ID A0A060LU02_9BACI Unreviewed; 308 AA.
AC A0A060LU02;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:AIC93485.1};
GN ORFNames=BleG1_0877 {ECO:0000313|EMBL:AIC93485.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC93485.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC93485.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC93485.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; CP003923; AIC93485.1; -; Genomic_DNA.
DR RefSeq; WP_038477615.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060LU02; -.
DR STRING; 1246626.BleG1_0877; -.
DR KEGG; ble:BleG1_0877; -.
DR PATRIC; fig|1246626.3.peg.882; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000027142; 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:AIC93485.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027142};
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..291
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 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 308 AA; 33516 MW; 4E286F4E7F774286 CRC64;
MSIAPPRLNQ GDTVGIVTLG SPLSADTIRT RIDYLEQLGF NILLGESVFN RTGFLAGSAE
SRANDFMSMV LNPDVKWILP TRGGVGVAGM IPYLDFTQIR DNPKIISGYS DITILLNALY
QFANLITFQG LLLIDFRDST PAYNFDQFFS ATMNGNAPYL FLNPPGIPLQ GKVDGVGTGE
LIGGNLTSFV DSLGTPYEIN TRGKVIFLED THEATNTIYR YLAHLEAAGK FEDCEAILMG
TCTDCPVSYN TSYQDLIETF IVPLGKPLVT NIQSAHNYYK GTLPIGANVR VDGTNGTITV
LDNTVADR
//
