CBPT_THEVU
ID CBPT_THEVU Reviewed; 424 AA.
AC P29068;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Carboxypeptidase T;
DE EC=3.4.17.18;
DE Flags: Precursor;
GN Name=cpt;
OS Thermoactinomyces vulgaris.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=2026;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1936254; DOI=10.1016/0014-5793(91)81107-j;
RA Smulevitch S.V., Osterman A.L., Galperina O.V., Matz M.V., Zagnitko O.P.,
RA Kadyrov R.M., Tsaplina I.A., Grishin N.V., Chestukhina G.G., Stepanov V.M.;
RT "Molecular cloning and primary structure of Thermoactinomyces vulgaris
RT carboxypeptidase T. A metalloenzyme endowed with dual substrate
RT specificity.";
RL FEBS Lett. 291:75-78(1991).
RN [2]
RP PROTEIN SEQUENCE OF 99-142.
RX PubMed=6424730;
RA Osterman A.L., Stepanov V.M., Rudenskaya G.N., Khodova O.M., Tsaplina I.A.,
RA Yakovleva M.B., Loginova L.G.;
RT "Carboxypeptidase T -- intracellular carboxypeptidase of
RT Thermoactinomycetes -- a distant analog of animal carboxypeptidase.";
RL Biokhimiia 49:292-301(1984).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 99-424 IN COMPLEX WITH CALCIUM
RP AND ZINC, AND DISULFIDE BONDS.
RX PubMed=1521526; DOI=10.1111/j.1432-1033.1992.tb17184.x;
RA Teplyakov A., Polyakov K., Obmolova G., Strokopytov B., Kuranova I.,
RA Osterman A.L., Grishin N.V., Smulevitch S.V., Zagnitko O.P.,
RA Galperina O.V., Matz M.V., Stepanov V.M.;
RT "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris.";
RL Eur. J. Biochem. 208:281-288(1992).
CC -!- FUNCTION: Able to split off hydrophobic and basic amino acids with
CC comparable efficiency.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Releases a C-terminal residue, which may be hydrophobic or
CC positively charged.; EC=3.4.17.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1521526};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1521526};
CC -!- ACTIVITY REGULATION: Binds four calcium ions which seem to play an
CC important role in the thermostability of the enzyme.
CC {ECO:0000305|PubMed:1521526}.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; X56901; CAA40219.1; -; Genomic_DNA.
DR PIR; S17571; S17571.
DR PDB; 1OBR; X-ray; 2.30 A; A=99-424.
DR PDB; 3PRT; X-ray; 1.66 A; A=99-421.
DR PDB; 3QNV; X-ray; 1.69 A; A=99-421.
DR PDB; 3V38; X-ray; 1.50 A; A=99-424.
DR PDB; 3V7Z; X-ray; 1.61 A; A=99-424.
DR PDB; 4DJL; X-ray; 1.55 A; A=99-421.
DR PDB; 4DUK; X-ray; 1.57 A; A=99-424.
DR PDB; 4F8Z; X-ray; 1.38 A; A=99-421.
DR PDB; 4GM5; X-ray; 1.39 A; A=99-421.
DR PDB; 4IAV; X-ray; 1.35 A; A=99-424.
DR PDB; 4IHM; X-ray; 1.29 A; A=99-424.
DR PDB; 4IK2; X-ray; 1.40 A; A=99-424.
DR PDB; 6F6Q; X-ray; 1.79 A; A=99-421.
DR PDB; 6F75; X-ray; 1.89 A; A=99-421.
DR PDB; 6F79; X-ray; 1.90 A; A=99-421.
DR PDB; 6GO2; X-ray; 1.90 A; A=99-421.
DR PDB; 6Q4L; X-ray; 2.30 A; A=99-421.
DR PDB; 6SN6; X-ray; 1.93 A; A=99-421.
DR PDB; 6T9Y; X-ray; 1.92 A; A=99-421.
DR PDB; 6TNK; X-ray; 1.90 A; A=99-421.
DR PDB; 6Z28; X-ray; 2.30 A; A=99-421.
DR PDB; 7AQP; X-ray; 2.60 A; A=99-421.
DR PDB; 7ARU; X-ray; 2.05 A; A=99-421.
DR PDB; 7Q87; X-ray; 1.73 A; A=99-421.
DR PDBsum; 1OBR; -.
DR PDBsum; 3PRT; -.
DR PDBsum; 3QNV; -.
DR PDBsum; 3V38; -.
DR PDBsum; 3V7Z; -.
DR PDBsum; 4DJL; -.
DR PDBsum; 4DUK; -.
DR PDBsum; 4F8Z; -.
DR PDBsum; 4GM5; -.
DR PDBsum; 4IAV; -.
DR PDBsum; 4IHM; -.
DR PDBsum; 4IK2; -.
DR PDBsum; 6F6Q; -.
DR PDBsum; 6F75; -.
DR PDBsum; 6F79; -.
DR PDBsum; 6GO2; -.
DR PDBsum; 6Q4L; -.
DR PDBsum; 6SN6; -.
DR PDBsum; 6T9Y; -.
DR PDBsum; 6TNK; -.
DR PDBsum; 6Z28; -.
DR PDBsum; 7AQP; -.
DR PDBsum; 7ARU; -.
DR PDBsum; 7Q87; -.
DR AlphaFoldDB; P29068; -.
DR SMR; P29068; -.
DR MEROPS; M14.007; -.
DR KEGG; ag:CAA40219; -.
DR BRENDA; 3.4.17.18; 6282.
DR EvolutionaryTrace; P29068; -.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03859; M14_CPT; 1.
DR InterPro; IPR033810; Carboxypeptidase_T.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carboxypeptidase; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..98
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:6424730"
FT /id="PRO_0000004415"
FT CHAIN 99..424
FT /note="Carboxypeptidase T"
FT /id="PRO_0000004416"
FT ACT_SITE 375
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:1521526"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1521526"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1521526"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1521526"
FT DISULFID 253..254
FT /evidence="ECO:0000269|PubMed:1521526"
FT DISULFID 412..421
FT /evidence="ECO:0000269|PubMed:1521526"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:4IHM"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4IHM"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:4IHM"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4IHM"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1OBR"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 325..342
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:4IHM"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:4IHM"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:4IHM"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:4IHM"
SQ SEQUENCE 424 AA; 47476 MW; 848934A9A7B1BEAE CRC64;
MRKKWLSLSL VLVLIVACVP ALGFSQNIEN PSIFDLGIKL YKIDGVSTKE QRSAIASTGA
AIEEVGKDYV KVLATPSEAK QIKQKGFTAT VDTSLTTQDF PSYDSGYHNY NEMVNKINTV
ASNYPNIVKK FSIGKSYEGR ELWAVKISDN VGTDENEPEV LYTALHHARE HLTVEMALYT
LDLFTQNYNL DSRITNLVNN REIYIVFNIN PDGGEYDISS GSYKSWRKNR QPNSGSSYVG
TDLNRNYGYK WGCCGGSSGS PSSETYRGRS AFSAPETAAM RDFINSRVVG GKQQIKTLIT
FHTYSELILY PYGYTYTDVP SDMTQDDFNV FKTMANTMAQ TNGYTPQQAS DLYITDGDMT
DWAYGQHKIF AFTFEMYPTS YNPGFYPPDE VIGRETSRNK EAVLYVAEKA DCPYSVIGKS
CSTK
