ID A0A2N4XGX0_9BACT Unreviewed; 303 AA.
AC A0A2N4XGX0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:PLK45701.1};
GN ORFNames=C0V77_06150 {ECO:0000313|EMBL:PLK45701.1};
OS Emticicia sp. TH156.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Emticicia.
OX NCBI_TaxID=2067454 {ECO:0000313|EMBL:PLK45701.1, ECO:0000313|Proteomes:UP000234203};
RN [1] {ECO:0000313|EMBL:PLK45701.1, ECO:0000313|Proteomes:UP000234203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH156 {ECO:0000313|EMBL:PLK45701.1,
RC ECO:0000313|Proteomes:UP000234203};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) 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:PLK45701.1}.
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DR EMBL; PKRS01000002; PLK45701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4XGX0; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000234203; 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:PLK45701.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000234203};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 16..132
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 173..289
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 303 AA; 33311 MW; 17FA4FEB185D6D77 CRC64;
MKSLIVPPVL GKGDKVAILA LASKIDPADI QQAIEFMREN WQVDIITGDL VGAAYFDFAG
NDNIRAADFQ QALNDSSVKA IFSARGGYGS SRIIDKIDFS LFKQNPKWIV GFSDITAVHS
HIQSLGFQSL HAPMPKTFMK DNASLKSIEP FLFGKEAMYE VAAHQMNRTG EAEGLVTGGN
LCLLAHLIGS ASDINYDNKI LFIEDVGEYL YNIDRMMVQL KRAGKLKKLA GLIVGSFNDL
KENNEPFGKD AYEIIAEHVA EYNYPVCYGF PVGHDIANRA LACGRAAQLE VNEIGVRLLF
LNS
//
