ID A0A085JEK2_9GAMM Unreviewed; 494 AA.
AC A0A085JEK2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN Name=mcar-1 {ECO:0000313|EMBL:KFD18898.1};
GN ORFNames=GTPT_2199 {ECO:0000313|EMBL:KFD18898.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD18898.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD18898.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD18898.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-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}.
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:KFD18898.1}.
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DR EMBL; JMPR01000035; KFD18898.1; -; Genomic_DNA.
DR RefSeq; WP_025903131.1; NZ_JMPR01000035.1.
DR AlphaFoldDB; A0A085JEK2; -.
DR MEROPS; M32.003; -.
DR eggNOG; COG2317; Bacteria.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000028602; 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:KFD18898.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:KFD18898.1};
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:UP000028602};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 263
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 494 AA; 55959 MW; EEE11952C3A87A35 CRC64;
MNNAYTRLCQ RFRRLSRFGH LSAIAGWDMQ TMMPAGGSEA RGEALAELSL LQHQLLTDKE
NGDLLRAAAD LPLTPDERAN LQEMTRQWQQ AVLLPAELVE AKSIAGMRCE HAWRTQRQAN
DWQGFSENLR EVVRLSRQEA DIRATANGTS RYDALLDLYE PGMDSQQLDS VFNDLKQWLP
ALLTRVVEKQ SATRPRTPTG TFPPPLQKQL GLQVMQTLGF DFNHGRLDIS AHPFCGGVPE
DVRITTRYDE QHLLSALMGV IHETGHARYE QNLPKQWAGQ PAGLARSTAI HESQSLFMEM
QLGRSREFLE FIQPQVEAIF GSQPALEKDN FVALAQQVKP GFIRVDADEV SYPAHVMLRY
DIEKALIEGE IEVEDIPSLW DEKMHHYLGL DTRGNYREGC MQDIHWTDGA FGYFPTYTLG
AMYAAQLFAA AKQQLPAISE EIARGNLQNI SGWLNDHIWQ YGSLLTTDEL LTKATGQTLN
PAFFRQHLEQ RYCS
//
