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P29068 (CBPT_THEVU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase T

EC=3.4.17.18
Gene names
Name:cpt
OrganismThermoactinomyces vulgaris
Taxonomic identifier2026 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Enzyme regulation

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

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 9875Activation peptide
PRO_0000004415
Chain99 – 424326Carboxypeptidase T
PRO_0000004416

Sites

Active site3531Proton donor
Active site3751Nucleophile
Metal binding1671Zinc
Metal binding1701Zinc
Metal binding3021Zinc

Amino acid modifications

Disulfide bond253 ↔ 254
Disulfide bond412 ↔ 421

Secondary structure

...................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29068 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 848934A9A7B1BEAE

FASTA42447,476
        10         20         30         40         50         60 
MRKKWLSLSL VLVLIVACVP ALGFSQNIEN PSIFDLGIKL YKIDGVSTKE QRSAIASTGA 

        70         80         90        100        110        120 
AIEEVGKDYV KVLATPSEAK QIKQKGFTAT VDTSLTTQDF PSYDSGYHNY NEMVNKINTV 

       130        140        150        160        170        180 
ASNYPNIVKK FSIGKSYEGR ELWAVKISDN VGTDENEPEV LYTALHHARE HLTVEMALYT 

       190        200        210        220        230        240 
LDLFTQNYNL DSRITNLVNN REIYIVFNIN PDGGEYDISS GSYKSWRKNR QPNSGSSYVG 

       250        260        270        280        290        300 
TDLNRNYGYK WGCCGGSSGS PSSETYRGRS AFSAPETAAM RDFINSRVVG GKQQIKTLIT 

       310        320        330        340        350        360 
FHTYSELILY PYGYTYTDVP SDMTQDDFNV FKTMANTMAQ TNGYTPQQAS DLYITDGDMT 

       370        380        390        400        410        420 
DWAYGQHKIF AFTFEMYPTS YNPGFYPPDE VIGRETSRNK EAVLYVAEKA DCPYSVIGKS 


CSTK 

« Hide

References

[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]"Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris."
Teplyakov A., Polyakov K., Obmolova G., Strokopytov B., Kuranova I., Osterman A.L., Grishin N.V., Smulevitch S.V., Zagnitko O.P., Galperina O.V., Matz M.V., Stepanov V.M.
Eur. J. Biochem. 208:281-288(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56901 Genomic DNA. Translation: CAA40219.1.
PIRS17571.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP29068.
SMRP29068. Positions 99-421.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM14.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000834. Peptidase_M14.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29068.

Entry information

Entry nameCBPT_THEVU
AccessionPrimary (citable) accession number: P29068
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: March 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references