ID W9BGP0_KLEPN Unreviewed; 495 AA.
AC W9BGP0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:CAH1468039.1};
GN ORFNames=GJJ13_013375 {ECO:0000313|EMBL:QOU76577.1}, VKR_02674
GN {ECO:0000313|EMBL:CAH1468039.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:CAH1468039.1, ECO:0000313|Proteomes:UP001158595};
RN [1] {ECO:0000313|EMBL:QOU76577.1, ECO:0000313|Proteomes:UP000438340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CriePir45 {ECO:0000313|EMBL:QOU76577.1,
RC ECO:0000313|Proteomes:UP000438340};
RX PubMed=32429555;
RA Shelenkov A., Mikhaylova Y., Yanushevich Y., Samoilov A., Petrova L.,
RA Fomina V., Gusarov V., Zamyatin M., Shagin D., Akimkin V.;
RT "Molecular Typing, Characterization of Antimicrobial Resistance, Virulence
RT Profiling and Analysis of Whole-Genome Sequence of Clinical Klebsiella
RT pneumoniae Isolates.";
RL Antibiotics 9:E261-E261(2020).
RN [2] {ECO:0000313|EMBL:CAH1468039.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BB1542 {ECO:0000313|EMBL:CAH1468039.1};
RA Delgado-Blas J.;
RL Submitted (JAN-2022) 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; OV753987; CAH1468039.1; -; Genomic_DNA.
DR EMBL; CP063023; QOU76577.1; -; Genomic_DNA.
DR RefSeq; WP_004176294.1; NZ_WXZN01000064.1.
DR KEGG; kpnk:BN49_2681; -.
DR Proteomes; UP000438340; Chromosome.
DR Proteomes; UP001158595; 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:QOU76577.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:CAH1468039.1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:CAH1468039.1}; Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 265
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 495 AA; 56469 MW; C886C3CA9202BC4A CRC64;
MTENTPYQQL TRTFQRLSRF SHLAAIAGWD MFAMMPPGGS VARSEALAEL GVLQHQILTD
KKVGQWLQEA RQQDLNDVEQ ANLREMQRQY DQAALLPESL VEAKSLAGSR CEHAWRSQRP
ANDWTGFADN LREVVRLSRQ EAQIRADARG GSRYDALLDI FEPDMTSARL DSLFADLKSW
LPSLLSQAVE KQAKQTLIAP QGPFPIAEQR ELGLQAMRIL GFDFDGGRLD ISAHPFCGGV
PQDVRITTRY NENDLLSALF GVIHETGHAR YEQNLPRPWV DQPVGLARST AIHESQSLFF
EMQLGRSERF LNRLLPAVRE RFGDRPAFSQ DNFVAWNQQV KPGFIRVDAD EVSYPAHVIL
RYEIERALID GEIEVDDIPS LWDEKMQHWL GLSTTGNYRD GCMQDIHWTD GGFGYFPSYT
LGAMYAAQLM AAARRALPTL DRDIEEGDFS ALFDWLRQNI WQHGSRFTTS QLIQQATGED
LNSRYFREHL TTRYL
//
