ID A0A0U1NQC8_9BACI Unreviewed; 307 AA.
AC A0A0U1NQC8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=L,D-carboxypeptidase {ECO:0000313|EMBL:CRK80227.1};
GN Name=ykfA {ECO:0000313|EMBL:CRK80227.1};
GN ORFNames=BN000_00108 {ECO:0000313|EMBL:CRK80227.1};
OS Neobacillus massiliamazoniensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK80227.1, ECO:0000313|Proteomes:UP000199087};
RN [1] {ECO:0000313|Proteomes:UP000199087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LF1 {ECO:0000313|Proteomes:UP000199087};
RA Urmite Genomes;
RL Submitted (MAY-2015) 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; CVRB01000001; CRK80227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1NQC8; -.
DR STRING; 1499688.BN000_00108; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000199087; 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:CRK80227.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199087};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 15..131
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 111
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 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 307 AA; 33629 MW; 5248DCD83912C5F8 CRC64;
MNAVKPYRLQ QGDKVGVIAP ASPPNQENLE RGIAYLEDLG LRVKVGKNVS RINGYLAGLD
QERLDDLHEM FQDPEVKAVI CACGGYGTGR IAEQIDYELI KCNPKIFWGY SDITFLHTAI
RQKTGLITFH GPMLGSDIGK SDTHSLSKEG FKQLFEPSAF VYTDQVSPLE TLVEGEASGE
LVGGNLSLLV STLGTNFEID TKSKLLLIED INEEPRSVDR MLNQLYMAGK LKDANGILVG
DFCNCIAKRD LTLALDEVIA YYVKLANKPA LKGFLMGHCN PNISIPLGVP AKLNTLENRL
IVDSGIV
//
