ID U7VDK0_9FUSO Unreviewed; 299 AA.
AC U7VDK0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=LD-carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0202_01202 {ECO:0000313|EMBL:ERT68878.1};
OS Cetobacterium somerae ATCC BAA-474.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT68878.1, ECO:0000313|Proteomes:UP000017081};
RN [1] {ECO:0000313|EMBL:ERT68878.1, ECO:0000313|Proteomes:UP000017081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT68878.1,
RC ECO:0000313|Proteomes:UP000017081};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERT68878.1}.
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DR EMBL; AXZF01000042; ERT68878.1; -; Genomic_DNA.
DR RefSeq; WP_023050741.1; NZ_KI518186.1.
DR AlphaFoldDB; U7VDK0; -.
DR STRING; 1319815.HMPREF0202_01202; -.
DR PATRIC; fig|1319815.3.peg.1155; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_0; -.
DR Proteomes; UP000017081; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000017081};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 10..126
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 173..286
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 204
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 299 AA; 33921 MW; 9BB8FFAB291E1FC4 CRC64;
MKRLKVGDTI GLVAPASSVN KDKLKSAIEN LEKLGFKVKV GKSVENIWYS FAGTDEERAT
DINNFFQDKD VDAIMCVRGG YGGIRMLSLL DYEVIKNNPK PFIGYSDVTS LHMAFFKKCN
LKTFHGPMAV SNFSEDYSLD TLDDFIKVMT SNESYTIKNF YEKIYFYNTL KGRGQLVGGN
LAVLVSNLGT EFDLEYDNKI LFLEDIGEST YKVDRMLWQL KNLGIFDKVS GIVLGDFKKC
DKSSEDDMSL QDVFYSHFKD LKKPVCYNLK SGHCTPMLTL EFGEILEIDG EKEEIIVIK
//
