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Protein

Carboxypeptidase T

Gene

cpt

Organism
Thermoactinomyces vulgaris
Status
Reviewed-Annotation score: 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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Binds four calcium ions which seem to play an important role in the thermostability of the enzyme.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi167Zinc; catalytic1 Publication1
Metal bindingi170Zinc; catalytic1 Publication1
Metal bindingi302Zinc; catalytic1 Publication1
Active sitei375Proton donor/acceptor1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.18. 6282.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000000441524 – 98Activation peptide1 PublicationAdd BLAST75
ChainiPRO_000000441699 – 424Carboxypeptidase TAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi253 ↔ 2541 Publication
Disulfide bondi412 ↔ 4211 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi102 – 104Combined sources3
Helixi110 – 123Combined sources14
Turni125 – 127Combined sources3
Beta strandi128 – 135Combined sources8
Beta strandi141 – 148Combined sources8
Turni149 – 152Combined sources4
Beta strandi159 – 164Combined sources6
Helixi172 – 186Combined sources15
Turni187 – 190Combined sources4
Helixi192 – 200Combined sources9
Beta strandi202 – 206Combined sources5
Helixi211 – 218Combined sources8
Helixi243 – 245Combined sources3
Turni249 – 252Combined sources4
Beta strandi254 – 260Combined sources7
Helixi275 – 286Combined sources12
Beta strandi290 – 293Combined sources4
Beta strandi295 – 302Combined sources8
Beta strandi304 – 311Combined sources8
Helixi325 – 342Combined sources18
Beta strandi345 – 348Combined sources4
Helixi349 – 351Combined sources3
Helixi359 – 367Combined sources9
Beta strandi370 – 375Combined sources6
Turni381 – 385Combined sources5
Helixi389 – 391Combined sources3
Helixi392 – 397Combined sources6
Helixi400 – 409Combined sources10
Helixi413 – 416Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29068.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK05996.

Family and domain databases

CDDicd03859. M14_CPT. 1 hit.
InterProiIPR033810. Carboxypeptidase_T.
IPR000834. 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:
EMBLi
GenBanki
DDBJi
Links Updated
X56901 Genomic DNA. Translation: CAA40219.1.
PIRiS17571.

Genome annotation databases

KEGGiag:CAA40219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56901 Genomic DNA. Translation: CAA40219.1.
PIRiS17571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM14.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA40219.

Phylogenomic databases

KOiK05996.

Enzyme and pathway databases

BRENDAi3.4.17.18. 6282.

Miscellaneous databases

EvolutionaryTraceiP29068.

Family and domain databases

CDDicd03859. M14_CPT. 1 hit.
InterProiIPR033810. Carboxypeptidase_T.
IPR000834. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.