UniProt Accession

 EFTU2_ECOLI; P0CE48; O68929; P02990; P0A6N1; Q2M704; Q2M8R6; Q8X4S9; Q8XED3 

Genbank Protein ID

 X57091; J01717; U00006; U00096; AP009048 

Genbank Nucleotide ID

 CAA40370.1; AAA24669.1; AAC43078.1; AAC76954.1; BAE77340.1 

Protein Name

 Elongation factor Tu 2 

Protein Synonyms/Alias

 EF-Tu 2; P-43 

Gene Name

 tufB 

Gene Synonyms/Alias

 b3980; JW3943 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
57	IDNAPEEKARGITIN	methylation	[1]
177	IVRGSALKALEGDAE	acetylation	[2]
188	GDAEWEAKILELAGF	acetylation	[2]
209	EPERAIDKPFLLPIE	acetylation	[2]
314	SEVYILSKDEGGRHT	acetylation	[2]
391	VGAGVVAKVLS****	acetylation	[2, 3]

Reference

 [1] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] 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] 

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.
 NP_BIND 81 85 GTP.
 NP_BIND 136 139 GTP.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 38 38 N6-succinyllysine.
 MOD_RES 57 57 N6,N6-dimethyllysine; alternate.
 MOD_RES 57 57 N6-methyllysine; alternate.
 MOD_RES 177 177 N6-succinyllysine.
 MOD_RES 249 249 N6-succinyllysine.
 MOD_RES 253 253 N6-succinyllysine.
 MOD_RES 295 295 N6-succinyllysine.
 MOD_RES 314 314 N6-acetyllysine; alternate.
 MOD_RES 314 314 N6-succinyllysine; alternate.
 MOD_RES 383 383 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; Antibiotic resistance; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 394 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 

Interpro

 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004541; Transl_elong_EFTu/EF1A_bac/org.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 

Pfam

 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 

SMART

  

PROSITE

 PS00301; EFACTOR_GTP 

PRINTS

 PR00315; ELONGATNFCT.