ID A0A098EK29_9BACL Unreviewed; 500 AA.
AC A0A098EK29;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN Name=ypwA {ECO:0000313|EMBL:CEG22648.1};
GN ORFNames=BN1080_01581 {ECO:0000313|EMBL:CEG22648.1};
OS Planococcus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG22648.1, ECO:0000313|Proteomes:UP000043699};
RN [1] {ECO:0000313|EMBL:CEG22648.1, ECO:0000313|Proteomes:UP000043699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES2 {ECO:0000313|EMBL:CEG22648.1,
RC ECO:0000313|Proteomes:UP000043699};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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; CCXS01000001; CEG22648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098EK29; -.
DR STRING; 1499687.BN1080_01581; -.
DR MEROPS; M32.006; -.
DR Proteomes; UP000043699; 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 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 ECO:0000313|EMBL:CEG22648.1};
KW Protease {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:CEG22648.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000043699};
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 500 AA; 57079 MW; EBD5AC6D2CA614FE CRC64;
MTLEKQYKDH VSKMQAYNEA LSLLYWDLRT GAPKKGTDLR SETIGTLSSE LFALSTSDEF
GQLLTDLEAD LAGLSRVMQR SVEESRKEYD LSKKIPPEEY KKYVILQSKA ESVWEDAKAA
ADFSLFEPYL EELVSMTKKM IGYWGEKNGS AYNTLLDQYE PGMTTDILDE VFGKLRSRIV
PLVQKIAASE NKPETGFLYE HFPKQAQRDL SIEILKQLGY DFEAGRLDET VHPFMTTINR
RDVRVTTKYD EQDFRTAVFG TIHEGGHALY DQNLGADLSG LAIEDGASMG IHESQSLFFE
NFIGRNKNFW TSNYDLLKKY APKQFEAVSL EDYVRAINES KPSLIRIEAD ELTYALHIMI
RYELEKGLFN GDLAVKDLPK LWNDKYEEYL GVRPSTDAEG VLQDVHWAGG SFGYFPSYAL
GYMYAAQFKN AMLKSLPDFD ELLAKGNITP IREWLTENVH QYGMSKKPLE ILEDATGEGL
NADYLAAYLE EKYSKIYQLN
//
