ID   SYL_BARBK               Reviewed;         875 AA.
AC   A1UR39;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=BARBAKC583_0104;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000524; ABM45658.1; -; Genomic_DNA.
DR   RefSeq; WP_005765856.1; NC_008783.1.
DR   AlphaFoldDB; A1UR39; -.
DR   SMR; A1UR39; -.
DR   STRING; 360095.BARBAKC583_0104; -.
DR   EnsemblBacteria; ABM45658; ABM45658; BARBAKC583_0104.
DR   KEGG; bbk:BARBAKC583_0104; -.
DR   PATRIC; fig|360095.6.peg.104; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000643; 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; -; 2.
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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..875
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009295"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           633..637
FT                   /note="'KMSKS' region"
FT   BINDING         636
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   875 AA;  98727 MW;  DF9B351DA23E27B8 CRC64;
     MTIERYNPRA QEQKWQAIWD EKKIFQTSHE DEGEKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARYKRAK GMNVLHPMGW DAFGMPAENA AMQNKVHPKA WTYQNIAAMR KQLQKLGLSI
     DWSREFATCD VDYYHRQQMI FLDLYQKGLV VRKVAKVNWD PVDQTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITEFG EGLLARLDDL TEWPDKVRVM QKNWIGKSQG LYIRWALDKT
     QLPHNDGCEG FDEITCYSTR PDTLFGASFL ALSVDHPVAQ ALARNDEELR AFIEMCRCGS
     TTTEALETAE KQGFRTGVLA VHPLNPAVRL PVYIANFVLM DYGTGAIFGC PAHDQRDLDF
     ARKYDLPVQI VVAPKEAEEQ DFTLSDTAYT GDGVMINSDF LNGLTPKDAF EVVAQHLEKQ
     VLNGQPQGQK TVQFRLRDWG VSRQRYWGCP IPMIHCAACG VVPVPRADLP VVLPEDVTFD
     RPGNPLARHE TWQTVACPSC GQPAKRETDT MDTFVDSSWY YARFTAPWAQ EPTDQDIAAQ
     WLPVQQYIGG IEHAILHLLY ARFFMRAMKL AGHVNADEPF TGLFTQGMVV HETYRDAQGW
     VAPDEVSIVE QDGKRRAYKL TDQSEVTIGS IEKMSKSKKN VVDPDDIISS YGADTARWFM
     LSDSPPERDV IWSESGIEGA HRFVQRVWRC VALSAPILST IEPCAGHQGE ALELSKAAHR
     TLCAVEDDLE KLAFNRAVAR LYEFLNIMAP LLNTVADLDD EMKSALRQAM DFFCAMIAPM
     MPHLAEECHA ALGGKTLMSE CAWPVYDKAL IVEDSVTLPV QINGKKRGDV TVPVTADQAE
     IEQAVLALSF VQAQLAGKSV KKMIIVPKRI VNVVL