sitei353 – 3531Proton donor
    Active sitei375 – 3751Nucleophile

    GO - Molecular functioni

    1. metallocarboxypeptidase activity Source: InterPro
    2. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM14.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase T (EC:3.4.17.18)
    Gene namesi
    Name:cpt
    OrganismiThermoactinomyces vulgaris
    Taxonomic identifieri2026 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 9875Activation peptide1 PublicationPRO_0000004415Add
    BLAST
    Chaini99 – 424326Carboxypeptidase TPRO_0000004416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi253 ↔ 254
    Disulfide bondi412 ↔ 421

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi102 – 1043
    Helixi110 – 12314
    Turni125 – 1273
    Beta strandi128 – 1358
    Beta strandi141 – 1488
    Turni149 – 1524
    Beta strandi159 – 1646
    Helixi172 – 18615
    Turni187 – 1904
    Helixi192 – 2009
    Beta strandi202 – 2065
    Helixi211 – 2188
    Helixi243 – 2453
    Turni249 – 2524
    Beta strandi254 – 2607
    Helixi275 – 28612
    Beta strandi290 – 2934
    Beta strandi295 – 3028
    Beta strandi304 – 3118
    Helixi325 – 34218
    Beta strandi345 – 3484
    Helixi349 – 3513
    Helixi359 – 3679
    Beta strandi370 – 3756
    Turni381 – 3855
    Helixi389 – 3913
    Helixi392 – 3976
    Helixi400 – 40910
    Helixi413 – 4164

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OBRX-ray2.30A99-424[»]
    3PRTX-ray1.66A99-421[»]
    3QNVX-ray1.69A99-421[»]
    3V38X-ray1.50A99-424[»]
    3V7ZX-ray1.61A99-424[»]
    4DJLX-ray1.55A99-421[»]
    4DUKX-ray1.57A99-424[»]
    4F8ZX-ray1.38A99-421[»]
    4GM5X-ray1.39A99-421[»]
    4IAVX-ray1.35A99-424[»]
    4IHMX-ray1.29A99-424[»]
    4IK2X-ray1.40A99-424[»]
    ProteinModelPortaliP29068.
    SMRiP29068. Positions 99-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29068.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29068-1 [UniParc]FASTAAdd to Basket

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    MRKKWLSLSL VLVLIVACVP ALGFSQNIEN PSIFDLGIKL YKIDGVSTKE    50
    QRSAIASTGA AIEEVGKDYV KVLATPSEAK QIKQKGFTAT VDTSLTTQDF 100
    PSYDSGYHNY NEMVNKINTV ASNYPNIVKK FSIGKSYEGR ELWAVKISDN 150
    VGTDENEPEV LYTALHHARE HLTVEMALYT LDLFTQNYNL DSRITNLVNN 200
    REIYIVFNIN PDGGEYDISS GSYKSWRKNR QPNSGSSYVG TDLNRNYGYK 250
    WGCCGGSSGS PSSETYRGRS AFSAPETAAM RDFINSRVVG GKQQIKTLIT 300
    FHTYSELILY PYGYTYTDVP SDMTQDDFNV FKTMANTMAQ TNGYTPQQAS 350
    DLYITDGDMT DWAYGQHKIF AFTFEMYPTS YNPGFYPPDE VIGRETSRNK 400
    EAVLYVAEKA DCPYSVIGKS CSTK 424
    Length:424
    Mass (Da):47,476
    Last modified:December 1, 1992 - v1
    Checksum:i848934A9A7B1BEAE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56901 Genomic DNA. Translation: CAA40219.1.
    PIRiS17571.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56901 Genomic DNA. Translation: CAA40219.1 .
    PIRi S17571.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OBR X-ray 2.30 A 99-424 [» ]
    3PRT X-ray 1.66 A 99-421 [» ]
    3QNV X-ray 1.69 A 99-421 [» ]
    3V38 X-ray 1.50 A 99-424 [» ]
    3V7Z X-ray 1.61 A 99-424 [» ]
    4DJL X-ray 1.55 A 99-421 [» ]
    4DUK X-ray 1.57 A 99-424 [» ]
    4F8Z X-ray 1.38 A 99-421 [» ]
    4GM5 X-ray 1.39 A 99-421 [» ]
    4IAV X-ray 1.35 A 99-424 [» ]
    4IHM X-ray 1.29 A 99-424 [» ]
    4IK2 X-ray 1.40 A 99-424 [» ]
    ProteinModelPortali P29068.
    SMRi P29068. Positions 99-421.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M14.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P29068.

    Family and domain databases

    InterProi IPR000834. Peptidase_M14.
    [Graphical view ]
    Pfami PF00246. Peptidase_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity."
      Smulevitch S.V., Osterman A.L., Galperina O.V., Matz M.V., Zagnitko O.P., Kadyrov R.M., Tsaplina I.A., Grishin N.V., Chestukhina G.G., Stepanov V.M.
      FEBS Lett. 291:75-78(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Carboxypeptidase T -- intracellular carboxypeptidase of Thermoactinomycetes -- a distant analog of animal carboxypeptidase."
      Osterman A.L., Stepanov V.M., Rudenskaya G.N., Khodova O.M., Tsaplina I.A., Yakovleva M.B., Loginova L.G.
      Biokhimiia 49:292-301(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 99-142.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

    Entry informationi

    Entry nameiCBPT_THEVU
    AccessioniPrimary (citable) accession number: P29068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 87 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3