ID M1JDR7_9CREN Unreviewed; 490 AA.
AC M1JDR7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=SacRon12I_08070 {ECO:0000313|EMBL:AGE73845.1};
OS Sulfolobus acidocaldarius Ron12/I.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1028567 {ECO:0000313|Proteomes:UP000011280};
RN [1] {ECO:0000313|EMBL:AGE73845.1, ECO:0000313|Proteomes:UP000011280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ron12/I {ECO:0000313|EMBL:AGE73845.1,
RC ECO:0000313|Proteomes:UP000011280};
RX PubMed=22418622; DOI=10.1038/ismej.2012.20;
RA Mao D., Grogan D.;
RT "Genomic evidence of rapid, global-scale gene flow in a Sulfolobus
RT species.";
RL ISME J. 6:1613-1616(2012).
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; CP002818; AGE73845.1; -; Genomic_DNA.
DR RefSeq; WP_011278473.1; NC_020247.1.
DR AlphaFoldDB; M1JDR7; -.
DR GeneID; 78442002; -.
DR KEGG; sacr:SacRon12I_08070; -.
DR PATRIC; fig|1028567.7.peg.1586; -.
DR HOGENOM; CLU_032916_1_1_2; -.
DR Proteomes; UP000011280; 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:AGE73845.1}; 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 Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 490 AA; 57339 MW; B7EA868BE63240AA CRC64;
MKRFENLKEL LAEYKKLWSL QYAESLMGWD IETYMPEDDA MTRGEVISTF SEIKREIYQK
LGKIIERYEG KEGLNDEERG ILRVLGRDYK YYSKIPLEII QQIERVRSEA TVVWRQAKAK
SDYSMFKPYL EKIKDLQIKI AEYWGYEDHP YNALLDLNEE GFSIRDGDRI FSRLLPELSD
IMKKVSEKGY FPKSHELEEV SYDIGRMKVV NEEVIKILEM PKGKFRLDIS AHPFTVRISA
DDVRITTRYE GKDFRSTLFS VVHECGHAIY ELGIDRELEG TPIGGGVSMG IHEAQSRFWE
NIIGRSREFV SLIYPKLKQN LDFLSKYNED DIYRYFNIVR PSFIRVDADE VTYNFHIAVR
YEIEKRLIGG EIKVDEIPSL WSELMEKYLG ITPKNDAEGA LQDIHWTGGF GYFPAYTLGN
VVSGIVYSKT PNLYNLLREG KIGEIKTIMT EKIYKYGATY SPKDLLRKTF GEEYNPEGLI
LYLRHKYLKS
//