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Database: UniProt
Entry: A0A0F0LBI7_9MICO
LinkDB: A0A0F0LBI7_9MICO
Original site: A0A0F0LBI7_9MICO 
ID   A0A0F0LBI7_9MICO        Unreviewed;       387 AA.
AC   A0A0F0LBI7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Carboxypeptidase G2 {ECO:0000313|EMBL:KJL30029.1};
DE            EC=3.4.17.11 {ECO:0000313|EMBL:KJL30029.1};
GN   Name=cpg2 {ECO:0000313|EMBL:KJL30029.1};
GN   ORFNames=RS83_01171 {ECO:0000313|EMBL:KJL30029.1};
OS   Microbacterium oxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL30029.1, ECO:0000313|Proteomes:UP000033640};
RN   [1] {ECO:0000313|EMBL:KJL30029.1, ECO:0000313|Proteomes:UP000033640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEL4b {ECO:0000313|EMBL:KJL30029.1,
RC   ECO:0000313|Proteomes:UP000033640};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL30029.1}.
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DR   EMBL; JYIW01000021; KJL30029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0LBI7; -.
DR   PATRIC; fig|82380.11.peg.1202; -.
DR   Proteomes; UP000033640; 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; 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:KJL30029.1};
KW   Hydrolase {ECO:0000313|EMBL:KJL30029.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:KJL30029.1}.
FT   DOMAIN          186..279
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ   SEQUENCE   387 AA;  39819 MW;  F664F75A22408661 CRC64;
     MLSVPTSEAV RNLEGSRFEL LEFLADLEHL VTIESPSADH DAVARSAVVL SDVIEHRLGR
     RPETLRIDGV DHVVLQGRDS RVLLLGHHDT VWPIGSLAEL PFTVDGGVIR GPGCFDMLVG
     VVQIVHALAM LRARHGDGVL DQVTVLVTGD EEVGSVTSRA LIESRATGCR AALVLEAAGP
     GGALKTERKG VSLYELEVLG RAAHSGLEPE RGINATVGVA HLVIALAALA DPAVGTTVTP
     TLMSSGTTGN TVPDRATVAV DVRATTIAEQ ERVDTAMREL RLGVEGATLV VHGGVNRPPL
     EAAASADLFA RAAALAADLG HPPLVGMAVG GASDGNFTAG AGVATLDGLG AVGGGAHARD
     EHAEVSAIQP RTELLAALVR DLISDGS
//
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