ID A0A1C4LQL9_9ACTN Unreviewed; 329 AA.
AC A0A1C4LQL9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SCD75876.1};
GN ORFNames=GA0115240_122710 {ECO:0000313|EMBL:SCD75876.1};
OS Streptomyces sp. DvalAA-14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCD75876.1, ECO:0000313|Proteomes:UP000199020};
RN [1] {ECO:0000313|EMBL:SCD75876.1, ECO:0000313|Proteomes:UP000199020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCD75876.1,
RC ECO:0000313|Proteomes:UP000199020};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMCH01000213; SCD75876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4LQL9; -.
DR Proteomes; UP000199020; 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 ECO:0000313|EMBL:SCD75876.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199020};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 38..157
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 202..313
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 329 AA; 34652 MW; 7A4BAF763A7901EC CRC64;
MSAGSARTGP MSADPVRGQA RPVPGLIRPR RLVPGDRIGI VAPSGPVPRE RLDAGADILR
GWGLEPVVAP HVLDEHPFGY LAGGDRERAA DLTRTWCDPS LAAVLCARGG YGVQRMVDLL
DWPAMRAAPP KAFIGYSDIT ALHEAFATRL GLATLHGPMA ATEAFVKDDP SQDHLRRTLF
TPEQAQTLTS PTARTLVPGR AEGVTLGGCV SLLAADLGTP RGRRSAAGGI LVLEDVGEEA
YRLDRIVTQL LRAGWLDGVA GIVLGSWQEC GPYPEVRALL LDRLGGLGVP IVEEFGFGHC
PSTLTIPLGV PAVLDADAAT LTLEVPALV
//
