ID A0A1H1MAA8_9CELL Unreviewed; 340 AA.
AC A0A1H1MAA8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SDR83305.1};
GN ORFNames=SAMN04489860_0173 {ECO:0000313|EMBL:SDR83305.1};
OS Paraoerskovia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Paraoerskovia.
OX NCBI_TaxID=545619 {ECO:0000313|EMBL:SDR83305.1, ECO:0000313|Proteomes:UP000185663};
RN [1] {ECO:0000313|EMBL:SDR83305.1, ECO:0000313|Proteomes:UP000185663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22126 {ECO:0000313|EMBL:SDR83305.1,
RC ECO:0000313|Proteomes:UP000185663};
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; LT629776; SDR83305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1MAA8; -.
DR STRING; 545619.SAMN04489860_0173; -.
DR eggNOG; COG1619; Bacteria.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000185663; 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; 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:SDR83305.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000185663};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..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"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 340 AA; 35734 MW; 10F8A12B80AB5565 CRC64;
MIRYPRPLAP GDTVGVTSPS AGVPDELSAR LAVAVTAVED RGFTVRVGDL MDGSGLTSGT
ADARGEELTA LMTNGDVRAV VPPWGGATAI DLLPRLDWDA LAADPTWLVG YSDVSTILLP
LTLRTGVATL YGQNLMDTPY RVPSPLLSWL DVATAPAGSV LTQGSAPFHR LSGFDDYATH
PAVAEYTLET PGGWRRLDGS GEVDVEGRLV GGCLETVSPL TGTPFGDVSA FAEQHAPEGL
VVYLESSRSD ASDVSRMLLG LRYAGWFDHA NAVLLGTTRG EELPDLTHDD AARHALGDLG
IPLIGGVDCG HVPPHLALVN GSLARVVHSS ERSTIEQRLV
//
