ID A0A1M4YT02_9BACE Unreviewed; 302 AA.
AC A0A1M4YT02;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SHF08881.1};
GN ORFNames=SAMN05444405_10570 {ECO:0000313|EMBL:SHF08881.1};
OS Bacteroides luti.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHF08881.1, ECO:0000313|Proteomes:UP000184509};
RN [1] {ECO:0000313|EMBL:SHF08881.1, ECO:0000313|Proteomes:UP000184509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26991 {ECO:0000313|EMBL:SHF08881.1,
RC ECO:0000313|Proteomes:UP000184509};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQTV01000005; SHF08881.1; -; Genomic_DNA.
DR RefSeq; WP_073400216.1; NZ_FQTV01000005.1.
DR AlphaFoldDB; A0A1M4YT02; -.
DR STRING; 1297750.SAMN05444405_10570; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000184509; 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:SHF08881.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184509};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 16..130
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 175..290
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 33528 MW; 2EF4F815B3B2F09F CRC64;
MRTIQFPPYL QEGDRVTIIS PAGKIDKNFL KDAKKTLESW GLEVVISKHA AGEAGRFSGS
VKQRTADLQS AMDDESTKAI LCSRGGYGAI HLIDQIDFTK FRENPKWLLG YSDITLLHEL
LQYNGFASVH SPMARHLSVE PKDDVCSLHL KNLLFGELPT YQSPKHKLNI KGTAKGTLRG
GNLSVLYGLR GTPYDFPAEG TILFIEDIGE RPYHIDRMMN NLKLGGVLEK LSGLIVGQFT
EYEEDLSIGK EVYEMIADMV KPYGYPVCFN FPVGHVVNNV PLICGCETEL TVGNNGAELI
FK
//
