ID L0K1D2_9EURY Unreviewed; 509 AA.
AC L0K1D2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=Natoc_2399 {ECO:0000313|EMBL:AGB38174.1};
OS Natronococcus occultus SP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB38174.1, ECO:0000313|Proteomes:UP000010878};
RN [1] {ECO:0000313|EMBL:AGB38174.1, ECO:0000313|Proteomes:UP000010878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP4 {ECO:0000313|EMBL:AGB38174.1,
RC ECO:0000313|Proteomes:UP000010878};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA Klenk H.-P.;
RT "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL Submitted (NOV-2012) 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; CP003929; AGB38174.1; -; Genomic_DNA.
DR RefSeq; WP_015321616.1; NC_019974.1.
DR AlphaFoldDB; L0K1D2; -.
DR STRING; 694430.Natoc_2399; -.
DR GeneID; 14404083; -.
DR KEGG; nou:Natoc_2399; -.
DR eggNOG; arCOG04247; Archaea.
DR HOGENOM; CLU_032916_1_1_2; -.
DR OrthoDB; 7244at2157; -.
DR Proteomes; UP000010878; 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:AGB38174.1}; 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:UP000010878};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 271
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 509 AA; 58226 MW; 90B3FC9E9B9797FA CRC64;
MATDQAQSEQ RDETYEQFEE RITRISNVGN AAGILRWDQE VVMPEAGTPA RAQQLSTLSS
ISHELLTADE TGELLEKLES DELADEQQAA VREVRRQYDR ETSVPQELVE EISETTANAH
PTWKQAKEDD DFEQFAPTLE KLVELKREYA EHIDPDADPY AVLFADYEPY LDLETAERVL
ERLREELVPL IDAIQDADVD RATDTFAGTF DDDDQEALAR DVLDALNYDW ERGRLDTAPH
PFSSGTQFDA RVTTRFEEDD LLGSLTSTIH EFGHANYTLG LPDEEYGTPL GESRDLSVHE
SQSRLWENHV GRSRPFWEQF LPTVADRFPE LEDATPEDAY EAANQVYDDN LIRVEADELT
YHLHIVIRFE IERALISGDL EVEDVPEVWN DKYEEYLGVR PETDAEGCLQ DIHWSHGSFG
YFPTYSLGSV LAAQLYAAAE DDLGDLNDDI RAGEFDDLNG WLRENVHQHG KRYTTPELIE
EATGESFTAD YFLEYAKSKY GELYDLEDY
//
