CBP1_THET8
ID CBP1_THET8 Reviewed; 510 AA.
AC Q5SLM3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Thermostable carboxypeptidase 1;
DE EC=3.4.17.19;
DE AltName: Full=TthCP1;
GN OrderedLocusNames=TTHA0270;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15272172; DOI=10.1107/s0907444904012557;
RA Nagata K., Tsutsui S., Lee W.C., Ito K., Kamo M., Inoue Y., Tanokura M.;
RT "Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from
RT Thermus thermophilus.";
RL Acta Crystallogr. D 60:1445-1446(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR,
RP CATALYTIC ACTIVITY, SUBUNIT, AND FUNCTION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=19544567; DOI=10.1002/prot.22478;
RA Lee M.M., Isaza C.E., White J.D., Chen R.P., Liang G.F., He H.T.,
RA Chan S.I., Chan M.K.;
RT "Insight into the substrate length restriction of M32 carboxypeptidases:
RT characterization of two distinct subfamilies.";
RL Proteins 77:647-657(2009).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues, but not Pro. Has lower activity with substrates
CC ending with Gly or Glu. {ECO:0000269|PubMed:19544567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000269|PubMed:19544567};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19544567};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19544567};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15272172,
CC ECO:0000269|PubMed:19544567}.
CC -!- SIMILARITY: Belongs to the peptidase M32 family. {ECO:0000305}.
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DR EMBL; AP008226; BAD70093.1; -; Genomic_DNA.
DR RefSeq; WP_011174078.1; NC_006461.1.
DR RefSeq; YP_143536.1; NC_006461.1.
DR PDB; 3HOA; X-ray; 2.10 A; A/B=1-509.
DR PDB; 5WVU; X-ray; 2.60 A; A/B/C=1-510.
DR PDBsum; 3HOA; -.
DR PDBsum; 5WVU; -.
DR AlphaFoldDB; Q5SLM3; -.
DR SMR; Q5SLM3; -.
DR STRING; 300852.55771652; -.
DR MEROPS; M32.001; -.
DR EnsemblBacteria; BAD70093; BAD70093; BAD70093.
DR GeneID; 3168368; -.
DR KEGG; ttj:TTHA0270; -.
DR PATRIC; fig|300852.9.peg.270; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_1_0; -.
DR OMA; EFGHALY; -.
DR PhylomeDB; Q5SLM3; -.
DR EvolutionaryTrace; Q5SLM3; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217; PTHR34217; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..510
FT /note="Thermostable carboxypeptidase 1"
FT /id="PRO_0000428835"
FT ACT_SITE 277
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P42663"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15272172"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15272172"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15272172"
FT HELIX 3..32
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 40..59
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 82..99
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:5WVU"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 128..150
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 178..200
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5WVU"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:5WVU"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5WVU"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 267..286
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:5WVU"
FT TURN 314..318
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5WVU"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:5WVU"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5WVU"
FT TURN 410..414
FT /evidence="ECO:0007829|PDB:5WVU"
FT TURN 418..422
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 428..448
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 480..488
FT /evidence="ECO:0007829|PDB:5WVU"
FT HELIX 495..508
FT /evidence="ECO:0007829|PDB:5WVU"
SQ SEQUENCE 510 AA; 58014 MW; 6EE48D42AA2FA379 CRC64;
MTPEAAYQNL LEFQRETAYL ASLGALAAWD QRTMIPKKGH EHRARQMAAL ARLLHQRMTD
PRIGEWLEKV EGSPLVQDPL SDAAVNVREW RQAYERARAI PERLAVELAQ AESEAESFWE
EARPRDDWRG FLPYLKRVYA LTKEKAEVLF ALPPAPGDPP YGELYDALLD GYEPGMRARE
LLPLFAELKE GLKGLLDRIL GSGKRPDTSI LHRPYPVEAQ RRFALELLSA CGYDLEAGRL
DPTAHPFEIA IGPGDVRITT RYYEDFFNAG IFGTLHEMGH ALYEQGLPKE HWGTPRGDAV
SLGVHESQSR TWENLVGRSL GFWERFFPRA REVFASLGDV SLEDFHFAVN AVEPSLIRVE
ADEVTYNLHI LVRLELELAL FRGELSPEDL PEAWAEKYRD HLGVAPKDYK DGVMQDVHWA
GGLFGYFPTY TLGNLYAAQF FQKAEAELGP LEPRFARGEF QPFLDWTRAR IHAEGSRFRP
RVLVERVTGE APSARPFLAY LEKKYAALYG
