ID A0A1H7Q5A7_9ACTN Unreviewed; 340 AA.
AC A0A1H7Q5A7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SEL43046.1};
GN ORFNames=SAMN05660976_02422 {ECO:0000313|EMBL:SEL43046.1};
OS Nonomuraea pusilla.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46177 {ECO:0000313|EMBL:SEL43046.1, ECO:0000313|Proteomes:UP000198953};
RN [1] {ECO:0000313|EMBL:SEL43046.1, ECO:0000313|Proteomes:UP000198953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43357 {ECO:0000313|EMBL:SEL43046.1,
RC ECO:0000313|Proteomes:UP000198953};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; FOBF01000005; SEL43046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7Q5A7; -.
DR STRING; 46177.SAMN05660976_02422; -.
DR Proteomes; UP000198953; 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:SEL43046.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198953};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 206..326
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 340 AA; 36526 MW; 37905E6D8151FFF4 CRC64;
MRYPAPLRPG DLVGVTAPSS GVDENLRARL KVAVRTVEEH GYRVVVGDCM DGATLVSAPA
PERARELMAM LTDPEIKAVV PPWGGEMAID LLPLLDWDAL READPTWLVG FSDLSTIITP
MTLLTGTATI HGNNLMDTPY HTPEGLLSWL DIVAMPQGST FTQTPPNRYR AQGWDDYTGH
PEVRDLTLDT PGRWTRLDGD GDVRVEGRLI GGCVEMLCNL AGTPYGDVAS FARAAAPEGL
VVYVEAAEHD AATICRNLHG MRLAGFFTGA TAVLVGRTRA PGLGSLTQHE AVLDALGGLG
VPIIADVECG HVPPYLPLVN GARCRVTYTE DHQEITQTID
//
