SYK_TREPA
ID SYK_TREPA Reviewed; 528 AA.
AC O83650;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Lysine--tRNA ligase;
DE EC=6.1.1.6;
DE AltName: Full=Lysyl-tRNA synthetase;
DE Short=LysRS;
GN Name=lysS; OrderedLocusNames=TP_0644;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65618.1; -; Genomic_DNA.
DR PIR; C71299; C71299.
DR RefSeq; WP_010882089.1; NC_021490.2.
DR AlphaFoldDB; O83650; -.
DR SMR; O83650; -.
DR IntAct; O83650; 3.
DR STRING; 243276.TPANIC_0644; -.
DR EnsemblBacteria; AAC65618; AAC65618; TP_0644.
DR GeneID; 57879169; -.
DR KEGG; tpa:TP_0644; -.
DR eggNOG; COG1384; Bacteria.
DR HOGENOM; CLU_025562_1_0_12; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 256927at2; -.
DR BRENDA; 6.1.1.6; 6429.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 6.10.20.10; -; 1.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..528
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152745"
FT MOTIF 36..44
FT /note="'HIGH' region"
FT MOTIF 287..291
FT /note="'KMSKS' region"
SQ SEQUENCE 528 AA; 60901 MW; B90425263C4EBF6D CRC64;
MSICEKSLHW ADKVAHKIIK ERADCDQYTC ASGITPSGTV HIGNFREIIS VDLVVRALRD
QGKSVRFVHS WDDYDVFRRI PDNVPAQDEL KQYIRMPITS VPDPFQQEDS YARHHEREIE
SALPEVGIYP EYVYQSKQYQ AGVYAQEIKI ALDNRHRIQA ILNEYRDEQH KISGTYWPVS
VFCTACHKDC TTVDAWDSHW CLQYHCECGH GEQVDLRQTS AVKLSWRVDW AMRWSKEHVV
FEPAGKDHHS QGGSFDTARL ISDHIYHWPA PVSFRYDFIG LKGLPGKMSS SAGKVVGLRD
VLEVYQPEVL RYLFVSTRPN TEFSISFDLD VLKIYEDYDK SERVAWGIHA AKSEHEFMRH
KRIYELSQVR GMPPCISYQV PFRHVCNILQ INSGDISAVL AFFSDIHKDQ IERFVRRCQC
AWNWIRDAGA PDDFKFTLKE DGVRVPLSAE ITEALRLIRD TLVPRTDVLS EKELSAELYA
VARQIPVGSK ELFTALYQVL IGKNQGPRLA GFMKVIGTQR LHRMLSVY