Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX

Contribute

Send feedback

Read comments (?) or add your own

Q7VEV7 (LYSX_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX

Including the following 2 domains:

Lysine--tRNA ligase
EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS
Phosphatidylglycerol lysyltransferase
EC=2.3.2.3
Alternative name(s):
Lysylphosphatidylglycerol synthetase
Short name=LPG synthetase

Gene names

Name:	lysX
Synonyms:	lysS2
Ordered Locus Names:	Mb1667c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	1172 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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. HAMAP MF_00252
Catalytic activity	ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP MF_00252 L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol. HAMAP MF_00252
Cofactor	Binds 3 magnesium ions per subunit By similarity. HAMAP MF_00252
Subcellular location	Cell membrane; Multi-pass membrane protein Potential HAMAP MF_00252.
Miscellaneous	There are two lysyl-tRNA ligases in M.bovis. HAMAP MF_00252
Sequence similarities	In the N-terminal section; belongs to the LPG synthetase family. In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. Contains 1 OB DNA-binding domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Lipid metabolism Virulence
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	lipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lysyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW lysine-tRNA ligase activity Inferred from electronic annotation. Source: EC lysyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1172

1172

Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX HAMAP MF_00252

PRO_0000152656

Regions

Transmembrane

80 – 100

Helical; Potential

Transmembrane

122 – 142

Helical; Potential

Transmembrane

146 – 166

Helical; Potential

Transmembrane

177 – 197

Helical; Potential

Transmembrane

214 – 234

Helical; Potential

Transmembrane

272 – 292

Helical; Potential

Transmembrane

612 – 632

Helical; Potential

DNA binding

726 – 804

OB HAMAP MF_00252

Region

1 – 663

663

Phosphatidylglycerol lysyltransferase HAMAP MF_00252

Region

664 – 1172

509

Lysine--tRNA ligase HAMAP MF_00252

Sites

Metal binding

1084

Magnesium 1 By similarity

Metal binding

1091

Magnesium 1 By similarity

Metal binding

1091

Magnesium 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7VEV7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 20B46091FC6FE926
Show »

FASTA

1,172

128,182

        10         20         30         40         50         60 
MGLHLTVPGL RRDGRGVQSN SHDTSSKTTA DISRCPQHTD AGLQRAATPG ISRLLGISSR 

        70         80         90        100        110        120 
SVTLTKPRSA TRGNSRYHWV PAAAGWTVGV IATLSLLASV SPLIRWIIKV PREFINDYLF 

       130        140        150        160        170        180 
NFPDTNFAWS FVLALLAAAL TARKRIAWLV LLANMVLAAV VNAAEIAAGG NTAAESFGEN 

       190        200        210        220        230        240 
LGFAVHVVAI VVLVLGYREF WAKVRRGALF RAAAVWLAGA VVGIVASWGL VELFPGSLAP 

       250        260        270        280        290        300 
DERLGYAANR VVGFALADPD LFTGRPHVFL NAIFGLFGAF ALIGAAIVLF LSQRADNALT 

       310        320        330        340        350        360 
GEDESAIRGL LDLYGKDDSL GYFATRRDKS VVFASSGRAC ITYRVEVGVC LASGDPVGDH 

       370        380        390        400        410        420 
RAWPQAVDAW LRLCQTYGWA PGVMGASSQG AQTYREAGLT ALELGDEAIL RPADFKLSGP 

       430        440        450        460        470        480 
EMRGVRQAVT RARRAGLTVR IRRHRDIAED EMAQTITRAD SWRDTETERG FSMALGRLGD 

       490        500        510        520        530        540 
PADSDCLLVE AIDPHNQVLA MLSLVPWGTT GVSLDLMRRS PQSPNGTIEL MVSELALHAE 

       550        560        570        580        590        600 
SLGITRISLN FAVFRAAFEQ GAQLGAGPVA RLWRGLLVFF SRWWQLETLY RSNMKYQPEW 

       610        620        630        640        650        660 
VPRYACYEDA RVIPRVGVAS VIAEGFLVLP FSRRNRVHTG HHPAVPERLA ATGLLHHDGS 

       670        680        690        700        710        720 
APDVSGLRQV GLTNGDGVER RLPEQVRVRF DKLEKLRSSG IDAFPVGRPP SHTVAQALAA 

       730        740        750        760        770        780 
DHQASVSVSG RIMRIRNYGG VLFAQLRDWS GEMQVLLDNS RLDQGCAADF NAATDLGDLV 

       790        800        810        820        830        840 
EMTGHMGASK TGTPSLIVSG WRLIGKCLRP LPNKWKGLLD PEARVRTRYL DLAVNAESRA 

       850        860        870        880        890        900 
LITARSSVLR AVRETLFAKG FVEVETPILQ QLHGGATARP FVTHINTYSM DLFLRIAPEL 

       910        920        930        940        950        960 
YLKRLCVGGV ERVFELGRAF RNEGVDFSHN PEFTLLEAYQ AHAGYLEWID GCRELIQNAA 

       970        980        990       1000       1010       1020 
QAANGAPIAM RPRTDKGSDG TRHHLEPVDI SGIWPVRTVH DAISEALGER IDADTGLTTL 

      1030       1040       1050       1060       1070       1080 
RKLCDAAGVP YRTQWDAGAV VLELYEHLVE CRTEQPTFYI DFPTSVSPLT RPHRSKRGVA 

      1090       1100       1110       1120       1130       1140 
ERWDLVAWGI ELGTAYSELT DPVEQRRRLQ EQSLLAAGGD PEAMELDEDF LQAMEYAMPP 

      1150       1160       1170 
TGGLGMGIDR VVMLITGRSI RETLPFPLAK PH

« Hide

References

[1]

"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.

Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248339 Genomic DNA. Translation: CAD96335.1.
RefSeq	NP_855320.1. NC_002945.3.
3D structure databases
ProteinModelPortal	Q7VEV7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000015021; EBMYCP00000014856; EBMYCG00000015018.
GeneID	1092607.
GenomeReviews	Gene locus Mb1667c in contig BX248333_GR.
KEGG	mbo:Mb1667c.
PATRIC	18005347. VBIMycBov88188_1820.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000017004.
HOGENOM	HBG431994.
OMA	TRRDKAV.
ProtClustDB	PRK02983.
Enzyme and pathway databases
BioCyc	MBOV233413:MB1667C-MONOMER.
Family and domain databases
HAMAP	MF_00252. Lys_tRNA_synth_class2. Fused. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR024320. LPG_synthase_DUF2156. IPR002313. Lys-tRNA-synth_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K04567.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF4. tRNA-synt_lys_2. 1 hit.
Pfam	PF09924. DUF2156. 1 hit. PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR00982. TRNASYNTHLYS.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00499. LysS_bact. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYSX_MYCBO

Accession

Primary (citable) accession number: Q7VEV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents