ID A0A2T0TG27_9PSEU Unreviewed; 357 AA.
AC A0A2T0TG27;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA involved in peptidoglycan recycling {ECO:0000313|EMBL:PRY44636.1};
GN ORFNames=CLV43_102201 {ECO:0000313|EMBL:PRY44636.1};
OS Umezawaea tangerina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Umezawaea.
OX NCBI_TaxID=84725 {ECO:0000313|EMBL:PRY44636.1, ECO:0000313|Proteomes:UP000239494};
RN [1] {ECO:0000313|EMBL:PRY44636.1, ECO:0000313|Proteomes:UP000239494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44720 {ECO:0000313|EMBL:PRY44636.1,
RC ECO:0000313|Proteomes:UP000239494};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PRY44636.1}.
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DR EMBL; PVTF01000002; PRY44636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0TG27; -.
DR Proteomes; UP000239494; 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; 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 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:PRY44636.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000239494};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 30..149
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 224..340
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 357 AA; 37340 MW; 11D8FFC4627D685B CRC64;
MIGRGRGRPL DYVDPMAVTF PAPLVPGDRI GVTAPSSGVP DDMKGRLDHA IRVVESHGYE
VVVGTCMDGS GHVSAPAAER AAELVAMLTD PAIKAVVPPW GGETAIDLLP LLDWDALRGA
EPTWVVGYSD ISTVITPLTL VTGVATVHGN NLMDTPYRTP EGLSSWLDVV AAPAGSTLVQ
TPPGLHRTAG FDDYRLHPEV DRFVLDAPGR WTRLDGEGDV DVVGRLVGGC VETLCNLTGT
PFGDVAGFRR RSAPEGLIVY VEASDSDAAA ICRHLHGMRL AGFFDGAEAV LVGRTAAPAW
GALTQHAAVL DALGGLGVPI IADVECGHVA PFMPLVNGAL GRVVHTAGHD RLEQTLA
//
