ID A0A2A8S980_9BACI Unreviewed; 343 AA.
AC A0A2A8S980;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:PEZ05080.1};
GN ORFNames=CN326_15160 {ECO:0000313|EMBL:PEZ05080.1};
OS Bacillus sp. AFS018417.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ05080.1, ECO:0000313|Proteomes:UP000220085};
RN [1] {ECO:0000313|EMBL:PEZ05080.1, ECO:0000313|Proteomes:UP000220085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ05080.1,
RC ECO:0000313|Proteomes:UP000220085};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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:PEZ05080.1}.
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DR EMBL; NTTM01000036; PEZ05080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8S980; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000220085; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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:SF4; CARBOXYPEPTIDASE-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:PEZ05080.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:PEZ05080.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220085}.
FT DOMAIN 14..135
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 209..328
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 343 AA; 39493 MW; 1CF1AFBD3475FCAE CRC64;
MLIKPKKLQP GDRVATVSPS WGGAGDPELR WRYEQGVKRL EEVFGLKVIP MPNSLKGEDY
LYKNPQARAA DLMTAFKDES IKGIFANIGG EDSIRLLPYI DFDVIRENPK IFMGYSDVTV
SHLFCHKAEI SSFYGPAILT DFAENVEMDP YTIEMVNRTL FSNEIIGEIQ PAKEWTSEYL
EWIEENKNRR RTMQKNLGYE VLQGSGVAQG HLIGGCIEVL ECAKGTELWP DKKYWNDSIL
FFETSEEKPE PNFIKYWLRN YAVQGILQKV NGIIFGKPLD EKYYDEYKEE IQKVMKEFNL
EDLPILYNLN FGHTEPKFIL PYGAMAEINC DKKTFTILES GVE
//
