SYK_CHLTB
ID SYK_CHLTB Reviewed; 526 AA.
AC B0BAN6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00252};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00252};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00252};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00252};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00252}; OrderedLocusNames=CTLon_0150;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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:0000255|HAMAP-Rule:MF_00252};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00252};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00252};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00252}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00252}.
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DR EMBL; AM884177; CAP06548.1; -; Genomic_DNA.
DR RefSeq; WP_009873399.1; NC_010280.2.
DR PDB; 6NRZ; X-ray; 2.10 A; A/B=1-526.
DR PDB; 6NS0; X-ray; 2.20 A; A/B=1-526.
DR PDB; 6O3F; X-ray; 2.40 A; A/B=1-521.
DR PDBsum; 6NRZ; -.
DR PDBsum; 6NS0; -.
DR PDBsum; 6O3F; -.
DR AlphaFoldDB; B0BAN6; -.
DR SMR; B0BAN6; -.
DR KEGG; ctl:CTLon_0150; -.
DR HOGENOM; CLU_008255_6_0_0; -.
DR OMA; EIFGEKC; -.
DR Proteomes; UP000000794; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 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 Pfam; PF00152; tRNA-synt_2; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..526
FT /note="Lysine--tRNA ligase"
FT /id="PRO_1000101108"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00252"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6O3F"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 66..79
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:6NRZ"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 186..208
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:6NRZ"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 295..313
FT /evidence="ECO:0007829|PDB:6NRZ"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 383..394
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 437..445
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 476..485
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 496..503
FT /evidence="ECO:0007829|PDB:6NRZ"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:6NRZ"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6NRZ"
SQ SEQUENCE 526 AA; 60076 MW; D758F8AA57360A9F CRC64;
MSVEVEYLQH EDYLYRTSKL KEIRDLGINP YPYQYTDCLE VQEIRNQFVD NELGDSEAAF
RKETPKVRFA GRLVLFRSMG KNAFGQILDN DAKIQVMFNR DFSAVAGLAA DAGISPIKFI
EKKLDLGDIL GLEGYLFFTH SGELTVLVET VTLLCKSLIS LPDKHAGLAD KEIRYRKRWA
DLISSEDVRK TFLTRSRILK LIREYMDQQS FLEVETPILQ TVYGGAEATP FVTTLQALHA
EMFLRISLEI ALKKLLVGGM SRVYEIGKVF RNEGIDRTHN PEFTMIEAYA AYWDYNDVMK
CVENLVEYIV RALNNGETQV QYSHLKSGPQ VVDFKAPWIR MTMKESISVY GGVDVDLHAD
HELRKILETQ TSLPEKTYVH ASRGELIALL FDELVCDKLI APHHITDHPL ETTPLCKTLR
SGDETLVERF ESFCLGKELC NAYSELNDPL QQRKLLEEQM RKKALNPDSE YHPIDEEFLE
ALCQGMPPAG GFGIGIDRLV MMLTDAASIR DVLFFPVMRR IEAKKD
