(data stored in SCRATCH zone)

SWISSPROT: C8U304_ECO10

ID   C8U304_ECO10            Unreviewed;       860 AA.
AC   C8U304;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049,
GN   ECO:0000313|EMBL:BAI29512.1};
GN   OrderedLocusNames=ECO103_0649 {ECO:0000313|EMBL:BAI29512.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29512.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29512.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-
CC         leucyl-tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613,
CC         Rhea:RHEA-COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57427, ChEBI:CHEBI:78442, ChEBI:CHEBI:78494,
CC         ChEBI:CHEBI:456215; EC=6.1.1.4; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; AP010958; BAI29512.1; -; Genomic_DNA.
DR   RefSeq; WP_001157890.1; NC_013353.1.
DR   SMR; C8U304; -.
DR   EnsemblBacteria; BAI29512; BAI29512; ECO103_0649.
DR   KEGG; eoh:ECO103_0649; -.
DR   HOGENOM; HOG000200747; -.
DR   KO; K01869; -.
DR   OMA; ALSMFPY; -.
DR   BioCyc; ECOL585395:ECO103_RS03385-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U304.
DR   SWISS-2DPAGE; C8U304.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000313|EMBL:BAI29512.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00049,
KW   ECO:0000256|RuleBase:RU363035}.
FT   DOMAIN       15    171       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      221    403       tRNA-synt_1_2. {ECO:0000259|Pfam:
FT                                PF13603}.
FT   DOMAIN      417    572       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      618    651       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      701    821       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        42     52       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   MOTIF       619    623       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00049}.
FT   BINDING     622    622       ATP. {ECO:0000256|HAMAP-Rule:MF_00049}.
SQ   SEQUENCE   860 AA;  97236 MW;  24EE83E7719955B8 CRC64;
     MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKMLGFGYD
     WSRELATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
     TKVERKEIPQ WFIKITAYAD ELLNDLDKLD HWPDTVKTMQ RNWIGRSEGV EITFNVNDYD
     NTLTVYTTRP DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK
     KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLNIKPVI
     LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA DKLTAMGVGE RKVNYRLRDW
     GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
     MPALRETDTF DTFMESSWYY ARYTCPEYKE GMLDSEAANY WLPVDIYIGG IEHAIMHLLY
     FRFFHKLMRD AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
     IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
     SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDALTEDQKA LRRDVHKTIA KVTDDIGRRQ
     TFNTAIAAIM ELMNKLAKAP TDGEQDRALM QEALLAVVRM LNPFTPHICF TLWQELKGEG
     DIDNAPWPVA DEKAMVEDST LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD
     GVTVRKVIYV PGKLLNLVVG
//

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