ID   TILS_BACSU              Reviewed;         472 AA.
AC   P37563; O31416;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=tRNA(Ile)-lysidine synthase;
DE            EC=6.3.4.19;
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE   AltName: Full=tRNA(Ile)-lysidine synthetase;
GN   Name=tilS; Synonyms=yacA; OrderedLocusNames=BSU00670;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=14527414; DOI=10.1016/s1097-2765(03)00346-0;
RA   Soma A., Ikeuchi Y., Kanemasa S., Kobayashi K., Ogasawara N., Ote T.,
RA   Kato J., Watanabe K., Sekine Y., Suzuki T.;
RT   "An RNA-modifying enzyme that governs both the codon and amino acid
RT   specificities of isoleucine tRNA.";
RL   Mol. Cell 12:689-698(2003).
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000269|PubMed:14527414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000269|PubMed:14527414};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05302.1; Type=Erroneous initiation; Evidence={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; D26185; BAA05302.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB11843.1; -; Genomic_DNA.
DR   PIR; S66097; S66097.
DR   RefSeq; NP_387948.1; NC_000964.3.
DR   RefSeq; WP_003243704.1; NZ_JNCM01000028.1.
DR   AlphaFoldDB; P37563; -.
DR   SMR; P37563; -.
DR   IntAct; P37563; 2.
DR   STRING; 224308.BSU00670; -.
DR   PaxDb; P37563; -.
DR   PRIDE; P37563; -.
DR   EnsemblBacteria; CAB11843; CAB11843; BSU_00670.
DR   GeneID; 936922; -.
DR   KEGG; bsu:BSU00670; -.
DR   PATRIC; fig|224308.179.peg.67; -.
DR   eggNOG; COG0037; Bacteria.
DR   InParanoid; P37563; -.
DR   OMA; QQYGMNA; -.
DR   PhylomeDB; P37563; -.
DR   BioCyc; BSUB:BSU00670-MON; -.
DR   BRENDA; 6.3.4.19; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR   PANTHER; PTHR43033; PTHR43033; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF09179; TilS; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..472
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181650"
FT   BINDING         25..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   472 AA;  53464 MW;  2723EEA0B6F4252D CRC64;
     MKSVKDFLNK HNLTLKGATI IVGVSGGPDS MALLHALHTL CGRSANVIAA HVDHRFRGAE
     SEEDMRFVQA YCKAEQLVCE TAQINVTAYA QEKGLNKQAA ARDCRYQFFE EIMSKHQADY
     LALAHHGDDQ VETMLMKLAK GTLGTGLAGM QPVRRFGTGR IIRPFLTITK EEILHYCHEN
     GLSYRTDESN AKDDYTRNRF RKTVLPFLKQ ESPDVHKRFQ KVSEALTEDE QFLQSLTKDE
     MNKVITSQSN TSVEINSSQL LALPMPLQRR GVQLILNYLY ENVPSSFSAH HIQQFLDWAE
     NGGPSGVLDF PKGLKVVKSY QTCLFTFEQW QCKNVPFEYQ ISGAADETAV LPNGYLIEAR
     HYADSPEEHG NAVFITSEKK VRFPLTIRTR KAGDRIKLKG MNGSKKVKDI FIDKKLPLQE
     RDNWPIVTDA SGEIIWIPGL KKSIFEDLVI PNSDRIVLQY RQHEKCRGQA KS