ID A0A1D2LEM5_BROTH Unreviewed; 282 AA.
AC A0A1D2LEM5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ATF26315.1};
GN ORFNames=CNY62_07955 {ECO:0000313|EMBL:ATF26315.1};
OS Brochothrix thermosphacta (Microbacterium thermosphactum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF26315.1, ECO:0000313|Proteomes:UP000243591};
RN [1] {ECO:0000313|EMBL:ATF26315.1, ECO:0000313|Proteomes:UP000243591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI {ECO:0000313|EMBL:ATF26315.1,
RC ECO:0000313|Proteomes:UP000243591};
RA Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT Brochothrix thermosphacta Isolated from Ground Chicken.";
RL Submitted (SEP-2017) 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; CP023483; ATF26315.1; -; Genomic_DNA.
DR RefSeq; WP_069125780.1; NZ_RSDU01000006.1.
DR AlphaFoldDB; A0A1D2LEM5; -.
DR GeneID; 66536986; -.
DR KEGG; bths:CNY62_07955; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000243591; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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:0000313|EMBL:ATF26315.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:ATF26315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243591}.
FT DOMAIN 8..126
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 169..280
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 282 AA; 31116 MW; 68919E2C90849A07 CRC64;
MLVKGDSIGL IACSNARPSR YEEKIKNVEG FITALGINIV RAETLLETDE KTTSAPQARA
LELHKLYDNE KIKLIFDISG GDLANQILPF LDFERITAAN KPFVGLSDLT TVLNAVLQQT
NQKNYYFQLM TLAGTKAVEQ QNFFKEYFVE GHETIIETRG LTDFKEIVGK MYGGNIRCLL
KLAGTSFWPE FKGNIILLEG FSGSYERNAS YIAQLQQLGV FTDCIGIVLG TFTELDQKNT
TLIESLILAA VPDDLPVART SEVGHGDDGK AIVLGHTITI RG
//
