TILS_RICRS
ID TILS_RICRS Reviewed; 478 AA.
AC A8GQJ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; OrderedLocusNames=A1G_00420;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01161}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01161};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
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:0000255|HAMAP-Rule:MF_01161}.
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DR EMBL; CP000848; ABV75672.1; -; Genomic_DNA.
DR RefSeq; WP_012150294.1; NC_009882.1.
DR AlphaFoldDB; A8GQJ7; -.
DR EnsemblBacteria; ABV75672; ABV75672; A1G_00420.
DR GeneID; 45538666; -.
DR KEGG; rri:A1G_00420; -.
DR HOGENOM; CLU_018869_3_2_5; -.
DR OMA; YKRTLYR; -.
DR Proteomes; UP000006832; 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; IPR005728; Rickett_RPE.
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 PANTHER; PTHR43033; PTHR43033; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
DR TIGRFAMs; TIGR01045; RPE1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT CHAIN 1..478
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_1000065626"
FT BINDING 27..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 478 AA; 55503 MW; 87766C23E283F81E CRC64;
MLYEKFEYNI NNLIGNFSLS KISIAVSGGS DSVALLYLAN IWAEKNNIEL FVISVDHNLR
EQSKQETHYI QNISNSLNRK HYSLSFDHQN NFSNLQERAR EGRYDLMTNL CLELDILVLL
TAHHEDDYVE NFCLRLERNS GIFGLSSSNI NWYNNIHIIR PLYNIPKSEL VEYLVSHNIK
WFEDESNSSD KYRRNVIRQK LAKGADYIRH FSKPVYREEF KGDTERSTAA YTSVREDAST
GTASKLSLEA KCGKMSKAAI ISQQLKTNKR IENEFKPELI SAIAEAVKIF EYGFAFLDLV
KFDKFSNEVK VQIINFLLII ISGQSRAARF YSVEPILKLI TQDVNFKNTL HGCIIKRIQN
ELLIYREFGK KLPESKILLD KSVIWDNRFC ITKNQEAPNC FVTHLSLKDY KIIKKQLDLE
PLKNLSCKNH NAVLLTLPII KILEKVIAIP HISYYDNDMW NFEVSFSPNF VSRFTHFC