ID A0A291R0M5_9BACT Unreviewed; 302 AA.
AC A0A291R0M5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ATL49692.1};
GN ORFNames=COR50_01460 {ECO:0000313|EMBL:ATL49692.1};
OS Chitinophaga caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL49692.1, ECO:0000313|Proteomes:UP000220133};
RN [1] {ECO:0000313|EMBL:ATL49692.1, ECO:0000313|Proteomes:UP000220133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 {ECO:0000313|EMBL:ATL49692.1,
RC ECO:0000313|Proteomes:UP000220133};
RA Jin D., Kong X., Deng Y., Bai Z.;
RT "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT sludge.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP023777; ATL49692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291R0M5; -.
DR KEGG; cbae:COR50_01460; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000220133; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:ATL49692.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000220133};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 173..289
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 33913 MW; 1CDD8BDF496CCD29 CRC64;
MKIPPYLKKG DLIGITCASS KMELHQAEYA AKVLESWGFR VYLGITVGTS FHNFSAPDEL
RLEELQDMLD HPEIKAILFG RGGYGMICLL DQLNLNKFKK HPKWVCGYSD VTALHSHIYQ
KTGIATLHSP MCSGITQVTQ GNQYVQSLHD ALTGKKYKYE FAAHELNRPG KAKGHLVGGN
LTLLAGLCGS KSQAKTKGAI LFLEDIGEYR YSVDRMMYTL KRAGYLEDLA GMIVGSFTES
KDTQTPFGQN EFEIIHNIVQ EYDFPVCYNF PVGHQHENYA LKHGMMHELK IGADCLLREI
KN
//
