LYSX_MYCA9
ID LYSX_MYCA9 Reviewed; 1110 AA.
AC B1MAX9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MAB_2319c;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM62400.1; -; Genomic_DNA.
DR RefSeq; WP_005110833.1; NZ_MLCG01000006.1.
DR AlphaFoldDB; B1MAX9; -.
DR SMR; B1MAX9; -.
DR EnsemblBacteria; CAM62400; CAM62400; MAB_2319c.
DR GeneID; 66972691; -.
DR KEGG; mab:MAB_2319c; -.
DR OMA; DISGEWP; -.
DR Proteomes; UP000007137; Chromosome.
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..1110
FT /note="Lysylphosphatidylglycerol biosynthesis bifunctional
FT protein LysX"
FT /id="PRO_0000394316"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DNA_BIND 675..749
FT /note="OB"
FT REGION 1..620
FT /note="Phosphatidylglycerol lysyltransferase"
FT REGION 621..1110
FT /note="Lysine--tRNA ligase"
FT BINDING 1022
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1029
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1029
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1110 AA; 122213 MW; B2655A31F523873A CRC64;
MTSIKPAVEP PAPDHPAVTA LPGIGARPAA RPPVTSRWRW VPAFFGWFVG IQAILNFLSS
ISPFIRMVTK LPREFVDEYL FGWPDGSLSW AFVLSLLAAA LAVRKSIAWW VLLIDLLGRS
ALNVGGFIEH RDTTELIGLV VHGAFILLLL LARKEFYAKV RRGATVKAAL VLIAGMAAGT
VLAWGLLELF PRTLVPGDRF WWALNRVAGF SIASHRDFDG LPPHFLNWLF GLFGALALIA
AAIVLFRSQR AVNALTGDDE SLIRGLLERY GQDDSLGYFA TRRDKAVIFA PNGRAAVTYR
VEVGVCLVSA DPIGDKSAWG QAISAWLQVC DAYGWAPAVM GASAEGALAY REHGLNALEL
GDEAILYPRS FSISGPHMAT VRQAVNRARR SGLSVRIRRH RELSAEETKQ IIVNADLWRD
GNTERGFSMA LGRLGDSTDG DCLLVEAIDS TGDPVAMLSL VPWGTNGVSL ELMRRSRQSP
NGTIEFMVTE LLTRAEGMGI TRVSLNFVMF RSVYADGSRI GAGPVLRLWR SVLMFASRFW
QFEQLYRSNV KYQPEWVPRF ACYEDARLIP RIGIASVIAE GFLVLPFGNR DKPRHTGQYS
AVPQAIVATG LLHHDGSTPE LLPQTAPQQR VPEQVKVRLG KLAALQEKGI DTYPVGSPPS
HTVAEALAAP DGSEVVISGR LLRIRDYGGV LFAQLRDWSA EVQLLIDDPR LHEEFTAAVD
LGDLVEASGV MGQSNNGTRS VLVESWRIIG KCLHPLPDKR KGLTDPEARV RARYLDLAIN
PEAREQIAAR SAIITSLRNT LLAQGFLEVE TPILQQVHGG ANARPFLTHI NAYNLDLYLR
IAPELYLKRL CVGGVEKVFE LGRAFRNEGV DFSHNPEFTL LEAYQAHADY VTWAQTTQRL
IQNAAKAAHG AEVVMRPGAD GRLAPVDIGG EWPIVPVHEA VSRALGEEVN AATEVPTLQR
FCQSAEVQFN PRWDAGHLVL ELYERLVEKH TTSPTFYSDF PVSVSPLTRP HRSIAGLAER
WDLVAWGVEL GTAYTELTDP VEQRRRLYEQ SLLAAGGDAE AMELDEDFLR AMEYAMAPTG
GMGMGVDRVV MLITGRSIRE TLPFPLAKPR
