ID A0A099JMQ4_9MICO Unreviewed; 388 AA.
AC A0A099JMQ4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:MBB5639861.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:MBB5639861.1};
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KGJ79415.1};
GN ORFNames=BJ997_000409 {ECO:0000313|EMBL:MBB5639861.1}, GY21_05230
GN {ECO:0000313|EMBL:KGJ79415.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ79415.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ79415.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ79415.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5639861.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5639861.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:KGJ79415.1}.
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DR EMBL; JPXF01000014; KGJ79415.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5639861.1; -; Genomic_DNA.
DR RefSeq; WP_035835612.1; NZ_JPXF01000014.1.
DR AlphaFoldDB; A0A099JMQ4; -.
DR STRING; 1001240.GY21_05230; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; 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:MBB5639861.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:MBB5639861.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:MBB5639861.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 186..279
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 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 388 AA; 39818 MW; ADF902367BC95248 CRC64;
MPDLIHTAEA HQTDILTDVH DLVGIESHSY DKSGLDRGLA HIDTLVRKHL GEPGESIRSD
GGALGDVLRL TYPGTGSGAV LVIAHYDTVW PTGTLAGWPV SSQTDAAGRS IETGPGIFDM
KTGLVQGIWA LKLLRESGKA YPTVTFLFNG DEEIGSLVSR PIIEEAARAA DAVLVLEPTS
DGAVKTGRKG VGIFKATATG VEAHAGLNPA DGASAIHALA AFVTAVSGIA DPDRGTTINV
GLISGGSGTN VVAGTAVADI DIRIEDPAEM ARVDAAFDAV ESADPRVTIT VDHGWNRPPM
SLTAPGERLL AVVQQSAADL GVELENVDVG GGSDANFVSA LGVPVLCGMG AVGHGAHARH
EFIYPDAIPL YTAITAGTLA RLADGLAV
//
