ID   DTD_BACAM               Reviewed;         147 AA.
AC   A0A023W421;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
DE            Short=DTD {ECO:0000255|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518};
DE   AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
GN   Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518};
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOTECHNOLOGY.
RC   STRAIN=A50;
RX   PubMed=25441601; DOI=10.1016/j.micres.2014.11.001;
RA   Geraskina N.V., Butov I.A., Yomantas Y.A., Stoynova N.V.;
RT   "The dtd gene from Bacillus amyloliquefaciens encodes a putative D-tyrosyl-
RT   tRNATyr deacylase and is a selectable marker for Bacillus subtilis.";
RL   Microbiol. Res. 171:90-96(2015).
CC   -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC       D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC       protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC       based rather than protein-based catalysis; rejects L-amino acids rather
CC       than detecting D-amino acids in the active site. By recycling D-
CC       aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC       counteracts the toxicity associated with the formation of D-aminoacyl-
CC       tRNA entities in vivo and helps enforce protein L-homochirality (By
CC       similarity). Upon expression in B.subtilis strain 168 confers
CC       resistance to D-Tyr and D-Asp, suggesting it acts on both of these
CC       amino acids (PubMed:25441601). {ECO:0000255|HAMAP-Rule:MF_00518,
CC       ECO:0000269|PubMed:25441601}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC         Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00518};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC         H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00518};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC       of the other monomer to allow specific chiral rejection of L-amino
CC       acids. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- BIOTECHNOLOGY: Confers the ability to grow in the presence of 20 mg/ml
CC       D-Tyr and 500 mg/ml D-Asp to B.subtilis, showing it can be used as a
CC       selective marker in bacteria that do not have a functional copy of this
CC       gene. Can also function in an E.coli MG1655 dtd deletion, although in
CC       this case it confers resistance to toxic amino acid D-Tyr but not D-Trp
CC       (D-Asp is not toxic in this experiment) (PubMed:25441601).
CC       {ECO:0000269|PubMed:25441601}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00518}.
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DR   EMBL; KJ499811; AHY24673.1; -; Genomic_DNA.
DR   RefSeq; WP_013353029.1; NZ_VRTX01000008.1.
DR   AlphaFoldDB; A0A023W421; -.
DR   SMR; A0A023W421; -.
DR   STRING; 692420.BAMF_2569; -.
DR   PATRIC; fig|1390.176.peg.648; -.
DR   eggNOG; COG1490; Bacteria.
DR   OMA; GVFQAHM; -.
DR   BRENDA; 3.1.1.96; 630.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043908; F:Ser(Gly)-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00563; Dtyr_deacylase; 1.
DR   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_sf.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; RNA-binding; tRNA-binding.
FT   CHAIN           1..147
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000441714"
FT   MOTIF           137..138
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   147 AA;  16019 MW;  ACA5A0C73571F29C CRC64;
     MKLVVQRVTD ASVTVDGAVA GRIGPGIMAL VGVTHEDTEE DAAYLADKIV NLRIFDDESG
     KMNLSLLDTG GEILSVSQFT LYGETKKGRR PNFMNAAKPD QALLLYEKWN ELLREKGVKV
     ETGIFGAMMD VQLTNSGPVT LIMDSKQ