| Tag | Content |
|---|
| CPLM ID | CPLM-003104 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine--tRNA ligase |
Protein Synonyms/Alias | Seryl-tRNA synthetase; SerRS; Seryl-tRNA(Ser/Sec) synthetase |
Gene Name | serS |
Gene Synonyms/Alias | b0893; JW0876 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 17 | EPDAVAEKLARRGFK | acetylation | [1] | | 24 | KLARRGFKLDVDKLG | acetylation | [1] | | 29 | GFKLDVDKLGALEER | acetylation | [1] | | 43 | RRKVLQVKTENLQAE | acetylation | [1, 2] | | 77 | PLRLEVNKLGEELDA | acetylation | [1] | | 86 | GEELDAAKAELDALQ | acetylation | [1] | | 115 | ADEVPVGKDENDNVE | acetylation | [1] | | 289 | IRMHQFDKVEMVQIV | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). |
Sequence Annotation | NP_BIND 268 270 ATP (By similarity).
NP_BIND 355 358 ATP (By similarity).
REGION 237 239 Serine binding (By similarity).
BINDING 291 291 Serine (By similarity).
BINDING 391 391 Serine (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 430 AA |
Protein Sequence | MLDPNLLRNE PDAVAEKLAR RGFKLDVDKL GALEERRKVL QVKTENLQAE RNSRSKSIGQ 60
AKARGEDIEP LRLEVNKLGE ELDAAKAELD ALQAEIRDIA LTIPNLPADE VPVGKDENDN 120
VEVSRWGTPR EFDFEVRDHV TLGEMHSGLD FAAAVKLTGS RFVVMKGQIA RMHRALSQFM 180
LDLHTEQHGY SENYVPYLVN QDTLYGTGQL PKFAGDLFHT RPLEEEADTS NYALIPTAEV 240
PLTNLVRGEI IDEDDLPIKM TAHTPCFRSE AGSYGRDTRG LIRMHQFDKV EMVQIVRPED 300
SMAALEEMTG HAEKVLQLLG LPYRKIILCT GDMGFGACKT YDLEVWIPAQ NTYREISSCS 360
NVWDFQARRM QARCRSKSDK KTRLVHTLNG SGLAVGRTLV AVMENYQQAD GRIEVPEVLR 420
PYMNGLEYIG 430 |
Gene Ontology | GO:0005829; C:cytosol; IDA:UniProtKB. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0000287; F:magnesium ion binding; IDA:EcoCyc. GO:0004828; F:serine-tRNA ligase activity; IDA:UniProtKB. GO:0016260; P:selenocysteine biosynthetic process; IDA:EcoCyc. GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. GO:0006434; P:seryl-tRNA aminoacylation; IDA:UniProtKB. |
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