ID B3RC58_CUPTR Unreviewed; 387 AA.
AC B3RC58;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Glutamate carboxypeptidase Peptidase, M20/M25/M40 family similar to Pseudomonas cpg2 {ECO:0000313|EMBL:CAQ72483.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:CAQ72483.1};
GN OrderedLocusNames=RALTA_B1901 {ECO:0000313|EMBL:CAQ72483.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ72483.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ72483.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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DR EMBL; CU633750; CAQ72483.1; -; Genomic_DNA.
DR RefSeq; WP_012356696.1; NC_010530.1.
DR AlphaFoldDB; B3RC58; -.
DR GeneID; 29764222; -.
DR KEGG; cti:RALTA_B1901; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_7_0_4; -.
DR BioCyc; CTAI977880:RALTA_RS24725-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 2.
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; 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.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:CAQ72483.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAQ72483.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:CAQ72483.1}.
FT DOMAIN 190..290
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 387 AA; 40805 MW; C08B260DAF927270 CRC64;
MQQSEAETQT AYAAVDWLAG QRPEMEALLG RIVDIDSGSR QEAGVAAVAQ TLRAHLDAAG
IATELHPVPG YGVLLDALVP GTADDAPVVL MGHMDTVYPA GTVARRPFRV EHGRAYGPGV
ADMKSGLVLN VFVAEALARC GGNTRPVRLF FSCDEEIGSP ATRERIMDVA RGAHAVFNAE
PGRVSGNLVT ERKGSMVVAF EVEGVAAHSG INHAHGASAI DALARKILAL HALTDPERGI
TTNVGQVQGG IVANMVAPHA KAELDVRYTA ETELDALYAT IREIIERESL PRTRGWITDT
RRTLPMARTP DALLALYQRG AQQLGFAVNG EFTGGAADSG LTASVGTPTL CGTGPVGGHP
HTEREYCELS TFVPRAQALA LAVIGLR
//
