ID A8EXQ0_RICCK Unreviewed; 464 AA.
AC A8EXQ0;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN Name=dnaK {ECO:0000313|EMBL:ABV73133.1};
GN OrderedLocusNames=A1E_00925 {ECO:0000313|EMBL:ABV73133.1};
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613 {ECO:0000313|EMBL:ABV73133.1, ECO:0000313|Proteomes:UP000007056};
RN [1] {ECO:0000313|Proteomes:UP000007056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel {ECO:0000313|Proteomes:UP000007056};
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-2007) 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; CP000409; ABV73133.1; -; Genomic_DNA.
DR AlphaFoldDB; A8EXQ0; -.
DR STRING; 293613.A1E_00925; -.
DR KEGG; rcm:A1E_00925; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_0_5; -.
DR Proteomes; UP000007056; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT COILED 29..71
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 233
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 464 AA; 53518 MW; 656311E4957FEAE6 CRC64;
MPIGSGESRS NEIITLTSLV HSMLKSPLLK ELLSKAKEES KNLNNWQNAN IREIERKITD
ANCIDEQLQK KLVAATNKAE LVWREARKNN DYNLFKPHLQ KVLDYTKEVA KARADVFNCG
LYDSLIDMYD PSRKSNEIKQ FFSVLKKELR ELINKVLEKQ KGEKKLVKIS RLDPKMQKRI
GKRIMEIMQF DLAKGRLDES NHPFCSGTPN DIRLTTRYDK DNFISGLMGI IHETGHALYE
QNLPEMYKGQ PVGLAKGMAF HESQSLFMEM QVGRSREFTE FLAKLLHDEF NIKGEEYSAE
NLYRKITRVM PDFIRVDADE ITYPMHVILR FEIEELLING NLNLDDLPTF WDSNMVEYLG
IKPTSFSNGC LQDIHWSHGS FGYFPAYTNG AIIAAMMMKK VKEMHPNIKD DILNGDFSNL
NNYLNKNFRN LGSLNNSADL LKSASGEDKI NPEVYIKYLE GKYL
//
