ID   SYL_BORAP               Reviewed;         840 AA.
AC   Q0SNR0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BAPKO_0261;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01518.1; -; Genomic_DNA.
DR   RefSeq; YP_709694.1; -.
DR   GeneID; 4227469; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0261.
DR   KEGG; baf:BAPKO_0261; -.
DR   NMPDR; fig|390236.5.peg.312; -.
DR   HOGENOM; Q0SNR0; -.
DR   OMA; Q0SNR0; YYLRFID.
DR   BioCyc; BAFZ390236:BAPKO_0261-MON; -.
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    840       Leucyl-tRNA synthetase.
FT                                /FTId=PRO_1000009299.
FT   MOTIF        44     55       "HIGH" region.
FT   MOTIF       617    621       "KMSKS" region.
FT   BINDING     620    620       ATP (By similarity).
SQ   SEQUENCE   840 AA;  98167 MW;  B488A7FF899B0BB3 CRC64;
     MSKYEFIKIE KKWQEFWDNN KTYKVIEDPN IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
     ATDIFARYKI LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP KKSTEENINK FKKQIKALGF
     AYDWDREIRT HDENYYKWTQ WIFLQLYKKG LAYAKEMPVW YCPELGTVLA NEEIIQTPNG
     PKSERGFHNV EKKYLRQWVL KITKYAERLL NDLEELEWPE SVKEMQRNWI GKSTGVEIDF
     EIEGYNDKIK VFTTRPDTIF GITYLVIAPE NKLVEKITKD NFKSNVLKYI KQEELKSDLK
     RTSLEKDKSG VFTGSYAFHP ITNVKIPIWV GSYVLGTYGS GAVMGVPAHD ERDFQFAKKY
     KLKILPVISK SGKNEILEKA FINDGISINS PDEFNNLKNS EVKDKVIKWL TKNKKGKETV
     TYKLRDWVFS RQRYWGEPIP ILFDKLGNAI PLEKNDLPLK LPETANYKPS GTGESPLSRI
     KNWVNVKDTD FTRETNTMPQ WAGSCWYYLR YLDPKNSKEF ANHKKIEYWM PVDLYIGGAE
     HTVLHLLYSR FWHKVLYDLG HVNTKEPFKK LINQGIITAF SYQKENGVLI PNDQVIEKDN
     KFFDKKDNKE VTQVIAKMSK SLKNVINPDG IIKEFGADSI RIYEMFMGPL TDSKPWNTKG
     IIGVFRFLNK IWNLREKELS KDNPPKEIMS QLHKVIKKVT EDTEKLNFNT AISAMMIFIN
     ELSKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGETPS LFKNSKWPKF DETLIIKETK
     EIVLQINGKI KDKILLNKET DEEELKEIAM ENSKIKSNLF NKKIVKIIVI KNKLVNIVIK
//