ID A0A317KIJ0_9ACTN Unreviewed; 309 AA.
AC A0A317KIJ0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:PWU53624.1};
GN ORFNames=DLJ46_00875 {ECO:0000313|EMBL:PWU53624.1};
OS Micromonospora globispora.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1450148 {ECO:0000313|EMBL:PWU53624.1, ECO:0000313|Proteomes:UP000245683};
RN [1] {ECO:0000313|Proteomes:UP000245683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2904 {ECO:0000313|Proteomes:UP000245683};
RA Carro L., Aysel V., Cetin D., Igual J.M., Klenk H.-P., Trujillo M.E.,
RA Sahin N.;
RT "Micromonospora globispora sp. nov. and Micromonospora rugosa sp. nov.,
RT isolated from marine sediment.";
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:PWU53624.1}.
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DR EMBL; QGSV01000036; PWU53624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317KIJ0; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000245683; 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:PWU53624.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000245683};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 18..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 182..295
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 309 AA; 32231 MW; 10CD5936BB9217DB CRC64;
MLTDDCLRPP VLRPGDTVML VSPSGPTRPE RVARGIELLT GWGLRPVLAP NAYARRGYLA
GGDELRAADL NTAFADPEVR GVICTRGGYG AQRVVDLIDM AAVRRDPKVV AGFSDITALQ
FALWRGARLA SVHGPGAAWL DDRTPPHSAE SLHTALMTTE PVTVAAVAEE ETVAVHVPGR
AEGPLLGGNL CLITASIGTP DMPDLTGAIL LIEEVQEPPY KVDRMLTHLR RCGALDGVAG
VAVGQFTDCA DAWDTTIVDV LTDRLADLGV PVLGGLPIGH GVGQLTVPVG TPATLDATAG
TLTASPAVR
//
