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Database: UniProt
Entry: A0A402AGB3_9CHLR
LinkDB: A0A402AGB3_9CHLR
Original site: A0A402AGB3_9CHLR 
ID   A0A402AGB3_9CHLR        Unreviewed;       391 AA.
AC   A0A402AGB3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:GCE18129.1};
GN   ORFNames=KDK_19290 {ECO:0000313|EMBL:GCE18129.1};
OS   Dictyobacter kobayashii.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Dictyobacter.
OX   NCBI_TaxID=2014872 {ECO:0000313|EMBL:GCE18129.1, ECO:0000313|Proteomes:UP000287188};
RN   [1] {ECO:0000313|Proteomes:UP000287188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno11 {ECO:0000313|Proteomes:UP000287188};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:GCE18129.1}.
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DR   EMBL; BIFS01000001; GCE18129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402AGB3; -.
DR   Proteomes; UP000287188; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03885; M20_CPDG2; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:GCE18129.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:GCE18129.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287188};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          188..287
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ   SEQUENCE   391 AA;  42420 MW;  722582CEA5E796A8 CRC64;
     MSQTATYAQS YLSSFQSYQK EYFQRLETLV NIDSGTGQVE GVNSIMDTLQ QWLGEYDFKV
     SLHPSKGYGN NLLARRKGNG KRRILIMGHV DTVYPAGAVR KQPFAMNDGV AIGPGVLDMK
     SGVLLGVYAM RALIEAGFDQ YGELVLLFNN DEEVGSPGSN PLIREIAREV DYGLVLEPAG
     KQSSLTHSRK GTDKYVLEVQ GISAHSGVEP YKGRSAVIEL AYKILAIQNL HAIFPGVTFN
     VTKLNSTEPL NVIPDMARCS ISVRSFSRQG LDAAAAALQK VAATSNVPDT TTTLTRNPGR
     HPYEPTPEIQ WLVELARLEG EALGINLKAE PKGGVSDANI LIDAGIPTLD TLGPVGGGMH
     NLDREHMQVS SFMARGPLLA GLIQRICLHE K
//
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