ID A0A0U2YNT9_9BACL Unreviewed; 307 AA.
AC A0A0U2YNT9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ALS76282.1};
GN ORFNames=AUC31_14240 {ECO:0000313|EMBL:ALS76282.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS76282.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS76282.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS76282.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-2016) 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; CP013659; ALS76282.1; -; Genomic_DNA.
DR RefSeq; WP_058382984.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2YNT9; -.
DR STRING; 200991.AUC31_14240; -.
DR KEGG; prt:AUC31_14240; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000067683; Chromosome.
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:ALS76282.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000067683};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..130
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 178..293
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 307 AA; 34003 MW; EB1B835918E4D5E1 CRC64;
MRTMPKRLQK GDTVGIISPS SPPNLENLKK ALPFLEELGL KVKMGKSVEA KNGYLAGTDD
ERLADLHAMF EDPEVKGIIC AGGGYGAARY ADRIDYAMIK ENPKIFWGYS DVTFLHNAIG
MYAELVTFHG PMLASDVGKP EFHERSGRMF GQMFQPFELH YDETISELET LASGMADGEL
VGGNLSLIRG TLGTKFEIDT KDKILLIEDT GEEPYQVDEM LNQLKMARKF EQVAGIVIGD
FKNAEPKKPE QSWTLAQVLD DYFKDLDVPV VKGFKIGHCE PHFSVPLGVK ARLDADAKTL
TILPGVE
//
