ID A0A2U1AYP2_9BACT Unreviewed; 296 AA.
AC A0A2U1AYP2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:PVY41461.1};
GN ORFNames=C8D82_11475 {ECO:0000313|EMBL:PVY41461.1};
OS Victivallis vadensis.
OC Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC Victivallis.
OX NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY41461.1, ECO:0000313|Proteomes:UP000245959};
RN [1] {ECO:0000313|EMBL:PVY41461.1, ECO:0000313|Proteomes:UP000245959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY41461.1,
RC ECO:0000313|Proteomes:UP000245959};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-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:PVY41461.1}.
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DR EMBL; QEKH01000014; PVY41461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1AYP2; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000245959; 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:PVY41461.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000245959};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 10..122
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 180..280
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 296 AA; 32146 MW; EB661B086CD6C393 CRC64;
MLIPETFRRI GVFAPAGKLA PELFQSGAEL LEAEGKSVRV APHVRQEYPV RYLAASAESR
AEELTRLWLD PETDLLLAAR GGFGCAHLLP LLDWKQLATR PELPLVGYSD VTVLHYAMLK
TGAGTPVIGP MLGKLAQAAD DPYTAGHFRK ALLKTPREVE APPEFGPVHI LKPGNAQGLP
LPGNLAVAAT LAGTGFLPDP AGKILFFEDL NEPVYKLDRY LTQLEQAGFL RNAAGIVFGQ
FSDCAPPEEL ERLFGEVAAR FGGPVRMNFP FGHVFPFASL NCRQLVALES DRICCC
//
