ID B8G8N9_CHLAD Unreviewed; 503 AA.
AC B8G8N9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=Cagg_1394 {ECO:0000313|EMBL:ACL24301.1};
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL24301.1, ECO:0000313|Proteomes:UP000002508};
RN [1] {ECO:0000313|Proteomes:UP000002508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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; CP001337; ACL24301.1; -; Genomic_DNA.
DR RefSeq; WP_012616665.1; NC_011831.1.
DR AlphaFoldDB; B8G8N9; -.
DR STRING; 326427.Cagg_1394; -.
DR KEGG; cag:Cagg_1394; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_1_0; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000002508; 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:ACL24301.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:ACL24301.1};
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 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 503 AA; 56845 MW; CF32B063BE956C50 CRC64;
MESRLQELRA RLLEIDDINS AAAVLGWDQS TYMPPGGAAA RARQLATLSR LAHVRSTDPA
LGALLAELMP YAEQLPYDHP DAALIRVAHR NYERMTRIPV ELASEIASHT AASYQAWTQA
RPANDFATML PYLERTLELS RRVADCFPGY DHPADPLIDF SDYGMRASEI RDLFARLRAG
LTPIIRAIVA QPPIDDSCLR KYYPRNDQLA FGEQIIRRFG YDFERGRQDL THHPFATKFS
IGDVRITTRI NEHDLGDGLF STLHESGHAM YEQGIDPAFE GTPLCNGVSA GVHESQSRLW
ENLIGRSRPF WEHFYPELQQ TFPQQLGNVS LDEFYRAINR VQPSLIRTDA DEVTYNLHVM
IRFDLELALL EGSLKITDLP EAWNARYAED LGVVVPDYRD GVLQDVHWFG GLIGGAFQGY
TIGNILSAQF LAAARSAHPE IDAEIGQGEF ATLHGWLREH IYRHGSVFTP AELIERATGR
SMQIEPYLQY LRQKYSAIYG IEL
//
