ID A4Z1M8_BRASO Unreviewed; 418 AA.
AC A4Z1M8;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Putative carboxypeptidase G2 (Folate hydrolase G2) (Pteroylmonoglutamic acid hydrolase G2) (Glutamate carboxypeptidase) putative Peptidase family M20/M25/M40 {ECO:0000313|EMBL:CAL80054.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:CAL80054.1};
GN OrderedLocusNames=BRADO6431 {ECO:0000313|EMBL:CAL80054.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL80054.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL80054.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CU234118; CAL80054.1; -; Genomic_DNA.
DR RefSeq; WP_012029938.1; NC_009445.1.
DR AlphaFoldDB; A4Z1M8; -.
DR STRING; 114615.BRADO6431; -.
DR KEGG; bra:BRADO6431; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_2_5; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000001994; Chromosome.
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:CAL80054.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAL80054.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:CAL80054.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001994};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002678018"
FT DOMAIN 215..316
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 418 AA; 44389 MW; 57876929E08DD1ED CRC64;
MTPSTSRLAA LVLLASSATV SAAYAAPDDK IRAAAEQAKP AVIDSLREMV LIESGSSDVE
GLKKMADLTE ARLKALGATT ERRKTTRGVG ADMVIGTFEG TGRRKLMLIA HMDTVYQPGI
LKTEPYHVEG DLIYGPGIAD DKGGIAVILH SLQILKDMGW RDYARLTVAF NPDEEVGSIG
SGEFIAELAD QHDVVLSCEP TAAKPAAPVD SLLLGASGTA TATMEVTGRA AHAGAAPERG
RNALIELSHQ LLQTRDIAKS IPGTQLNWTT ATAGTVRNQI PEKASAGGDV RLTVADGVEK
LQAALDETIK THLVPDTEVK VRIDKGRPPF IASERGRALG KEAQAIYAEM ERPLALVDMT
GGATDAGLAN RSGKAIVVES FGIAGFNYHA HNEYIDATTI VPRLYLMTRM LIEQGKKM
//