ID A0A3D9IT53_9BACL Unreviewed; 307 AA.
AC A0A3D9IT53;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:RED64934.1};
GN ORFNames=DFP95_102356 {ECO:0000313|EMBL:RED64934.1};
OS Cohnella lupini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED64934.1, ECO:0000313|Proteomes:UP000256869};
RN [1] {ECO:0000313|EMBL:RED64934.1, ECO:0000313|Proteomes:UP000256869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8236 {ECO:0000313|EMBL:RED64934.1,
RC ECO:0000313|Proteomes:UP000256869};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RED64934.1}.
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DR EMBL; QRDY01000002; RED64934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9IT53; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000256869; 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:RED64934.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000256869};
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 178..290
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 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 307 AA; 32910 MW; FC8F09CA4CB519EA CRC64;
MAIKPLALQQ GDTVGIVTLG SPLAAETIDA RIAYLRSLGL KVIVGRYVYA ANGFLAGTDQ
QRAEDLMAMF ANENVRLILP SRGGVGVEGV LPYLDYDFIR KNPKIVSGYS DITILLNVLA
QLSGIVTLHS LLLLDFKPET APYNFNQFFT ATSSVTVPRP IVNPPGKRLI GKVPGNVSGI
LVGGNLTSFV GSLGTPYEID TKGKILMLEE VHEPVNTVYR YVEQLKLAGK FADCRGIIMG
ECTGCEEAYG QTYEDLIDDF IVPLGKPLIT NLASGHGTLK AAIPIGAFVN MNGGTGTITL
LESAVRY
//
