ID   YBAK_SALTY              Reviewed;         159 AA.
AC   P37174;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK;
DE            EC=4.2.-.-;
GN   Name=ybaK; OrderedLocusNames=STM0495;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3031310; DOI=10.1016/0022-2836(86)90358-x;
RA   Burns D.M., Beacham I.R.;
RT   "Identification and sequence analysis of a silent gene (ushA0) in
RT   Salmonella typhimurium.";
RL   J. Mol. Biol. 192:163-175(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Functions in trans to edit the amino acid from incorrectly
CC       charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Reaction mechanism involves exclusion of catalytic water
CC       from the active site and substrate-mediated catalysis: the sulfhydryl
CC       side chain of the Cys substrate acts as a nucleophile and attacks the
CC       carbonyl center of the ester bond, leading to the cleavage of the Cys-
CC       tRNA ester bond and formation of a cyclic cysteine thiolactone
CC       intermediate. In contrast, the INS editing domain of ProRS catalyzes
CC       Ala-tRNA(Pro) hydrolysis via nucleophilic attack by a catalytic water
CC       molecule (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prolyl-tRNA editing family. YbaK/EbsC
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X04651; CAA28349.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19449.1; -; Genomic_DNA.
DR   RefSeq; NP_459490.1; NC_003197.2.
DR   RefSeq; WP_000186618.1; NC_003197.2.
DR   AlphaFoldDB; P37174; -.
DR   SMR; P37174; -.
DR   STRING; 99287.STM0495; -.
DR   PaxDb; P37174; -.
DR   EnsemblBacteria; AAL19449; AAL19449; STM0495.
DR   GeneID; 1252015; -.
DR   KEGG; stm:STM0495; -.
DR   PATRIC; fig|99287.12.peg.529; -.
DR   HOGENOM; CLU_094875_1_1_6; -.
DR   OMA; PYDYVEH; -.
DR   PhylomeDB; P37174; -.
DR   BioCyc; SENT99287:STM0495-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd00002; YbaK_deacylase; 1.
DR   Gene3D; 3.90.960.10; -; 1.
DR   InterPro; IPR004369; Prolyl-tRNA_editing_YbaK/EbsC.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PIRSF; PIRSF006181; EbsC_YbaK; 1.
DR   SUPFAM; SSF55826; SSF55826; 1.
DR   TIGRFAMs; TIGR00011; YbaK_EbsC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..159
FT                   /note="Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK"
FT                   /id="PRO_0000168621"
FT   SITE            29
FT                   /note="Participates in proton transfer during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  17054 MW;  B5EBB03391F22D66 CRC64;
     MTPAVKLLEK NKIPFNIHTY DHDPNETNFG DEVVRKLGLN ADQVYKTLLV AVNGDMKQLA
     VAVTPVAGQL DLKKVAKALG AKKVDMADPM VAQRTTGYLV GGISPLGQKK RLPTLIDAPA
     RTFATIYVSG GKRGLDIELA ADDLAAILGA KFADIARRD