SYK_CAUVN
ID SYK_CAUVN Reviewed; 552 AA.
AC B8GXH3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=CCNA_00082;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR EMBL; CP001340; ACL93549.1; -; Genomic_DNA.
DR RefSeq; WP_010917973.1; NC_011916.1.
DR RefSeq; YP_002515457.1; NC_011916.1.
DR AlphaFoldDB; B8GXH3; -.
DR SMR; B8GXH3; -.
DR PRIDE; B8GXH3; -.
DR EnsemblBacteria; ACL93549; ACL93549; CCNA_00082.
DR GeneID; 7332173; -.
DR KEGG; ccs:CCNA_00082; -.
DR PATRIC; fig|565050.3.peg.82; -.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
DR OrthoDB; 256927at2; -.
DR PhylomeDB; B8GXH3; -.
DR Proteomes; UP000001364; 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 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; 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..552
FT /note="Lysine--tRNA ligase"
FT /id="PRO_1000199265"
FT MOTIF 72..80
FT /note="'HIGH' region"
FT MOTIF 320..324
FT /note="'KMSKS' region"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ SEQUENCE 552 AA; 61026 MW; A64727130E6BD6A1 CRC64;
MFEGLSPLAR DARSWPFEQA RATIARVLRV RLPDRADQDA AKALIDAGKT DEAVKAYPAL
AKAVIFETGY GPSGLPHLGT FGEVARTTMV RQAFRALTDE AIPTRLIAFS DDMDGLRKVP
DNIENKQPLI EDLGKPLTVV RDPFGTHDSF GAHNNARLRA FLDGFGFEYE FVSSTDCYKG
GLFDATLLTA LERFDAIQKV MLPTLGEERR ATYSPFLPIS PSTGKVLQVP TLERNVEKGT
IVFEDEDGSK VEVPVTGGHV KMQWKPDWAM RWTALGVDYE MSGKDLIDSV KASGAICKAL
GGVPPEGFNY ELFLDENNQK ISKSKGNGLS MEDWLRYGAP ESLSYYMFQS PKSAKKLYFD
VIPKASDEYL QQLDGFGRQE PAKQLDNPVW HIHGGKPPQQ GSPVSFSLML NLVSAADAST
KEILWGFLSR YIPGASPETQ PLLDRLAGYA INYYEDFVKP SKVFRAPSDQ ERAAMLDLLA
KLKAMPAGTQ DAELIQNEVF EVGKTHGFDP LRAWFQALYE VLLGQSQGPR FGSFAAIFGI
DRTVALIEEK LG