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P29068

- CBPT_THEVU

UniProt

P29068 - CBPT_THEVU

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Protein

Carboxypeptidase T

Gene

cpt

Organism
Thermoactinomyces vulgaris
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MRKKWLSLSL VLVLIVACVP ALGFSQNIEN PSIFDLGIKL YKIDGVSTKE
60 70 80 90 100
QRSAIASTGA AIEEVGKDYV KVLATPSEAK QIKQKGFTAT VDTSLTTQDF
110 120 130 140 150
PSYDSGYHNY NEMVNKINTV ASNYPNIVKK FSIGKSYEGR ELWAVKISDN
160 170 180 190 200
VGTDENEPEV LYTALHHARE HLTVEMALYT LDLFTQNYNL DSRITNLVNN
210 220 230 240 250
REIYIVFNIN PDGGEYDISS GSYKSWRKNR QPNSGSSYVG TDLNRNYGYK
260 270 280 290 300
WGCCGGSSGS PSSETYRGRS AFSAPETAAM RDFINSRVVG GKQQIKTLIT
310 320 330 340 350
FHTYSELILY PYGYTYTDVP SDMTQDDFNV FKTMANTMAQ TNGYTPQQAS
360 370 380 390 400
DLYITDGDMT DWAYGQHKIF AFTFEMYPTS YNPGFYPPDE VIGRETSRNK
410 420
EAVLYVAEKA DCPYSVIGKS CSTK
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