P29068 (CBPT_THEVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carboxypeptidase T
EC=3.4.17.18

Gene names

Name:

cpt

Organism

Thermoactinomyces vulgaris

Taxonomic identifier

2026 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Thermoactinomycetaceae › Thermoactinomyces

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Propeptide

24 – 98

75

Activation peptide

PRO_0000004415

Chain

99 – 424

326

Carboxypeptidase T

PRO_0000004416

Sites

Active site

353

1

Proton donor

Active site

375

1

Nucleophile

Metal binding

167

1

Zinc

Metal binding

170

1

Zinc

Metal binding

302

1

Zinc

Amino acid modifications

Disulfide bond

253 ↔ 254

Disulfide bond

412 ↔ 421

Secondary structure

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424

Helix Strand Turn

Details...

Helix

102 – 104

3

Helix

110 – 123

14

Turn

125 – 127

3

Beta strand

128 – 135

8

Beta strand

141 – 147

7

Turn

149 – 152

4

Beta strand

159 – 164

6

Helix

172 – 186

15

Turn

187 – 190

4

Helix

192 – 200

9

Beta strand

202 – 206

5

Helix

211 – 218

8

Helix

243 – 245

3

Turn

249 – 252

4

Beta strand

254 – 259

6

Helix

275 – 286

12

Beta strand

290 – 293

4

Beta strand

295 – 302

8

Beta strand

304 – 311

8

Helix

325 – 342

18

Beta strand

345 – 348

4

Helix

349 – 351

3

Helix

359 – 367

9

Beta strand

370 – 375

6

Turn

381 – 385

5

Helix

389 – 391

3

Helix

392 – 397

6

Helix

400 – 409

10

Helix

413 – 416

4

Sequences

	Sequence		Length	Mass (Da)
	P29068 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 848934A9A7B1BEAE	FASTA	424	47,476
	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

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.

PIR

S17571.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P29068.

SMR

P29068. Positions 99-421.

ModBase

Search...

Protein family/group databases

MEROPS

M14.007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000834. Peptidase_M14.
[Graphical view]

Pfam

PF00246. Peptidase_M14. 1 hit.
[Graphical view]

PRINTS

PR00765. CRBOXYPTASEA.

SMART

SM00631. Zn_pept. 1 hit.
[Graphical view]

PROSITE

PS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29068.

Entry information

Entry name

CBPT_THEVU

Accession

Primary (citable) accession number: P29068

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program