ID A0A1B6Y6Z9_9BACT Unreviewed; 340 AA.
AC A0A1B6Y6Z9;
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=LD-carboxypeptidase {ECO:0000313|EMBL:OAN60767.1};
GN ORFNames=A8B79_09625 {ECO:0000313|EMBL:OAN60767.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN60767.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN60767.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN60767.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN60767.1}.
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DR EMBL; LXYG01000018; OAN60767.1; -; Genomic_DNA.
DR RefSeq; WP_066223402.1; NZ_LXYG01000018.1.
DR AlphaFoldDB; A0A1B6Y6Z9; -.
DR STRING; 1849360.A8B79_09625; -.
DR InParanoid; A0A1B6Y6Z9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000078514; 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:OAN60767.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000078514};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 49..166
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 211..324
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 340 AA; 37071 MW; DD6692DF6312E933 CRC64;
MSLSRKQFLK NTSLASLGLV GLSKNSCEEE KTEVNELILP NAISWGSTIG LIAPASPIYD
ASQFDEMIIT LKSLGFNLKL GKHVQDQYGY LAGSDEDRAA DLVDMFKDSE IDAILCVRGG
WGCNRILDLI DYEAIKSNPK PLIGFSDITS LHNAVLSKTG LVSFHGPVGK SDWNDFTKES
FEKVLIKKEK QKYSLPSNQA DAFTITSGVA EGQLLGGNLS VLVAMMGSEY LPDFTNAILF
LEDVGEDVYR LDRMLTQLKL NGILDVISGF IFGKCTNCDA GANSLTLPQL LNDTIKPLKI
PAFYGAMISH EELNITIPVG LRGRMDADNK SFEVLSAAVK
//
