(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z5G9_SHISS

ID   Q3Z5G9_SHISS            Unreviewed;       432 AA.
AC   Q3Z5G9;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
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=mesJ {ECO:0000313|EMBL:AAZ86993.1};
GN   Synonyms=tilS {ECO:0000256|HAMAP-Rule:MF_01161};
GN   OrderedLocusNames=SSON_0201 {ECO:0000313|EMBL:AAZ86993.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86993.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86993.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86993.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86993.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ86993; AAZ86993; SSON_0201.
DR   KEGG; ssn:SSON_0201; -.
DR   HOGENOM; HOG000236507; -.
DR   KO; K04075; -.
DR   OMA; HGGRKLK; -.
DR   BioCyc; SSON300269:G1GL2-233-MONOMER; -.
DR   Proteomes; UP000002529; 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; Q3Z5G9.
DR   SWISS-2DPAGE; Q3Z5G9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161,
KW   ECO:0000256|SAAS:SAAS00995156};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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;  48119 MW;  87167D4F20FA9670 CRC64;
     MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GVTLRAIHVH HGLSANADAW
     VRHCENICQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA FARTLLPGEV LVTAQHLDDQ
     CETFLLALKR GSGPAGLSAM GEVSEFAGTR LIRPLLARTR GELEQWALAH GLRWIEDESN
     QDDSYDRNFL RLRVVPLLQQ RWPHFAEATA RSAALCAEQE SLLDELLADD LAHCQTSQGT
     LQIAPMLAMS DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRFGAFEI
     RRYQSQLWWI KSVTGQSETI VPWQTWLQPL ELPAGLGSVQ LTAGGDIRPP RADEAVSVRF
     KAPGLLHIVG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG ETLIAAAGVF VTQEGVAEGE
     NGVSFVWQKT LS
//

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