SYL_MYCTU
ID SYL_MYCTU Reviewed; 969 AA.
AC P9WFV1; L0T451; P67510; P71698;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 56.
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}; OrderedLocusNames=Rv0041;
GN ORFNames=MTCY21D4.04;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
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DR EMBL; AL123456; CCP42763.1; -; Genomic_DNA.
DR PIR; A70912; A70912.
DR RefSeq; NP_214555.1; NC_000962.3.
DR RefSeq; WP_003900794.1; NZ_NVQJ01000005.1.
DR PDB; 5AGR; X-ray; 1.30 A; A=309-513.
DR PDB; 5AGS; X-ray; 1.47 A; A=309-513.
DR PDB; 5AGT; X-ray; 1.45 A; A=309-513.
DR PDBsum; 5AGR; -.
DR PDBsum; 5AGS; -.
DR PDBsum; 5AGT; -.
DR AlphaFoldDB; P9WFV1; -.
DR SMR; P9WFV1; -.
DR STRING; 83332.Rv0041; -.
DR BindingDB; P9WFV1; -.
DR ChEMBL; CHEMBL4105844; -.
DR iPTMnet; P9WFV1; -.
DR PaxDb; P9WFV1; -.
DR DNASU; 887040; -.
DR GeneID; 45424000; -.
DR GeneID; 887040; -.
DR KEGG; mtu:Rv0041; -.
DR TubercuList; Rv0041; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR PhylomeDB; P9WFV1; -.
DR BRENDA; 6.1.1.4; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 3.
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; 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 PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..969
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152052"
FT MOTIF 78..89
FT /note="'HIGH' region"
FT MOTIF 739..743
FT /note="'KMSKS' region"
FT BINDING 742
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:5AGR"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:5AGR"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:5AGR"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:5AGR"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:5AGR"
FT HELIX 492..505
FT /evidence="ECO:0007829|PDB:5AGR"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:5AGR"
SQ SEQUENCE 969 AA; 107595 MW; A07C835FC1B428D8 CRC64;
MTESPTAGPG GVPRADDADS DVPRYRYTAE LAARLERTWQ ENWARLGTFN VPNPVGSLAP
PDGAAVPDDK LFVQDMFPYP SGEGLHVGHP LGYIATDVYA RYFRMVGRNV LHALGFDAFG
LPAEQYAVQT GTHPRTRTEA NVVNFRRQLG RLGFGHDSRR SFSTTDVDFY RWTQWIFLQI
YNAWFDTTAN KARPISELVA EFESGARCLD GGRDWAKLTA GERADVIDEY RLVYRADSLV
NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYADRLLDD LDVLDWPEQV
KTMQRNWIGR STGAVALFSA RAASDDGFEV DIEVFTTRPD TLFGATYLVL APEHDLVDEL
VAASWPAGVN PLWTYGGGTP GEAIAAYRRA IAAKSDLERQ ESREKTGVFL GSYAINPANG
EPVPIFIADY VLAGYGTGAI MAVPGHDQRD WDFARAFGLP IVEVIAGGNI SESAYTGDGI
LVNSDYLNGM SVPAAKRAIV DRLESAGRGR ARIEFKLRDW LFARQRYWGE PFPIVYDSDG
RPHALDEAAL PVELPDVPDY SPVLFDPDDA DSEPSPPLAK ATEWVHVDLD LGDGLKPYSR
DTNVMPQWAG SSWYELRYTD PHNSERFCAK ENEAYWMGPR PAEHGPDDPG GVDLYVGGAE
HAVLHLLYSR FWHKVLYDLG HVSSREPYRR LVNQGYIQAY AYTDARGSYV PAEQVIERGD
RFVYPGPDGE VEVFQEFGKI GKSLKNSVSP DEICDAYGAD TLRVYEMSMG PLEASRPWAT
KDVVGAYRFL QRVWRLVVDE HTGETRVADG VELDIDTLRA LHRTIVGVSE DFAALRNNTA
TAKLIEYTNH LTKKHRDAVP RAAVEPLVQM LAPLAPHIAE ELWLRLGNTT SLAHGPFPKA
DAAYLVDETV EYPVQVNGKV RGRVVVAADT DEETLKAAVL TDEKVQAFLA GATPRKVIVV
AGRLVNLVI
