| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lysine--tRNA ligase |
Protein Synonyms/Alias | LysRS |
Gene Name | lysS |
Gene Synonyms/Alias | SPD_0620 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 125 | VEGEVMRTDMGELSI | T | HTP | [1] | | 131 | RTDMGELSIKATHIT | S | HTP | [1] | | 135 | GELSIKATHITHLSK | T | HTP | [1] | |
Reference | [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY J. Proteome Res. 2010, Jan;9(1):275-82. [ PMID:19894762] |
Functional Description From UniProt | |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Proteinbiosynthesis |
Protein Sequence | MSTEHMEELN DQQIVRREKM AALREQGIDP FGKRFERTAN SQELKDKYAN LDKEQLHDKN 60
ETATIAGRLV TKRGKGKVGF AHLQDREGQI QIYVRKDAVG EENYEIFKKA DLGDFLGVEG 120
EVMRTDMGEL SIKATHITHL SKALRPLPEK FHGLTDVETI YRKRYLDLIS NRESFERFVT 180
RSKIISEIRR YLDQKGFLEV ETPVLHNEAG GAAARPFITH HNAQNIDMVL RIATELHLKR 240
LIVGGMERVY EIGRIFRNEG MDATHNPEFT SIEVYQAYAD FQDIMDLTEG IIQHAAKSVK 300
GDGPVNYQGT EIKINEPFKR VHMVDAIREI TGVDFWQDMT LEEAKAIAAE KKVPVEKHYT 360
EVGHIINAFF EEFVEETLIQ PTFVYGHPVA VSPLAKKNPE DQRFTDRFEL FIMTKEYGNA 420
FTELNDPIDQ LSRFEAQAKA KELGDDEATG IDYDYIEALE YGMPPTGGLG IGIDRLCMLL 480
TDTTTIRDVL LFPTMK 496 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0004824 F:lysine-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0003676 F:nucleic acid binding IEA:InterPro GO:0006430 P:lysyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
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