TILS_NEIMB
ID TILS_NEIMB Reviewed; 426 AA.
AC Q4W568;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=tilS1 {ECO:0000255|HAMAP-Rule:MF_01161}; OrderedLocusNames=NMB1140;
GN and
GN Name=tilS2 {ECO:0000255|HAMAP-Rule:MF_01161}; OrderedLocusNames=NMB1178;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAY52148.1; -; Genomic_DNA.
DR EMBL; AE002098; AAY52164.1; -; Genomic_DNA.
DR RefSeq; YP_338291.1; NC_003112.2.
DR RefSeq; YP_338292.1; NC_003112.2.
DR AlphaFoldDB; Q4W568; -.
DR SMR; Q4W568; -.
DR STRING; 122586.NMB1140; -.
DR PaxDb; Q4W568; -.
DR EnsemblBacteria; AAY52148; AAY52148; NMB1178.
DR EnsemblBacteria; AAY52164; AAY52164; NMB1140.
DR KEGG; nme:NMB1140; -.
DR KEGG; nme:NMB1178; -.
DR PATRIC; fig|122586.8.peg.1443; -.
DR HOGENOM; CLU_018869_2_0_4; -.
DR OMA; PMPNQNA; -.
DR Proteomes; UP000000425; 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 SMART; SM00977; TilS_C; 1.
DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..426
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181734"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 426 AA; 47732 MW; 623B51BCD8212A9E CRC64;
MKDCFPQGLN GKKTAVALSG GLDSVVLLHL LVRAGKKGGF IPDALHIHHG LSPRADDWAD
FCQNYCDMLG VGLETVKVCV EKNGLGIEAA ARQKRYAAFA EKGFDVLALA HHRDDQIETF
MLAVARGGGL RALAAMPAVR PFGEKGIIWR PLLPFSRQDI WDYAQKHGLP NIEDESNTDT
AYLRNRFRHR ILPELSAQIP HFGRHVLNNV RALQEDLALL DEVVVQDCRW VCGAGYFDTA
RWLTFSPRRK THILRHFLKE NGIPVPNQNA LADIARVLTE AKTGRWNLQG FELHHYAGRL
FVFRLEKTDK LRFLKDRQIS GNLREILTGQ GFVLKRHPFG LPEHLLEQDG ILRTVAASDT
LAMGGIHKDV KKILQGKRVL PVLRPIWPLV ADSGNRPLAL ANCCADFQYS VSDGILPVHP
DFPILF
