ID   A0A1I7K2N7_9BRAD        Unreviewed;       416 AA.
AC   A0A1I7K2N7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:SFU91681.1};
GN   ORFNames=SAMN05192541_107142 {ECO:0000313|EMBL:SFU91681.1};
OS   Bradyrhizobium arachidis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=858423 {ECO:0000313|EMBL:SFU91681.1, ECO:0000313|Proteomes:UP000199591};
RN   [1] {ECO:0000313|EMBL:SFU91681.1, ECO:0000313|Proteomes:UP000199591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26795 {ECO:0000313|EMBL:SFU91681.1,
RC   ECO:0000313|Proteomes:UP000199591};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; FPBQ01000007; SFU91681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7K2N7; -.
DR   OrthoDB; 9776600at2; -.
DR   Proteomes; UP000199591; 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:SF10; BLL3749 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.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:SFU91681.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:SFU91681.1}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..416
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011694258"
FT   DOMAIN          213..314
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ   SEQUENCE   416 AA;  43868 MW;  116600D85B4CB089 CRC64;
     MTARSVSMLA VLGLVAASST ALAAADEKLK AAAEQEKAPL IETLREMVMT ESGSGDAEGL
     KKMADFTEAR LKALGASTER RKTTAGTRAD MVIATFKGSG TRKLMLIAHM DTVYQRGILA
     SEPYHVDGNR IYGPGIADDK GGIAVVLHAL KMLKDVGWKD YATLTVSFNP DEEVGSIGSG
     EIIAELADQH DVVLSCEPTA ASPPAKNDAL LLGASGTATA KMEVKGRASH AGAAPDLGRN
     ALIELAHQLL QAKDVAKSIP GTQLNWTTAQ AGTVRNQIPE KAEAGADVRL TIPDGVAKLQ
     AALDEKLKTK LVPDTETTVT IIAGRPPFVA SERGRALAQE GQAIYAEIDR KLDIAEMTGG
     GTDAGYASRS GKAVVVESFG LAGFGYHARD EFIDTNSIVP RLYLMSRMLI EQGKKK
//