ID B9ZZP1_9BACI Unreviewed; 500 AA.
AC B9ZZP1;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 03-MAY-2023, entry version 32.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN Name=Carb {ECO:0000313|EMBL:BAH28805.1};
OS Geobacillus sp. SBS-4S.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=446356 {ECO:0000313|EMBL:BAH28805.1};
RN [1] {ECO:0000313|EMBL:BAH28805.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBS-4S {ECO:0000313|EMBL:BAH28805.1};
RX PubMed=21126910; DOI=10.1016/j.jbiosc.2010.11.002;
RA Tayyab M., Rashid N., Angkawidjaja C., Kanaya S., Akhtar M.;
RT "Highly active metallocarboxypeptidase from newly isolated Geobacillus
RT strain SBS-4S: Cloning and characterization.";
RL J. Biosci. Bioeng. 111:259-265(2011).
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; AB457188; BAH28805.1; -; Genomic_DNA.
DR AlphaFoldDB; B9ZZP1; -.
DR MEROPS; M32.006; -.
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:BAH28805.1}; 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 266
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 500 AA; 58003 MW; 5DA6A0BDBC3CF6BF CRC64;
MKPIEAQFLQ YVKKMTGYRE AIGLMYWDLR TGAPKKGVEQ RSEVIGMLSE EVFRMSTSEE
MAAFIAKLSP KAVYEQLNDV TKKTLDECKK EYERNKKIPA DEYKEFVVLC SKAESVWEEA
KAAADFARFR PYLEQIIEFQ RRFIRYWGYE GHPYNTLLDQ YEPGMTVDLL DELFSRLRER
IVPLVHAISA ASDKPDTSFL FAPFPKEKQR AFLLELLKEL GYDFGKGRLD ETVHPFAIGL
NPNDVRITTR YDERDFRTAV FGTIHECGHA LYEQHISEAL VGTPLASGAS MGIHESQSLF
FENMIGRHYA FWKRHYPRLQ QYAPTQFADV SLDAFYRAIN EAKPSLIRIE ADELTYPLHI
IIRYEIEKQL FAGELEAIDL PDVWNEKYEQ YLGIRPHNDA VGVLQDVHWS GGSFGYFPSY
ALGYMYAAQF KQAMEKELDV AGLLEEGNIA PIREWLTVHI HQFGKMKKPL ELVRDATGET
LKADYLIQYL EEKYKALYRL
//
