(data stored in SCRATCH zone)

SWISSPROT: B7UJ89_ECO27

ID   B7UJ89_ECO27            Unreviewed;       437 AA.
AC   B7UJ89;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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:CAS07741.1};
GN   OrderedLocusNames=E2348C_0193 {ECO:0000313|EMBL:CAS07741.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07741.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07741.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07741.1; -; Genomic_DNA.
DR   RefSeq; WP_000176585.1; NC_011601.1.
DR   EnsemblBacteria; CAS07741; CAS07741; E2348C_0193.
DR   KEGG; ecg:E2348C_0193; -.
DR   HOGENOM; HOG000236507; -.
DR   KO; K04075; -.
DR   OMA; HGGRKLK; -.
DR   BioCyc; ECOL574521:E2348C_RS00995-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UJ89.
DR   SWISS-2DPAGE; B7UJ89.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995156};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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   437 AA;  48491 MW;  DA07EB8B0BC2194C CRC64;
     MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GVTLRAIHVH HGLSANADVW
     VKHCENICQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA FARTLLPGEV LVTAQHLDDQ
     CETFLLALKR GSGPAGLSAM AEVSAFAGTQ LIRPLLARTR GELEQWALAH GLRWIEDESN
     QDDSYDRNFL RLRVVPLLQQ RWPHFAEATA RSAALCAEQE SLLDELLADD LAHCQTPQGT
     LQIAPMLAMS DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRLGAFEI
     RRYQSQLWWI KSVAGQSETI VPWQTWLQPL ELPAGLGSVQ LTAGGDIRPP RADEAVSVRF
     KAPGLLHIIG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG ETLIAAAGVF VTQEGVAEGE
     NGVSFVWQKT LSQVKAG
//

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