ID A0A1M6T0M5_9FLAO Unreviewed; 318 AA.
AC A0A1M6T0M5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SHK50485.1};
GN ORFNames=SAMN05443634_101206 {ECO:0000313|EMBL:SHK50485.1};
OS Chishuiella changwenlii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chishuiella.
OX NCBI_TaxID=1434701 {ECO:0000313|EMBL:SHK50485.1, ECO:0000313|Proteomes:UP000184120};
RN [1] {ECO:0000313|Proteomes:UP000184120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27989 {ECO:0000313|Proteomes:UP000184120};
RA Varghese N., Submissions S.;
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; FRBH01000001; SHK50485.1; -; Genomic_DNA.
DR RefSeq; WP_072929023.1; NZ_FRBH01000001.1.
DR AlphaFoldDB; A0A1M6T0M5; -.
DR STRING; 1434701.SAMN05443634_101206; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000184120; 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:SHK50485.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 175..299
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 207
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 318 AA; 36302 MW; DE0CF0D657D20BC3 CRC64;
MIQPDFLKEG DKIAIVAPAK RMLNGELEEA IELIKSWKLV PVLGKNIYAE YDFGYRYAGT
DEMRTEDFQW ALDDHEIKAI WCARGGYGSV KIIDELDLTE FTKNPKWIIG YSDITVFHNH
FNRLGYQTLH AVTAKKLADT IYHPSSYQSV YDSLFGKDIH YSLTNHPYNK VGEAEGELIG
GNLSIVYSLL GSDSAIINPS NKILFLEDWF ENWYAVDRML MNLKRNGILK QVKGVILGSF
THMDTEEENA ENFNNAFDPK TYDIIHQFTK ELSVPVVFNF PAGHTGHNVA MKMGAKVQLK
ISSNSVNLHF IENQYETR
//
