ID A0A1I2EKJ7_9BACT Unreviewed; 342 AA.
AC A0A1I2EKJ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SFE92921.1};
GN ORFNames=SAMN05216167_12246 {ECO:0000313|EMBL:SFE92921.1};
OS Spirosoma endophyticum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=662367 {ECO:0000313|EMBL:SFE92921.1, ECO:0000313|Proteomes:UP000198598};
RN [1] {ECO:0000313|EMBL:SFE92921.1, ECO:0000313|Proteomes:UP000198598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26130 {ECO:0000313|EMBL:SFE92921.1,
RC ECO:0000313|Proteomes:UP000198598};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLQ01000022; SFE92921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2EKJ7; -.
DR STRING; 662367.SAMN05216167_12246; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000198598; Unassembled WGS sequence.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:SFE92921.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198598};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 40..157
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 210..327
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 312
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 342 AA; 37395 MW; 444B21E77CEED939 CRC64;
MPSRRSFLRT TSLAPLLSLT TNQTAPTLIK PAKLRPGDTI GLFCPAAPAY SHETVKITQE
SLQALGFQTK LGPHIYDRYG YLAGRDADRV SDLHAFFNDQ SVKAVMAIHG GWGCARLLPL
LDYDLIQRNP KVLIGYSDIT ALLLAIYAKT GLVTMHGPVG SATFNTYTVD WFRRVLMEGE
TVTMRNPTDK GDNLTQTQDR ITTIRPGLAR GRLVGGNLTV LSHLVGSPYL PDWKNTILFL
EDTHEDIYRM DRMFTQLKLA GILNQIAGFV FGKCSDCGPG NGSYGSLTLD DVLTEYIIPL
DKPAYSGATI GHISNKFTVP LGIDTEIDAT AGTIRLLESA VS
//
