ID B7C7J4_9FIRM Unreviewed; 326 AA.
AC B7C7J4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:EEC91302.1};
GN ORFNames=EUBIFOR_00141 {ECO:0000313|EMBL:EEC91302.1};
OS Holdemanella biformis DSM 3989.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemanella.
OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC91302.1, ECO:0000313|Proteomes:UP000004315};
RN [1] {ECO:0000313|EMBL:EEC91302.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91302.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC91302.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91302.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL Submitted (NOV-2008) 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:EEC91302.1}.
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DR EMBL; ABYT01000011; EEC91302.1; -; Genomic_DNA.
DR RefSeq; WP_003863958.1; NZ_DS996839.1.
DR AlphaFoldDB; B7C7J4; -.
DR STRING; 518637.EUBIFOR_00141; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_1_1_9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000004315; 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 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:EEC91302.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:EEC91302.1}.
FT DOMAIN 14..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 192..311
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 326 AA; 36703 MW; 03D700F5DE706EE3 CRC64;
MKYPKFLNEN NNTIGVCAMS SGVGHKLDSF DESMDYIQSF GFHIVESSSV RNDSEPSCDA
LTRVDELNAL VKDSSIGAVW LAAGGDFQFE TLPYIDFEWI EKNPKWYLGA SDPTNLLFPV
TCKCDLATVY GFNAGSFDAY GVNEYSNLCL DFLKGKNIEL HSSSLHQDVD FYNDGAPILN
TKTEYDGSCS VSGRLLGGCF ESINDMAGTP YDFVEEFNER YKSDGVIWFF DIFSMNSCDV
YRALLKMKYM GYFKYTKAIL VGRVLFKNVS DLIGYEEAFK RALPDIDVVF KMDIGHTYPH
MYVVNGAMAR VDICDGHGSI QYEMKE
//
