ID H0TX42_9BRAD Unreviewed; 376 AA.
AC H0TX42;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative carboxypeptidase G2 (Folate hydrolase G2 Pteroylmonoglutamic acid hydrolase G2 Glutamate carboxypeptidase) {ECO:0000313|EMBL:CCE11030.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:CCE11030.1};
GN ORFNames=BRAS3843_60002 {ECO:0000313|EMBL:CCE11030.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE11030.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCE11030.1}.
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DR EMBL; CAFK01000307; CCE11030.1; -; Genomic_DNA.
DR RefSeq; WP_008973540.1; NZ_CAFK01000307.1.
DR AlphaFoldDB; H0TX42; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000002686; 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:CCE11030.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCE11030.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:CCE11030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 182..272
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 376 AA; 40438 MW; C813191D925BFB66 CRC64;
MNPANLPFDV EAMLQGLRGW VECESPTWDA LAVERMLDLA ARDMAIMGAT IERIAGRQGF
AGCVRARFPH PKQGEPGILI AGHFDTVHPV GTIAKLPWRR EGNKCYGPGI FDMKGGNYLS
LEAIRQLLRA SLTTPLPITV LFTPDEEVGT PSTRDIIEAE ARRNKYVLVP EPGRPDNGVV
TGRYAIARFN LEATGRPSHA GARLSAGRSA IREMARQILV IDDMTTEDCT FSVGIVHGGQ
WVNCVATTCT GEALSMAKRQ EDLDHGVERM LALSGTTNDV TFKVTRGVTR PVWEPDSGTM
SLYDTARGVA EQLGMKLPHG SAGGGSDGNF TGALGIPTLD GLGVRGADAH TLNEHIEIDS
LVERGRLMAG LLATLE
//
