ID A0A3A9KF55_9BACI Unreviewed; 507 AA.
AC A0A3A9KF55;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=CR203_04050 {ECO:0000313|EMBL:RKL69211.1};
OS Salipaludibacillus neizhouensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL69211.1, ECO:0000313|Proteomes:UP000281498};
RN [1] {ECO:0000313|EMBL:RKL69211.1, ECO:0000313|Proteomes:UP000281498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL69211.1,
RC ECO:0000313|Proteomes:UP000281498};
RA Wang H.;
RT "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKL69211.1}.
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DR EMBL; PDOE01000001; RKL69211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9KF55; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000281498; Unassembled WGS sequence.
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:RKL69211.1}; 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:UP000281498};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
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 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 507 AA; 58050 MW; AA245829B651FCF4 CRC64;
MTTETETLEE RFLTYIKKIS HFEESIGLMA WDLRTGAPRK GASQRSEVLG TLSSEVFAMS
TSKELKGYLE GLRETSVWSK LAEVTKGSVE ECEKQLKKYE NIPPQEFKAY VILTSNAEVA
WEKAKNDADF KTFQPYLEKI VDYNRKYTEW VGYKGNKYNA LLDDYEPGLT VDIIDDVFGK
LKKALVPLVK EITEAKDQPQ TDFLFQPFPA KNQEALSREI LESMRYDFDA GRLDTTVHPF
AIGLNPGDVR VTTKYDEMDF RTAVFGTIHE GGHALYEQNI DEKFIGTPLC TGTSMGIHES
QSLFWENFVG RHFSFWEKYY DLLKKNANGQ FDDIDLHTFY RGINVAGPSL IRIEADEMTY
SLHIIARYEL EKALINGELE VADLPGAWND KMEELLGVRP SHDGEGVLQD VHWPSGAFGY
FPSYALGYVY AAQLKKAMEK ELPDFKQLLQ KGDLAPIKEW LTKNIHQYGK SKEPLEILKD
TTGEGVNPSY LIEYLESKYR NVYRITE
//
