ID   SYL_BORA1               Reviewed;         885 AA.
AC   Q2KXE5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BAV2492;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ50102.1; -; Genomic_DNA.
DR   RefSeq; YP_787004.1; -.
DR   GeneID; 6266007; -.
DR   GenomeReviews; AM167904_GR; BAV2492.
DR   KEGG; bav:BAV2492; -.
DR   NMPDR; fig|521.1.peg.6; -.
DR   HOGENOM; Q2KXE5; -.
DR   OMA; Q2KXE5; ATREKEG.
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    885       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_1000009298.
FT   MOTIF        48     58       "HIGH" region.
FT   MOTIF       639    643       "KMSKS" region.
FT   BINDING     642    642       ATP (By similarity).
SQ   SEQUENCE   885 AA;  99022 MW;  A55D8D4B863156EF CRC64;
     MQERYQPNLV EAAAQQDWQA RDAYLVHESA KNADGSEKPK FYACSMLPYP SGKLHMGHVR
     NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMKA
     MGLAIDWSRE MCACDPAYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
     RGWRSGAPVE KREIPGYYLR ITDYADELLD QVKNGLPGWP ERVRVMQENW IGKSEGVRLA
     FPHDIKDENG QLIQDGKLFV FTTRADTVMG VTFCAVAPEH PLATLAARNN PALATFIEQC
     KLGGTTEAEI ATREKEGIPT GLSVKHPLTG QAVDLWVGNY VLMSYGDGAV MGVPAHDERD
     FAFARKYGLT IRQVIAQEGK TYSDQAWQEW YGDKQTGRTI NSGKYDGLST AEAVDAIAAD
     LNALGLGEKQ TTYRLRDWGI SRQRYWGTPI PIIHCQDCGP VPVPEQDLPV VLPDDLIPDG
     SGNPLAKNEA FLSCSCPACG KPARRETDTM DTFVDSSWYF MRYTSPGNDQ AMVDKRNDYW
     MPMDQYIGGI EHAVLHLLYA RFWTKVMRDL GMLKFDEPFT RLLCQGMVLN HIYSRRTPQG
     GIEYFWPEEV ENIYDAKGAI VGARLKSDGS EITYGGVGTM SKSKNNGVDP QSLIDTLGAD
     TARLFVMFAS PPEQTLEWSD SGVDGANRFL RRLWALAYDR RAAVARGLAS GYAWQDAPAP
     VKDLRRELYG LLKQAEYDYQ RIQYNTVVSA SMKMLNAIDN AQLPEGPAAD AAIAEGLGLL
     LRVLYPVVPH VTWHIWRDLG YAAELGDLLD APWPHVDEAA LIADEIELML QVNGKLRGAI
     RVAAQAAKED IEKIAVAQEE VARFLEGRPP KRVIVVPGKL VNVVG
//