ID A0A238VWW4_9FLAO Unreviewed; 325 AA.
AC A0A238VWW4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SNR38738.1};
GN ORFNames=SAMN06265371_102193 {ECO:0000313|EMBL:SNR38738.1};
OS Lutibacter agarilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR38738.1, ECO:0000313|Proteomes:UP000198384};
RN [1] {ECO:0000313|EMBL:SNR38738.1, ECO:0000313|Proteomes:UP000198384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR38738.1,
RC ECO:0000313|Proteomes:UP000198384};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZNT01000002; SNR38738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238VWW4; -.
DR Proteomes; UP000198384; 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:SNR38738.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198384};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 41..156
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 198..314
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 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 325 AA; 36853 MW; A8AC8C3AE7DCE66F CRC64;
MQKYGLFVRK VNSCFGFRNL QVDLVNLKMI QPTYLQKNDT VAIVSTARKI SLPEIQPAIE
LLKSWGLKVV VGETIGFEEH QFAGTDAQRT ADFQKMLDNQ KIKAIWCARG GYGTVRIIDK
LDFTEFKKNP KWMIGYSDIT VLHNHIHNLG FQTLHATMPL DVEKNQKKAL NSLKKSLFGK
PISYEINASE ENKTGKTEGI LVGGNLSMLY SLLGSETSIK TDGKILFIED LDEYLYHIDR
MLMNLKRNGY FNHLKGLVVG GMTDMHDNAI PFGKNAKKII LDIVSEFNFP IVFDFPAGHL
KDNRALVFGR KVELEVSEEK TSIKF
//
