Tag | Content |
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CPLM ID | CPLM-009200 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Elongation factor Tu-B |
Protein Synonyms/Alias | EF-Tu-B |
Gene Name | tufB |
Gene Synonyms/Alias | TTHA0251 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
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3 | *****MAKGEFIRTK | acetylation | [1] | 53 | KDYGDIDKAPEERAR | acetylation | [1] | 75 | HVEYETAKRHYSHVD | acetylation | [1] |
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Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
Functional Description | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. |
Sequence Annotation | NP_BIND 19 26 GTP (By similarity). NP_BIND 82 86 GTP (By similarity). NP_BIND 137 140 GTP (By similarity). MOD_RES 395 395 Phosphothreonine (By similarity). |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 406 AA |
Protein Sequence | MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVTAAEN PNVEVKDYGD IDKAPEERAR 60 GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH 120 ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL 180 EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT 240 GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE 300 RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV 360 EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE 406 |
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