CBP1_PYRFU
ID CBP1_PYRFU Reviewed; 499 AA.
AC Q8U3L0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thermostable carboxypeptidase 1;
DE EC=3.4.17.19;
DE AltName: Full=Carboxypeptidase Pfu;
DE Short=PfuCP;
GN OrderedLocusNames=PF0456;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-30; 41-72 AND 480-495, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10595552; DOI=10.1110/ps.8.11.2474;
RA Cheng T.C., Ramakrishnan V., Chan S.I.;
RT "Purification and characterization of a cobalt-activated carboxypeptidase
RT from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL Protein Sci. 8:2474-2486(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND LEAD
RP IONS, SUBUNIT, AND COFACTOR.
RX PubMed=11839307; DOI=10.1016/s0969-2126(02)00698-6;
RA Arndt J.W., Hao B., Ramakrishnan V., Cheng T., Chan S.I., Chan M.K.;
RT "Crystal structure of a novel carboxypeptidase from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL Structure 10:215-224(2002).
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, Gly, Asp and Glu.
CC {ECO:0000269|PubMed:10595552}.
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:10595552};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:10595552, ECO:0000269|PubMed:11839307};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10595552, ECO:0000269|PubMed:11839307};
CC Note=Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in
CC vitro). Is not active with zinc ions. {ECO:0000269|PubMed:10595552,
CC ECO:0000269|PubMed:11839307};
CC -!- ACTIVITY REGULATION: EDTA and DTT reversibly abolish carboxypeptidase
CC activity. {ECO:0000269|PubMed:10595552}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.2-6.6. {ECO:0000269|PubMed:10595552};
CC Temperature dependence:
CC Optimum temperature is 90-100 degrees Celsius.
CC {ECO:0000269|PubMed:10595552};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10595552,
CC ECO:0000269|PubMed:11839307}.
CC -!- SIMILARITY: Belongs to the peptidase M32 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80580.1; -; Genomic_DNA.
DR RefSeq; WP_011011573.1; NZ_CP023154.1.
DR PDB; 1K9X; X-ray; 2.30 A; A/B/C/D=1-499.
DR PDB; 1KA2; X-ray; 2.20 A; A=1-499.
DR PDB; 1KA4; X-ray; 3.00 A; A=1-499.
DR PDBsum; 1K9X; -.
DR PDBsum; 1KA2; -.
DR PDBsum; 1KA4; -.
DR AlphaFoldDB; Q8U3L0; -.
DR SMR; Q8U3L0; -.
DR STRING; 186497.PF0456; -.
DR MEROPS; M32.002; -.
DR EnsemblBacteria; AAL80580; AAL80580; PF0456.
DR GeneID; 41712256; -.
DR KEGG; pfu:PF0456; -.
DR PATRIC; fig|186497.12.peg.480; -.
DR eggNOG; arCOG04247; Archaea.
DR HOGENOM; CLU_032916_1_1_2; -.
DR OMA; EFGHALY; -.
DR OrthoDB; 15879at2157; -.
DR PhylomeDB; Q8U3L0; -.
DR BRENDA; 3.4.17.B5; 5243.
DR EvolutionaryTrace; Q8U3L0; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; 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; Cobalt; Direct protein sequencing;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..499
FT /note="Thermostable carboxypeptidase 1"
FT /id="PRO_0000428834"
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P42663"
FT BINDING 269
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11839307"
FT BINDING 273
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11839307"
FT BINDING 299
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11839307"
FT HELIX 8..36
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 102..124
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 169..192
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:1KA2"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1KA2"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1KA2"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1KA2"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 261..278
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:1KA2"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1KA2"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 359..375
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:1KA2"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 421..440
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 444..450
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:1KA2"
FT HELIX 488..498
FT /evidence="ECO:0007829|PDB:1KA2"
SQ SEQUENCE 499 AA; 59043 MW; 627A8347CD899BC0 CRC64;
MEEVFQNETI KQILAKYRRI WAIGHAQSVL GWDLEVNMPK EGILERSVAQ GELSVLSHEL
LLHPEFVNLV EKAKGLENLN EYERGIVRVL DRSIRIARAF PPEFIREVSE TTSLATKAWE
EAKAKDDFSK FEPWLDKIIS LAKRAAEYLG YEEEPYDALL DLYEEGLRTR DVEKMFEVLE
KKLKPLLDKI LEEGKVPREH PLEKEKYERE WMERVNLWIL QKFGFPLGTR ARLDVSAHPF
TTEFGIRDVR ITTRYEGYDF RRTILSTVHE FGHALYELQQ DERFMFTPIA GGVSLGIHES
QSRFWENIIG RSKEFVELIY PVLKENLPFM SNYTPEDVYL YFNIVRPDFI RTEADVVTYN
FHILLRFKLE RLMVSEEIKA KDLPEMWNDE MERLLGIRPR KYSEGILQDI HWAHGSIGYF
PTYTIGTLLS AQLYYHIKKD IPDFEEKVAK AEFDPIKAWL REKIHRWGSI YPPKELLKKA
IGEDMDAEYF VRWVKEKYL
