ID   A0A417VSR2_9FIRM        Unreviewed;       340 AA.
AC   A0A417VSR2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 10.
DE   SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:RHV72146.1};
GN   ORFNames=DXB15_00710 {ECO:0000313|EMBL:RHV72146.1};
OS   Roseburia sp. OM02-15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=2292368 {ECO:0000313|EMBL:RHV72146.1, ECO:0000313|Proteomes:UP000285983};
RN   [1] {ECO:0000313|EMBL:RHV72146.1, ECO:0000313|Proteomes:UP000285983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM02-15 {ECO:0000313|EMBL:RHV72146.1,
RC   ECO:0000313|Proteomes:UP000285983};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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:RHV72146.1}.
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DR   EMBL; QULX01000001; RHV72146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A417VSR2; -.
DR   Proteomes; UP000285983; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd07062; Peptidase_S66_mccF_like; 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   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:0000313|EMBL:RHV72146.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:RHV72146.1}.
FT   DOMAIN          13..135
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          204..326
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        243
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        311
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ   SEQUENCE   340 AA;  38130 MW;  ADDC61A3D598EDE2 CRC64;
     MRYPEFLKKN GCIGFVAPSF GCNIEPYKTA FGHALDKFEK MGYRTELGPN CYEGCGIGIS
     NTPEKCGQEL MEYYCNDTSD VLISCGGGEL MCEDLPYVDF EKIKEAKPKW YLGYSDNTNM
     TFLLTTLCDV ASIYGPCAAA FGMEPWHPAI QDAFDVLTGE KLTIKGYDLY EKEGLKDEEN
     PLVPYNVTEP CIRKKVPDTD IKMEGRLVGG CLDVLTLLLG TKYDKVQEFT ERYKEDGIIW
     FIEACDLNVM GIRRALWQME QAGWFGHVKG FLIGRPYCNG EEFLGLDQYE AVTGILGKYN
     VPIIMDLDIG HIPPAMPLIC GSYAKVTSVG NDVEVEMEFN
//