ID M1P5D5_BARAA Unreviewed; 874 AA.
AC M1P5D5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:AGF75050.1};
GN OrderedLocusNames=BAnh1_11830 {ECO:0000313|EMBL:AGF75050.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF75050.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF75050.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF75050.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
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:0000256|ARBA:ARBA00001372, 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 family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP003123; AGF75050.1; -; Genomic_DNA.
DR RefSeq; WP_015398553.1; NC_020300.1.
DR AlphaFoldDB; M1P5D5; -.
DR STRING; 1094489.BAnh1_11830; -.
DR KEGG; baus:BAnh1_11830; -.
DR PATRIC; fig|1094489.3.peg.1447; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000011729; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 38..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..417
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 435..591
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 598..671
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 715..838
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 874 AA; 99243 MW; 34651FCACA60F992 CRC64;
MTIERYNPRA QEQKWQAIWD EKKIFQITPD DEREKYYVLE MFPYPSGRIH MGHVRNYAMG
DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKL WTYQNIAVMR TQLKRLGFSL
DWSREFATCD VDYYHRQQIL FLDLYNKGLI TRKVAKVNWD PVDQTVLANE QVVDGRGWRS
GALVEQRELT QWFFKISDFS EDLLARLEEL DKWPEKVRIM QKNWIGKSRG LFIRWALHKT
DIADDSCSTF DEIVCYSTRP DTLFGASFLA LSVDHPIAQA LAQKNEELEA FIARCRCGAT
TTAALEKVEK EGFRTSLLAI HPFNPAVRIP VYVANFVLMS YGTGAIFGCP AHDQRDLDFA
RKYALPVRPV VLPKDADVKD FVISETAYTG DGVMINSDFL NGLTPQEAFE ASAKKLEEQL
LNNQPQGQKT IQFRLRDWGI SRQRYWGCPI PMIHCAVCGV VPAPRADLPV VLPDDVAFDQ
PGNPLARHEA WQTVACPSCG RSAKRETDTM DTFVDSSWYY ARFTNPWAQE PVDQKAAAQW
LPVQQYIGGI EHAILHLLYA RFFMRAMKSA GYVAGDEPFE GLFTQGMVVH ETYRDDQGWV
SPMEVSIIEK EGKRHAYKLT DQSEVTIGPI EKMSKSKKNV VDPDDIIASY GADTVRWFVL
SDSPPERDII WTESGVEGAH RFVQRIWRSV ALSASVLREV VPRTGRQGAA LELSKVVHRT
LCAVEDDLEK LAFNRAIARL YELLNIMAPF LNKIENAEDE MKSALRQAMD FFLAMIAPMM
PHLAEECHAE LGKKTLISQC PWPAYDPALI VEDSITLPVQ INGKKRGDVT VAVTADKEAI
EEAVLALGFV RAQLVEKPVK KIIIIPQRIV NVVV
//
