ID A0A0L6CSH1_9RHOB Unreviewed; 380 AA.
AC A0A0L6CSH1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carboxypeptidase G2 {ECO:0000313|EMBL:KNX40463.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:KNX40463.1};
GN Name=cpg2 {ECO:0000313|EMBL:KNX40463.1};
GN ORFNames=ROTO_29700 {ECO:0000313|EMBL:KNX40463.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40463.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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:KNX40463.1}.
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DR EMBL; LGVV01000051; KNX40463.1; -; Genomic_DNA.
DR RefSeq; WP_050663822.1; NZ_LGVV01000051.1.
DR AlphaFoldDB; A0A0L6CSH1; -.
DR PATRIC; fig|74031.6.peg.3027; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000037046; 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:KNX40463.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KNX40463.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KNX40463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 183..268
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 380 AA; 40715 MW; 1161BD7B4CDD28AB CRC64;
MPSDPLKLPF DVDEMLCGLR PWIETESPTF DAAAVNRMMD LVQHDLATLG ARVERIPGRR
GLGDSVRATM PHPRAGEGGI LLLGHMDTVH PIGTLSTLPF RREGDICYGP GLMDMKGGNY
VYLDALRKIL QAGIETPLPV TVLFTPDEEI GTPSTRDLIE AEAKRHKYIL VPEPACPDGS
AVIGRYAIAR FNLTARGTPS HASWALSEGR SAIAEMARKV AEIEGFTTDD CSFSVGVIHG
GQWVNCVSST CDAEVLSMAK TQDLLEEGVQ RMLDLNGGDD AVRLEVRRGV TRPLWQEGQP
GTMAMLDVAR GIASEIGFDL PACSAGGGSD GNFTGALGLA TLDSIGVRGK GLHTLTEHIE
VASLEERAKL AAALFCRLGR
//
