ID A0A378I252_9GAMM Unreviewed; 407 AA.
AC A0A378I252;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Carboxypeptidase G2 {ECO:0000313|EMBL:STX29259.1};
DE EC=3.4.17.11 {ECO:0000313|EMBL:STX29259.1};
GN Name=cpg2_2 {ECO:0000313|EMBL:STX29259.1};
GN ORFNames=NCTC13315_01797 {ECO:0000313|EMBL:STX29259.1};
OS Legionella beliardensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=91822 {ECO:0000313|EMBL:STX29259.1, ECO:0000313|Proteomes:UP000254968};
RN [1] {ECO:0000313|EMBL:STX29259.1, ECO:0000313|Proteomes:UP000254968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13315 {ECO:0000313|EMBL:STX29259.1,
RC ECO:0000313|Proteomes:UP000254968};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; UGNV01000001; STX29259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378I252; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000254968; 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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:STX29259.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:STX29259.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:STX29259.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254968};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 201..299
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 407 AA; 44341 MW; 7DEC0378C8EF2775 CRC64;
MNSTIKDLLL SLQENQPIMV EQLHQFCEIN SGTYNQTGLQ IMHQKLVDAF QPLADKVDSL
SLPGVTTMDM KGNITTLRSG DTLFIRKRPK LKRRILLAGH MDTVFSINHP FQKLTFINDN
HLNGPGVADM KGGLIVMLHA LSAFEQTKES KLVGWDVLIN ADEEIGSPAS SALFNDLASH
YQAGLVYEPA MDSDGTLAKN RKGSGKLTLL ATGKAAHAGR AFYDGRNAIC YLAEAVTAIH
ALNGKRDGVT INVGKIAGGT ALNIVPEKAI AKLDVRISQP NDEYWVRDEL NQIIQNLKHP
DYSLTVHGNF NRPVKRVSGG TERLYQRIKS VGQALGLTLN WQDSGGCCDG NNLAAQGLPV
IDTLGVRGGN IHSEDEFILI DSLVERARLS ALILMDLAQG GLEELII
//
