ID A0A1H1M081_9ACTN Unreviewed; 315 AA.
AC A0A1H1M081;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SDR80216.1};
GN ORFNames=SAMN04488543_0511 {ECO:0000313|EMBL:SDR80216.1};
OS Friedmanniella luteola.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Friedmanniella.
OX NCBI_TaxID=546871 {ECO:0000313|EMBL:SDR80216.1, ECO:0000313|Proteomes:UP000199092};
RN [1] {ECO:0000313|EMBL:SDR80216.1, ECO:0000313|Proteomes:UP000199092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21741 {ECO:0000313|EMBL:SDR80216.1,
RC ECO:0000313|Proteomes:UP000199092};
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; LT629749; SDR80216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1M081; -.
DR STRING; 546871.SAMN04488543_0511; -.
DR Proteomes; UP000199092; Chromosome i.
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 ECO:0000313|EMBL:SDR80216.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199092};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 16..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 181..294
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 315 AA; 33130 MW; 51908A9FC6F3856E CRC64;
MTGVDGLGPL VPGDRVALVA PAGPTPPEQL GRAEALLRSW GLEPVVFPGA RASHPRAPYL
AAEDAQRARD LEDAWCDATV AGVFALRGGY GSVRVLDRLD VQRMRAARPK PFYGSSDLTA
VHEWLREQLG VASWFTPMVG TTSVLDDAEA TASLRAAVLE GLAGRRWSAR AASVLVPGTA
TGTLIGGNAS LLAMTLGARR RPPLDHRGTI VLLEDVTEET YRIDGYLASL LRAGWFDGVV
GIALGSWQAC SPLPEIEALC RELLAPLGVP LVWELGFGHG PAAHSLPLGR RGTLVAEPGR
PPELVMAPEP AGAAA
//
