ID   SYL_BAUCH               Reviewed;         861 AA.
AC   Q1LTM9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Leucyl-tRNA synthetase;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucine--tRNA ligase;
DE            Short=LeuRS;
GN   Name=leuS; OrderedLocusNames=BCI_0232;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP +
CC       diphosphate + L-leucyl-tRNA(Leu).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000238; ABF13994.1; -; Genomic_DNA.
DR   RefSeq; YP_588685.1; -.
DR   GeneID; 4056741; -.
DR   GenomeReviews; CP000238_GR; BCI_0232.
DR   KEGG; bci:BCI_0232; -.
DR   HOGENOM; Q1LTM9; -.
DR   OMA; Q1LTM9; YYLRFID.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00049; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-synth_Ia_bac/mito.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF7; Leu_tRNAsyn_1a; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    861       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_1000009296.
FT   MOTIF        42     52       "HIGH" region.
FT   MOTIF       620    624       "KMSKS" region.
FT   BINDING     623    623       ATP (By similarity).
SQ   SEQUENCE   861 AA;  99335 MW;  151E545728E934B5 CRC64;
     MQEFYDPKNI ESTIQQYWHE NNTFTVTEDF SKEKYYCLSM LPYPSGNLHM GHVRNYTIGD
     VLSRYHRMLG KNVMQPIGWD AFGLPAERAA LKNQTAPATW TYANIETMKK QLKQLGFSYD
     WSREITTCRP EYYRWEQWFF IQLYEKGLVY KKTSFVNWCS NDQTVLANEQ VIDGCCWRCG
     APIMLKDIPQ WFLKITAYAD QLLHDLDKLD GWPEQIKNMQ RNWIGRSEGI NITFQVIDMK
     ETLTIYTTRP DTLMGVTYLS IAINHHLAQQ AANNNRLLSD FIEHSRPTKL SEAEIVKVNR
     VKTGIFTGLY AIHPLTEEKL PIWVTNFVLM DYGTGAIMAV PGHDQRDWDF ARQYNLPVKN
     IIRNIDGSKP TISGIIPEGI LYNSGEFNGL RSLEASKIIT DILVARGIGE TKVNYRLRDW
     VISRQRYWGT PIPMMTLEDG TVVPTPVDQL PVILPEYLLI NSISNPLKDD HLWMKTNYNN
     NIATRETDTF DTFMESSWYY ARYTCPNYDQ GMLDTTAANY WLPIDQYIGG IEHAIMHLMY
     FRFYHKLLRD AGMLTSDEPT IRILCQGMVL ADSFYYISCT TGERIWVSPI NVRVQRDEKG
     NIINAIDLQG HHLVYAGTIK MSKSKNNSID PLTMVEKYGA DTIRLFIMFA SPVTMALEWR
     ESGVEGANRF LKRLWKLTYD HIQRGKVIKL DLAAMSNDNK ILRRELHQTI AKVTDDISRR
     YAFNTAIAAL MEITNKLMHA SYHSQQDRAI VQEALLAVVR MLYPFTPHLC FKLWQALNGE
     GDIDNAPWPI VDQLALVEDT NLIVIQINGR FRSKIIVPVS ADKALIIERA SKEKLVAKYL
     EGTKVQKIIY VPGKLLNLVL K
//