ID A0A1T4K6L4_9BACT Unreviewed; 302 AA.
AC A0A1T4K6L4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SJZ38056.1};
GN ORFNames=SAMN04488132_101489 {ECO:0000313|EMBL:SJZ38056.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SJZ38056.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SJZ38056.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SJZ38056.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUWH01000001; SJZ38056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4K6L4; -.
DR STRING; 413434.SAMN04488132_101489; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000190888; 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:SJZ38056.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000190888};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 174..287
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 205
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; 33612 MW; 1D1426C447E67330 CRC64;
MIKIPPYLKK GDTIGIVCPS GQMPFEKAAT CIEVLKQWGY HVVVGKTLGS QFHYFSGTDE
ERLADLQQML DDDSINAILC GRGGYGMSRI VDQLDFSRFR KKPKWVIGFS DITVLHAHIY
NRHKTACLHA PMAGAFNEGE YENEFIQSLR KAIAGKKSSY SCAAHPFNRK GKAEGILIGG
NLSLIAHIIG SKSAFSTKGK ILFLEDVGEY IYNVDRMFIQ LKRSGMLDEL AGLIIGGFSE
MKDTLIPFGS DVFDLISEHV AGYDYPVCYD FPVSHERNNY ALKVGLEHTF HVTAGKVTLK
EI
//
