ID A0A1I0FZ29_9CLOT Unreviewed; 309 AA.
AC A0A1I0FZ29;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SET63795.1};
GN ORFNames=SAMN05660297_02999 {ECO:0000313|EMBL:SET63795.1};
OS Natronincola peptidivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=426128 {ECO:0000313|EMBL:SET63795.1, ECO:0000313|Proteomes:UP000199568};
RN [1] {ECO:0000313|EMBL:SET63795.1, ECO:0000313|Proteomes:UP000199568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18979 {ECO:0000313|EMBL:SET63795.1,
RC ECO:0000313|Proteomes:UP000199568};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOHU01000017; SET63795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0FZ29; -.
DR STRING; 426128.SAMN05660297_02999; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000199568; 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 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:SET63795.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199568};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 178..294
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 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 309 AA; 33615 MW; 5363EA18E35EBC9B CRC64;
MIKPKALTQG DTIGVIAPSS PATEDKVQLA VEELTKLGFK VKLTESCYAT HGYLAGSDEL
RAEDFNRMFN DKEVQGIICL RGGYGAMKIL HKIDQKAIKN NPKVFIGYSD ITSLHLLINQ
NCNLVTFHGP MAAADIAKGL DDFSKESFLK AVTKSEAMGL IGNPEDSKIE CIVKGEARGK
IVGGNLALVS GTMGTPYEID TRGKLLFLEE IGEEPYRVDR MLTQLALAGK LEDAEGVILG
DWNDCDPQKR QVSLSLMEVF EEIIVPYGKP TIYNLKAGHC TPKVTLPFGV EAALKATEGK
LYIEEAATS
//
