ID A0A2Z3JK29_9DEIO Unreviewed; 508 AA.
AC A0A2Z3JK29;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=DKM44_12400 {ECO:0000313|EMBL:AWN23931.1};
OS Deinococcus irradiatisoli.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN23931.1, ECO:0000313|Proteomes:UP000245368};
RN [1] {ECO:0000313|EMBL:AWN23931.1, ECO:0000313|Proteomes:UP000245368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17bor-2 {ECO:0000313|EMBL:AWN23931.1,
RC ECO:0000313|Proteomes:UP000245368};
RA Srinivasan S.;
RT "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
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:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
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DR EMBL; CP029494; AWN23931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3JK29; -.
DR KEGG; dez:DKM44_12400; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000245368; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:AWN23931.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Reference proteome {ECO:0000313|Proteomes:UP000245368};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 273
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 508 AA; 57254 MW; 233D21EC67705D84 CRC64;
MTSPASLTDA STAFAELKRR LNLISDLGAA QGLMSWDQET QMPPDAARVR GLQMAGLAGL
SHQLFTADET RALLEAAERE DAPGEVEADL LRVVRRDFDK ATRLPTAFVE EMSRARNEAH
HAWIKARTDN DFAHFAPYLQ RVLDLTRQYA ELSGYAEHPY DALLDDYEPG MKTAQVRRIF
ADLRERTLPL LRAIVAAGDA TDYGVLSRPF PASAQRDFAL KVAGEAFGLR PAFSRLDESA
HPFQTNFSAD DLRITTRFDE HYFPMSLFGT WHEAGHAMYE HGVSRELERT PLSRGASLGV
HESQSRMFEN LLGRSRAFWQ RYFEEFAQAA PDVAAGQDAE NLYRAVNRVQ PSLIRVEADE
VTYNFHIMLR FELELALLEG TLSVEELPSA WNARMQEYLG VTPPNDAEGV LQDIHWSSGL
IGYFPTYSLG NLLSVQLLEA ARREPQVAGG LERADYTPLR EWLRQQVHQY GRRRTPDQLV
QAATGAPLSA DAYVKYLHEK YADIYQLG
//
