(data stored in SCRATCH zone)

SWISSPROT: C8U1Q6_ECO10

ID   C8U1Q6_ECO10            Unreviewed;       432 AA.
AC   C8U1Q6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00052161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00360151};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161,
GN   ECO:0000313|EMBL:BAI29064.1};
GN   OrderedLocusNames=ECO103_0186 {ECO:0000313|EMBL:BAI29064.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29064.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29064.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_01161,
CC       ECO:0000256|SAAS:SAAS00557872}.
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-
CC         COMP:10670, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:33019, ChEBI:CHEBI:82748,
CC         ChEBI:CHEBI:83665, ChEBI:CHEBI:456215; EC=6.3.4.19;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01161,
CC         ECO:0000256|SAAS:SAAS01121949};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161,
CC       ECO:0000256|SAAS:SAAS00749588}.
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       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161, ECO:0000256|SAAS:SAAS00552175}.
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DR   EMBL; AP010958; BAI29064.1; -; Genomic_DNA.
DR   RefSeq; WP_000176573.1; NC_013353.1.
DR   EnsemblBacteria; BAI29064; BAI29064; ECO103_0186.
DR   KEGG; eoh:ECO103_0186; -.
DR   HOGENOM; HOG000236507; -.
DR   KO; K04075; -.
DR   OMA; HGGRKLK; -.
DR   BioCyc; ECOL585395:ECO103_RS00950-MONOMER; -.
DR   Proteomes; UP000000959; 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: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   TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1Q6.
DR   SWISS-2DPAGE; C8U1Q6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995156};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00749569};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054817};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995160};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00054814}.
FT   DOMAIN      356    427       TilS_C. {ECO:0000259|SMART:SM00977}.
FT   NP_BIND      20     25       ATP. {ECO:0000256|HAMAP-Rule:MF_01161}.
SQ   SEQUENCE   432 AA;  48004 MW;  87608A0D9F7B38F3 CRC64;
     MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GVTLRAIHVH HGLSANADAW
     VTHCENVCQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA FARTLLPGEV LVTAQHLDDQ
     CETFLLALKR GSGPAGLSAM AEVSEFAGTR LIRPLLARTR GELEQWALAH GLRWIEDESN
     QDDSYDRNFL RLRVVPLLQQ RWPHFAEATA RSAALCAEQE SLLDELLADD LAHCQTSQGT
     LQIAPMLAMS DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRLGAFEI
     RRYQSQLWWI KSVTGQSETI VPWQTWLQPL ELPAGLGSVQ LTAGGDIRPP RADEAVSVRF
     KAAGLLHIVG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG ETLIAAAGVF VTQEGVAEGE
     NGVSFVWQKT LS
//

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