GenomeNet

Database: UniProt
Entry: A0A248KJU7_9ENTR
LinkDB: A0A248KJU7_9ENTR
Original site: A0A248KJU7_9ENTR 
ID   A0A248KJU7_9ENTR        Unreviewed;       435 AA.
AC   A0A248KJU7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
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=CEW81_20085 {ECO:0000313|EMBL:ASG64085.1};
OS   Kluyvera genomosp. 3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kluyvera.
OX   NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG64085.1, ECO:0000313|Proteomes:UP000197098};
RN   [1] {ECO:0000313|EMBL:ASG64085.1, ECO:0000313|Proteomes:UP000197098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YDC799 {ECO:0000313|EMBL:ASG64085.1,
RC   ECO:0000313|Proteomes:UP000197098};
RA   Ito R., Pacey M.P., Doi Y.;
RT   "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL   Submitted (JUN-2017) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP022114; ASG64085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248KJU7; -.
DR   KEGG; kgo:CEW81_20085; -.
DR   Proteomes; UP000197098; 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; 1.20.59.20; -; 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   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
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; PF09179; TilS; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF82829; MesJ substrate recognition domain-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   Reference proteome {ECO:0000313|Proteomes:UP000197098};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          359..430
FT                   /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00977"
FT   BINDING         23..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   435 AA;  48552 MW;  198F9751423D25B8 CRC64;
     MTMTPSSLVQ QLSPHRQFLV AFSGGLDSTV LLHQLVCWRR QEPGISLRAI HIHHGISQNA
     DSWVEHCQQL CAEWQVPLVV ERVTLRQSGA GLEAEARAAR YQAFREALLP GEVLLTAQHL
     DDQSETLLLA LKRGSGPAGL SAMPMSATFA DTLLIRPLLD ETRAALLQWA QRHGLRWIED
     ESNQDDAYDR NFLRLHVLPL LNARWPHFAE AAARSAALCG EQEQLLDELL ADELSRLLDE
     NGSLAIEPLL NMSGPKRAAL LRRWLAGLGA TMPSREMLTR LWQEVALARE DASPCLRLGD
     FDVRRFQQRL WWVKALPGQT DSEIVWQNLR APLVLPDGLG RVFLSPGGDI RPPHAGEPVT
     IRFKAPGMLH IVGRHGGRKL KKIWQELGVP PWLRDTTPLL FYGDTLMAAA GRFVTREGLC
     ETGEGVQLSW QKTGS
//
DBGET integrated database retrieval system