ID C3MKM5_SULIL Unreviewed; 467 AA.
AC C3MKM5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=LS215_2425 {ECO:0000313|EMBL:ACP36396.1};
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572 {ECO:0000313|EMBL:ACP36396.1, ECO:0000313|Proteomes:UP000001747};
RN [1] {ECO:0000313|EMBL:ACP36396.1, ECO:0000313|Proteomes:UP000001747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1 {ECO:0000313|Proteomes:UP000001747};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP36396.1; -; Genomic_DNA.
DR RefSeq; WP_012714308.1; NC_012589.1.
DR AlphaFoldDB; C3MKM5; -.
DR GeneID; 7798410; -.
DR KEGG; sis:LS215_2425; -.
DR HOGENOM; CLU_032916_1_1_2; -.
DR OrthoDB; 7244at2157; -.
DR Proteomes; UP000001747; 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:ACP36396.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:ACP36396.1};
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 Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 248
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 467 AA; 54797 MW; B41C0B988D5A61DE CRC64;
MYEDIWAIEH AISLLDWDIQ TYMPQSGIKA RGEALARLSN LRRKLLLGIR GEIEKLEPKN
DIEKGLKRVL DREYKYYDAV PEELDMKLHR IASEATVVWR NAKAKGDFNA FKPYLEQILE
IKREIAHKLG YKDHPYSALL DRYEEGFTVT DAERVFNELL PGLSKILNKI DDKFTRKYHF
EDEKYDVFQM SKTIEAIAYE VLKMPKDRFR IDVSPHPFTV SMSRNDVRIT VRYEGYDFKR
VLYSLVHESG HAIYELQIDP SLEYSPLANA PSMGLHESQS RFWENVVGRS YGFIKTIYPL
LNVKDSIDDV YYYVNGVKRQ PIRVDADEVT YNFHIAIRYE IEKRAIEGSL EASEFPSLFN
DLMDKYLNIR PKNDGEGVLQ DVHWSQGSFG YFPTYTLGNV IAGMVYYHMK SERGFDISNI
EGIKNWLRER IHKYGSIYSP KELQMRSFGE AYNPSRLLDY MREKYNA
//
