ID A0A1B9B1I7_9BACI Unreviewed; 312 AA.
AC A0A1B9B1I7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:OCA89843.1};
GN ORFNames=A8L44_02590 {ECO:0000313|EMBL:OCA89843.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA89843.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA89843.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA89843.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
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:OCA89843.1}.
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DR EMBL; MAYV01000001; OCA89843.1; -; Genomic_DNA.
DR RefSeq; WP_066101086.1; NZ_MAYV01000001.1.
DR AlphaFoldDB; A0A1B9B1I7; -.
DR STRING; 1743146.A8L44_02590; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000092673; 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:OCA89843.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000092673};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 16..133
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 180..295
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 211
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 312 AA; 34442 MW; 00AC1CF353793B78 CRC64;
MLEQLKPKRI KKGDTVGVIA PASPPKKEAL QKALSFLEQD LGLTVKMGSH IYKEYGYLAG
EDAERVEDLE AMFKDEDVKA IICACGGYGT ARIADAINYE VIRNNPKIFW GYSDITFIHT
AIRQKTGLVT FHGPMLASDL GNDDIHPRSK ESFKQLFQSE EVNYKEDISP LHPFIEGEAE
GELVGGNLSL ITTTLGTPFE IDTKGKLLLI EDIYEEPRNI DIFLNHLWLA GKLSDIAGLV
IGDFANCDPK SRRTLTLDEV LTHYTKLINK PAMSGFKIGH CNPHVGIPLG VKAKISTAEK
TLTIESGIAD EN
//
