LYSX_MYCTK
ID LYSX_MYCTK Reviewed; 1174 AA.
AC C6DS31;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX;
DE Includes:
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
DE Includes:
DE RecName: Full=Phosphatidylglycerol lysyltransferase;
DE EC=2.3.2.3;
DE AltName: Full=Lysylphosphatidylglycerol synthetase;
DE Short=LPG synthetase;
GN Name=lysX; OrderedLocusNames=TBMG_02353;
OS Mycobacterium tuberculosis (strain KZN 1435 / MDR).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=478434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KZN 1435 / MDR;
RA Murray M., Pillay M., Borowsky M.L., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I., Hepburn T.A.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Galagan J., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis strain KZN 1435.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the
CC transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound
CC phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol
CC (LPG), one of the components of the bacterial membrane with a positive
CC net charge. LPG synthesis contributes to the resistance to cationic
CC antimicrobial peptides (CAMPs) and likely protects M.tuberculosis
CC against the CAMPs produced by competiting microorganisms
CC (bacteriocins). In fact, the modification of anionic
CC phosphatidylglycerol with positively charged L-lysine results in
CC repulsion of the peptides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-
CC tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-
CC glycerol + tRNA(Lys); Xref=Rhea:RHEA:10668, Rhea:RHEA-COMP:9696,
CC Rhea:RHEA-COMP:9697, ChEBI:CHEBI:64716, ChEBI:CHEBI:75792,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529; EC=2.3.2.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LPG synthetase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC aminoacyl-tRNA synthetase family. {ECO:0000305}.
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DR EMBL; CP001658; ACT25426.1; -; Genomic_DNA.
DR AlphaFoldDB; C6DS31; -.
DR SMR; C6DS31; -.
DR KEGG; mtb:TBMG_02353; -.
DR HOGENOM; CLU_008255_2_0_11; -.
DR OMA; DISGEWP; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050071; F:lysyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd04322; LysRS_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR024320; LPG_synthase_C.
DR InterPro; IPR002313; Lys-tRNA-ligase_II.
DR InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR031553; tRNA-synt_2_TM.
DR Pfam; PF09924; LPG_synthase_C; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF16995; tRNA-synt_2_TM; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00982; TRNASYNTHLYS.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00499; lysS_bact; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; Antibiotic resistance; ATP-binding;
KW Cell membrane; DNA-binding; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Transferase;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..1174
FT /note="Lysylphosphatidylglycerol biosynthesis bifunctional
FT protein LysX"
FT /id="PRO_0000394330"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DNA_BIND 728..806
FT /note="OB"
FT REGION 1..665
FT /note="Phosphatidylglycerol lysyltransferase"
FT REGION 9..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..1174
FT /note="Lysine--tRNA ligase"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1086
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1093
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1093
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1174 AA; 128396 MW; C674E65773AF1266 CRC64;
MGVGLHLTVP GLRRDGRGVQ SNSHDTSSKT TADISRCPQH TDAGLQRAAT PGISRLLGIS
SRSVTLTKPR SATRGNSRYH WVPAAAGWTV GVIATLSLLA SVSPLIRWII KVPREFINDY
LFNFPDTNFA WSFVLALLAA ALTARKRIAW LVLLANMVLA AVVNAAEIAA GGNTAAESFG
ENLGFAVHVV AIVVLVLGYR EFWAKVRRGA LFRAAAVWLA GAVVGIVASW GLVELFPGSL
APDERLGYAA NRVVGFALAD PDLFTGRPHV FLNAIFGLFG AFALIGAAIV LFLSQRADNA
LTGEDESAIR GLLDLYGKDD SLGYFATRRD KSVVFASSGR ACITYRVEVG VCLASGDPVG
DHRAWPQAVD AWLRLCQTYG WAPGVMGASS QGAQTYREAG LTALELGDEA ILRPADFKLS
GPEMRGVRQA VTRARRAGLT VRIRRHRDIA EDEMAQTITR ADSWRDTETE RGFSMALGRL
GDPADSDCLL VEAIDPHNQV LAMLSLVPWG TTGVSLDLMR RSPQSPNGTI ELMVSELALH
AESLGITRIS LNFAVFRAAF EQGAQLGAGP VARLWRGLLV FFSRWWQLET LYRSNMKYQP
EWVPRYACYE DARVIPRVGV ASVIAEGFLV LPFSRRNRVH TGHHPAVPER LAATGLLHHD
GSAPDVSGLR QVGLTNGDGV ERRLPEQVRV RFDKLEKLRS SGIDAFPVGR PPSHTVAQAL
AADHQASVSV SGRIMRIRNY GGVLFAQLRD WSGEMQVLLD NSRLDQGCAA DFNAATDLGD
LVEMTGHMGA SKTGTPSLIV SGWRLIGKCL RPLPNKWKGL LDPEARVRTR YLDLAVNAES
RALITARSSV LRAVRETLFA KGFVEVETPI LQQLHGGATA RPFVTHINTY SMDLFLRIAP
ELYLKRLCVG GVERVFELGR AFRNEGVDFS HNPEFTLLEA YQAHADYLEW IDGCRELIQN
AAQAANGAPI AMRPRTDKGS DGTRHHLEPV DISGIWPVRT VHDAISEALG ERIDADTGLT
TLRKLCDAAG VPYRTQWDAG AVVLELYEHL VECRTEQPTF YIDFPTSVSP LTRPHRSKRG
VAERWDLVAW GIELGTAYSE LTDPVEQRRR LQEQSLLAAG GDPEAMELDE DFLQAMEYAM
PPTGGLGMGI DRVVMLITGR SIRETLPFPL AKPH
