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Database: UniProt
Entry: A0A0H4QMR2_9LACO
LinkDB: A0A0H4QMR2_9LACO
Original site: A0A0H4QMR2_9LACO 
ID   A0A0H4QMR2_9LACO        Unreviewed;       435 AA.
AC   A0A0H4QMR2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
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   ORFNames=ABM34_05565 {ECO:0000313|EMBL:AKP68406.1};
OS   Companilactobacillus ginsenosidimutans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1007676 {ECO:0000313|EMBL:AKP68406.1, ECO:0000313|Proteomes:UP000036106};
RN   [1] {ECO:0000313|Proteomes:UP000036106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EMML 3041 {ECO:0000313|Proteomes:UP000036106};
RA   Kim M.K., Im W.-T., Srinivasan S., Lee J.-J.;
RT   "Lactobacillus ginsenosidimutans/EMML 3141/ whole genome sequencing.";
RL   Submitted (JUL-2015) 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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000047, ECO:0000256|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|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       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
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DR   EMBL; CP012034; AKP68406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4QMR2; -.
DR   STRING; 1007676.ABM34_05565; -.
DR   KEGG; lgn:ABM34_05565; -.
DR   PATRIC; fig|1007676.4.peg.1103; -.
DR   OrthoDB; 9807403at2; -.
DR   Proteomes; UP000036106; 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; HUPs; 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   NCBIfam; TIGR02433; lysidine_TilS_C; 1.
DR   NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR   PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56037; PheT/TilS domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          361..428
FT                   /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00977"
FT   BINDING         22..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   435 AA;  50714 MW;  982FB08048968AAA CRC64;
     MVTNVRKILK QYHAHNVLIA VSGGVDSIVL TDIVSKIHPK NHMAVVNVDH DLRPESQSEV
     EFVKKFCEKS QLKFFTSKWD HHQSNLGMEA AARKFRYGYF KQVMDQYGFD TLLTAHHAND
     LSENILMKLI RSGNVYEVTS LKSHRDFGNG QLLRPLLGFS KNVIKQYANK HDLKHVQDET
     NFEDITMRNR LRNDIFPQLQ EENGQLLRHF KLFDEQAGAL IEIANQRFAE IASQMKLLST
     NGEITGNLLP VRQLTSNQQT LFWGYVFKQN LVELSISNKQ IQQIIDVVMG DKPNGTVNLE
     HSWNFTRIYD QFKISRIVGD SDFEIEIELG QKYSVNNKIF RLTISTEENA TFSVDEIPKH
     IILRTRQTGD RLTISPSEHQ KLSKRFINKK ISKEERNKIP ILLFDNQIIW VEKIYNLSDY
     LKKRRIFFKI DFDEV
//
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