ID A0A316EJ68_9BACT Unreviewed; 304 AA.
AC A0A316EJ68;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:PWK28889.1};
GN ORFNames=LV89_00442 {ECO:0000313|EMBL:PWK28889.1};
OS Arcicella aurantiaca.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcicella.
OX NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK28889.1, ECO:0000313|Proteomes:UP000245489};
RN [1] {ECO:0000313|EMBL:PWK28889.1, ECO:0000313|Proteomes:UP000245489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK28889.1,
RC ECO:0000313|Proteomes:UP000245489};
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 (MAY-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:PWK28889.1}.
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DR EMBL; QGGO01000002; PWK28889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316EJ68; -.
DR Proteomes; UP000245489; 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:PWK28889.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000245489};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 12..127
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 171..285
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 304 AA; 33890 MW; 7155A8579F2B0F8A CRC64;
MRPTPLQKGD SVGIVALACK VDFEMLKPSI ELMQEIWGLN VVIGESVMSA YHQFAGTDDV
RTEDFQLMLD NPEIKAIFSA RGGYGSSRLL DSIDFTDFQK SPKWVVGFSD ITAVLSHIHL
LDIESLHATM PKLFLQEGGE ESLESLRKVL FGEALNYEVN IHEMNRLGMA KGQLIGGNLA
ILSHITGSKS DINYDGKILF LEDVNEYLYS LDRMMIQLKR SGKLKNLAGL IVGHFSDCQD
NDVPFGKTAN EIIQEAVSTY NFPVCYGFPV GHEPENWAMP VGREVILEVK NDGVFLKDVN
KIQN
//
