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Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX [Includes: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS); Phosphatidylglycerol lysyltransferase (EC 2.3.2.3) (Lysylphosphatidylglycerol synthetase) (LPG synthetase)]

 LYSX_MYCSS              Reviewed;        1112 AA.
Q1B7P4;
18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 1.
05-JUL-2017, entry version 87.
RecName: Full=Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX;
Includes:
RecName: Full=Lysine--tRNA ligase;
EC=6.1.1.6;
AltName: Full=Lysyl-tRNA synthetase;
Short=LysRS;
Includes:
RecName: Full=Phosphatidylglycerol lysyltransferase;
EC=2.3.2.3;
AltName: Full=Lysylphosphatidylglycerol synthetase;
Short=LPG synthetase;
Name=lysX; OrderedLocusNames=Mmcs_2983;
Mycobacterium sp. (strain MCS).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=164756;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MCS;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L.,
Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J.,
Sims R.C., Richardson P.;
"Complete sequence of chromosome of Mycobacterium sp. MCS.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the production of L-lysyl-tRNA(Lys)transfer
and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to
membrane-bound phosphatidylglycerol (PG), which produces
lysylphosphatidylglycerol (LPG), one of the components of the
bacterial membrane with a positive net charge. LPG synthesis
contributes to the resistance to cationic antimicrobial peptides
(CAMPs) and likely protects M.tuberculosis against the CAMPs
produced by competiting microorganisms (bacteriocins). In fact,
the modification of anionic phosphatidylglycerol with positively
charged L-lysine results in repulsion of the peptides (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
+ L-lysyl-tRNA(Lys).
-!- CATALYTIC ACTIVITY: L-lysyl-tRNA(Lys) + phosphatidylglycerol =
tRNA(Lys) + 3-O-L-lysyl-1-O-phosphatidylglycerol.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the LPG
synthetase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-II
aminoacyl-tRNA synthetase family. {ECO:0000305}.
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EMBL; CP000384; ABG09090.1; -; Genomic_DNA.
RefSeq; WP_011560376.1; NC_008146.1.
ProteinModelPortal; Q1B7P4; -.
SMR; Q1B7P4; -.
EnsemblBacteria; ABG09090; ABG09090; Mmcs_2983.
GeneID; 32421216; -.
KEGG; mmc:Mmcs_2983; -.
HOGENOM; HOG000046227; -.
KO; K04567; -.
OMA; WDLVAFG; -.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
GO; GO:0050071; F:lysyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
InterPro; IPR004364; aa-tRNA-synt_II.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR024320; LPG_synthase_C.
InterPro; IPR002313; Lys-tRNA-ligase_II.
InterPro; IPR018149; Lys-tRNA-synth_II_C.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
InterPro; IPR031553; tRNA-synt_2_TM.
Pfam; PF09924; DUF2156; 1.
Pfam; PF00152; tRNA-synt_2; 1.
Pfam; PF16995; tRNA-synt_2_TM; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PRINTS; PR00982; TRNASYNTHLYS.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00499; lysS_bact; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase; Antibiotic resistance; ATP-binding;
Cell membrane; DNA-binding; Ligase; Lipid metabolism; Magnesium;
Membrane; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 1112 Lysylphosphatidylglycerol biosynthesis
bifunctional protein LysX.
/FTId=PRO_0000394327.
TRANSMEM 18 38 Helical. {ECO:0000255}.
TRANSMEM 60 80 Helical. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
DNA_BIND 675 748 OB.
REGION 1 613 Phosphatidylglycerol lysyltransferase.
REGION 614 1112 Lysine--tRNA ligase.
METAL 1024 1024 Magnesium 1. {ECO:0000250}.
METAL 1031 1031 Magnesium 1. {ECO:0000250}.
METAL 1031 1031 Magnesium 2. {ECO:0000250}.
SEQUENCE 1112 AA; 121837 MW; AB2DB8DD268CBFE8 CRC64;
MTLTSPPRTR ADSRYSWVPA AAGWTVGVIA TLSLIASVSP LVRWIIRVPR EFVDDYIFNF
PDTSFAWAFV LALLAGALAA RKRIAWWILL LYMVAAAGWN VADLLTGDES VVDEMGEVIG
LAFHLAAVAF LLLARPLFWA RVRRGALFKA AGVLAAGMAV GVLVGWGLLE LFPGDLERDY
RLAYAANRVF AFAGVDPDAF DGQHPHVVVN ALLGLFGALA LMAAAIVLFQ SQRSENALTG
EDESAIRGLL ELYGKNDSLG YFATRRDKSV VFAPNGRAAI TYRVEVGVCL ASGDPVGDPK
AWPQAIDAWL ALCGTYGWAP GVMGASVGGA EAFRAAGLSA IQLGDEAILL PDSFRLSGPD
MRAVRQAVTR ARRAGVTVRI RRHRELSPEQ MAEVIAHADA WRDTETERGF SMALGRLGDP
ADSDCLLVEA VQGGNGGQER SDPGDGTVVA MLSLVPWGSN GASLDVMRRS PQSPNGTIEL
MVSELCMQAE DIGVTRISLN FAMFRSAFEQ GAQLGAGPVA RLWRWLLVFF SRWWQLETLY
RSNMKYQPQW VPRYACYEDA RLIPRVGVAS VIAEGFLVLP FSRRNKQHTG HHTSAPQDLV
ASGVLHHDGT APDMSGLRTD TADDEPPRLP EQVRVRMAKL KALQADGVDA YPVGRPPSHT
AAAAVDSPDD VELDVAGRVL RIRDYGGVLF AQLRDWSGEV QLLLDNSTLE QGSTADFTAA
IDLGDLIAAT GTMGYSKNGT RSLLVRHWRL TGKCLRPLPD KWKGLTDQEA RVRARYVDLA
VNTEARDLIR ARSGVLHAIR DTLYHKGFLE VETPILQQIH GGANARPFLT HINAYDLDLY
LRIAPELYLK RLCVGGVERV FELGRAFRNE GVDFSHNPEF TLLEAYQAHA DYHVWIDGCR
ELIQNAAMAA NGEHVFLRPR DDGVLEPVDI SGPWTVKTVH EAVSEALGEH IDAATELPTL
RKLADAAGIP YLTHWDEGAV VLEMYEHLVE DRTQKPTFYK DFPTSVSPLT RPHRSIAGVA
ERWDLVAWGV ELGTAYSELT DPVEQRRRLQ AQSLLAAGGD PEAMELDEDF LQAMEYAMPP
TGGLGMGVDR VVMLITGRSI RETLPFPLAR PR


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