LYSX_MYCGI
ID LYSX_MYCGI Reviewed; 1101 AA.
AC A4T9U2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Mflv_3544;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) 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; CP000656; ABP46018.1; -; Genomic_DNA.
DR RefSeq; WP_011894402.1; NC_009338.1.
DR AlphaFoldDB; A4T9U2; -.
DR SMR; A4T9U2; -.
DR STRING; 350054.Mflv_3544; -.
DR EnsemblBacteria; ABP46018; ABP46018; Mflv_3544.
DR KEGG; mgi:Mflv_3544; -.
DR eggNOG; COG1190; Bacteria.
DR eggNOG; COG2898; Bacteria.
DR HOGENOM; CLU_008255_2_0_11; -.
DR OMA; DISGEWP; -.
DR OrthoDB; 63621at2; -.
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.
FT CHAIN 1..1101
FT /note="Lysylphosphatidylglycerol biosynthesis bifunctional
FT protein LysX"
FT /id="PRO_0000394319"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DNA_BIND 662..740
FT /note="OB"
FT REGION 1..601
FT /note="Phosphatidylglycerol lysyltransferase"
FT REGION 602..1101
FT /note="Lysine--tRNA ligase"
FT BINDING 1013
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1020
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1020
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1101 AA; 120683 MW; 8D1D8F42B36FC41C CRC64;
MTATRLVRAH PESSHRWVPA AAGWIVGVIA TLSLLASVSP LVRSIIRVPR EFVDDYIFNF
PDTSFAWAFV LALLAAALAA RKRIAWWILT GYMVAAAVWN VTGLLDGDRW FEDVGEIIGL
GFHLAAIASL LLARREFWAR VRPGALVKAA VTLVAGLGVG TLIGWGLLEL FPGTLARPDR
FWYALNRVGA FAGADAGAFS GHPHVLVNAL LGLFGAMALM IAAVVLFQSQ RADNALTGED
ESAIRGLLEL YGKNDSLGYF ATRRDKAVVF APNGRAAITY RVEVGVCLAS GDPVGDPKAW
PQAIEAWLTL CETYGWAPGV MGASATGAQA FRQAGLHALQ LGDEAILHPD DFRLSGPEMR
AVRQAVTRAR RAGVAVRFRR HRELSPDEMA EVIAHADAWR DTEDERGFSM ALGRLGDPAD
ADCLLVEAVQ NGTQVVAMLS LVPWGSNGVS LDLMRRAPQS PNGTIELMVS ELCLQSESIG
ISRISLNFAM FRSAFEQGAQ LGAGPVARLW RWLLVFFSRW WQLETLYRSN MKYQPEWVPR
YACYEDARLV PRVGVASVIA EGFLVLPFSR RHDQPHTGHH IAAPGDLIAT GRLHSDGTAP
DRIGPVGDGA DDDAAPRLPE QVRVRMAKLS ALQDRGVDAY PVGSPPSHTI AEAIAAEEGT
EVTVSGRVLR ARDYGGVLFG QLRDWSAETQ VALDNSALLD GTTTDFTRTV DLGDLIEVTG
TMGHTRSGSW SVLVTRWRLI GKCLRPLPDK WKGLTDQEAR VRARYVDLAV NTDARELIKA
RSAILHAIRE TLVGKGFLEV ETPILQQIHG GANARPFLTH INAYDLDLYL RIAPELYLKR
LCVGGVERVF ELGRAFRNEG VDFSHNPEFT LLEAYQAHAD YTVWIDGCRE LIQNAAMAAN
GSHVFFRPRE DGVLEPVDIS GRWAVKTVHG AVSEALGEHI DVDTDLATLR RLCDKAGIPY
LTHWDAGAVV LEMYEHLVED QTTEPTFYKD FPTSVSPLTR PHRSIPGVAE RWDLVAWGVE
LGTAYSELTD PVEQRRRLQE QSLLAAGGDP EAMELDEDFL QAMEYAMPPT GGLGMGVDRV
VMLITGRSIR ETLPFPLAKP R
