(data stored in ACNUC7421 zone)

SWISSPROT: TILS_ECO57

ID   TILS_ECO57              Reviewed;         431 AA.
AC   Q8X8W8; Q7AHL7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 103.
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}; Synonyms=mesJ;
GN   OrderedLocusNames=Z0200, ECs0190;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34
CC       of the AUA codon-specific tRNA(Ile) that contains the anticodon
CC       CAU, in an ATP-dependent manner. Cytidine is converted to
CC       lysidine, thus changing the amino acid specificity of the tRNA
CC       from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}.
CC   -!- CATALYTIC ACTIVITY: (tRNA(Ile2))-cytidine(34) + L-lysine + ATP =
CC       (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; AE005174; AAG54490.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33613.1; -; Genomic_DNA.
DR   PIR; F85503; F85503.
DR   PIR; F90652; F90652.
DR   RefSeq; NP_308217.1; NC_002695.1.
DR   RefSeq; WP_000176537.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; Q8X8W8; -.
DR   SMR; Q8X8W8; -.
DR   STRING; 155864.Z0200; -.
DR   EnsemblBacteria; AAG54490; AAG54490; Z0200.
DR   EnsemblBacteria; BAB33613; BAB33613; BAB33613.
DR   GeneID; 913916; -.
DR   KEGG; ece:Z0200; -.
DR   KEGG; ecs:ECs0190; -.
DR   PATRIC; fig|386585.9.peg.293; -.
DR   eggNOG; ENOG4105D3U; Bacteria.
DR   eggNOG; COG0037; LUCA.
DR   HOGENOM; HOG000236507; -.
DR   KO; K04075; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; IPR020825; Phe-tRNA_synthase_B3/B4.
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:SF1; PTHR43033:SF1; 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   SUPFAM; SSF56037; SSF56037; 1.
DR   TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X8W8.
DR   SWISS-2DPAGE; Q8X8W8.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   tRNA processing.
FT   CHAIN         1    431       tRNA(Ile)-lysidine synthase.
FT                                /FTId=PRO_0000181690.
FT   NP_BIND      20     25       ATP. {ECO:0000255|HAMAP-Rule:MF_01161}.
SQ   SEQUENCE   431 AA;  47879 MW;  0BAC272BF7D69967 CRC64;
     MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GGALRAIHVH HGLSANADAW
     VTHCENVCQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA FARTLLPGEV LVTAQHLDDQ
     CETFLLALKR GSGPAGLSAM AEVSEFAGTR LIRPLLARTR GELAQWALAH GLRWIEDESN
     QDDSYDRNFL RLRVVPLLQQ RWPHFAETTA RSAALCAEQE SLLDELLADD LAHCQSPQGT
     LQIVPMLAMS DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRLGAFEI
     RRYQSQLWWI KSVTGQSENI VPWQTWLQPL ELPAGQGSVQ LNAGGDIRPP RADEAVSVRF
     KAPGLLHIVG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG ETLIAAAGGF VTQEGVAEGE
     NGISFVWQRN A
//

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