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Database: UniProt
Entry: A0A0V8S1D3_9CELL
LinkDB: A0A0V8S1D3_9CELL
Original site: A0A0V8S1D3_9CELL 
ID   A0A0V8S1D3_9CELL        Unreviewed;      1084 AA.
AC   A0A0V8S1D3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   ORFNames=ATM99_02745 {ECO:0000313|EMBL:KSW14116.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW14116.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW14116.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW14116.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT   Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-2015) 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. {ECO:0000256|ARBA:ARBA00024681}.
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         Evidence={ECO:0000256|ARBA:ARBA00000367};
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         Evidence={ECO:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC         Rule:MF_00252};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00252};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00252};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_00252}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       aminoacyl-tRNA synthetase family. {ECO:0000256|ARBA:ARBA00009968}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LPG synthetase
CC       family. {ECO:0000256|ARBA:ARBA00005270}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KSW14116.1}.
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DR   EMBL; LNTD01000267; KSW14116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V8S1D3; -.
DR   STRING; 1295626.ATM99_02745; -.
DR   Proteomes; UP000054319; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0050071; F:phosphatidylglycerol lysyltransferase activity; IEA:UniProtKB-EC.
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; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
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; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00252};
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          771..1080
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         993
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         1000
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         1000
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   1084 AA;  118029 MW;  B22003046E3A4EEA CRC64;
     MLQAYALWLL VTLVLFPFWP HQIRAVGHVL SMTNIPAQPG LFSAILVGVV ASGVLRRLRA
     AVWFVVVVWQ LPVALIGVLT LVLVATGSAT LDELEVTTRD VVAFCFSLPI IAVLVSARRA
     FPARLRRGAW WRAVLVTGAT ALAAAALAYT LLQFDPAGLT TQGDRLGWSL SHVLGIHSSV
     VASGHGPAWV GALVGLVSAA GLLLGIAVFL RSSASPAGER AADALAVRRL LLADPEHDSL
     GYFATRDDRS AVFSPDGRAA VSYRVVSGVS LAAGDPVGAH ESWPAAVERW LAHTRQHGWI
     PAVTSTTEAG ARTYRDAGLH PVPMGDEAVV VTRRIDLTNP ALRPVRRAVE RGRAAGYEVR
     VRRQAAIPAD ELAALVRDAD RWRHGEERGY SMALERLGDP VDPRIVVVTA HDADGAVQGL
     LSFVPWGRRG LSLDVMRRSP GAVAGVTELM VAELAAASRD LGIEKVSMNF AMFRSTFEVG
     ERVGATPVQR FNRRVLLLAS RFWQLEQLYR SNEKYLPDWE PRLMCYEAAG QLTRVVFALG
     QAEGFLPRNP RWLTSADDRS DRSPELHDPA FAAAVVAQEE ELLAVTAPPR RLTEQQRTRH
     AKLDVLQAAG MDPYPVGVPR TASVRAARDM LAAVPPGTTS PVAGADELAV VGRVVRLRDL
     GGVAFAVLRE GGAELQVMLT ASGSADLVLW RRVVDLGDQV SVTGAPVRSR SGEPTLLARS
     WCMASKALTP PPDKHRGLAD PEARVRLRHM DLAMNDRAEH LLRSRAAAVW AIRSSLVEHG
     FIEVETPILQ RIHGGANARP FTTHINAYDL DLYLRIAPEL FLKRLMVGGV GRVFELGRNF
     RNEGVDATHN PEFTSMEAYQ AYGDYTTMRH LTRDLVVAAA TAVHGEPVAH RPDGTVVRLD
     GEWPVLTVHD AVSRALGTPV TPDLPLAELR ELCRTHDVAF DDDESHGALV EELYERFVEG
     QTVEPTFYTD FPVETSPLTR RHRDDPRLAE RWDLVAFGAE LGTAYSELVD PVEQRRRLTE
     QSILAAAGDP EAMEVDEDFL SALEFAMPPT GGVGIGVDRV VMMLVGGSIR DTLAFPFVRP
     SGRR
//
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