tufA
168
elongation factor Tu, binds to charged tRNAs to form ternary complexes, brings charged tRNAs to empty ribosome A sites
locus
BSU_01130
Molecular weight
43.43 kDa
pI
4.72
function
translation
product
elongation factor Tu
essential
yes
ec
3.6.5.3
synonyms
tufA
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0050 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
132,882 134,072
Phenotypes of a mutant
essential [Pubmed|12682299]
The protein
Catalyzed reaction/ biological activity
binds to charged tRNAs to form ternary complexes, brings charged tRNAs to empty ribosome A sites [pubmed|20025795]
Protein family
[wiki|TRAFAC class translation factor GTPase superfamily] (according to UniProt)
[wiki|Classic translation factor GTPase family] (according to UniProt)
[wiki|Domains]
[wiki|tr-type G domain] (aa 10-205) (according to UniProt)
Structure
[PDB|3U6B] (from ''E. coli '', 77% identity) [Pubmed|21999529]
[AF|P33166]
Modification
acetylated by [protein|C2283BDD806221A285A27F24F52F92F4D47F0C55|rimI] [pubmed|35398352]
phosphorylated on Thr-384 by [protein|23FF4A00C36EC1B7297F51A9EF3579B41F0B7EBA|prkC], dephosphorylated by [protein|84447F9A6644EA8A7593BB99B2B69D4377E670E2|prpC] [Pubmed|19246764], [Pubmed|17726680]
Cys83 is S-bacillithiolated in B. subtilis and other Bacillus species [Pubmed|22938038]
phosphorylated on Arg-265 [Pubmed|31221751]
phosphorylated on several Arg residues [Pubmed|24263382]
phosphorylated during [wiki|sporulation] on Thr-63 by [protein|E86A96B832351FF513DD9853EAD8998CC44C9951|yabT], dephosphorylated by [protein|84447F9A6644EA8A7593BB99B2B69D4377E670E2|prpC] [Pubmed|26056311]
phosphorylated on Tyr-270 [Pubmed|26381121]
Effectors of protein activity
phosphorylation by YabT results in inhibtion of GTP hydrolysis; as a result, EF-Tu remains stably bound
to the [wiki|ribosome], stalling protein [wiki|translation] [Pubmed|26056311]
[wiki|Localization]
EF-Tu localizes in a helical pattern underneath the cell membrane and colocalizes with [protein|A4C8719E06F774A6EB4D79757CC79CF89E453A54|mreB] [Pubmed|20133608]
membrane [Pubmed|18763711]
cytoplasm (according to UniProt)
Additional information
belongs to the 100 most abundant proteins [PubMed|15378759]
Expression and Regulation
Operons
genes
[gene|11D7ABA61FC4069B48614875AF2C6C694291B545|rplGB]-[gene|0E4CB387626F53E5F60C7639D525B57D50C65C03|rpsL]-[gene|8049CACE85B2627A08CB4D8A8587D52E2DB24C7F|rpsG]-[gene|297844645CCCF40CB40E84339997F6610883DF4E|fusA]-[gene|E771685D6D41D48E0C0AF77F15B4F380820FCDC2|tufA]
description
[pubmed|22383849]
regulation
[protein|CEE73284EFC0DBE8870CE0B474922DED79475A57|rel] dependent downregulation (Class I) during stringent response [Pubmed|11948165]
the mRNA is processed between [gene|11D7ABA61FC4069B48614875AF2C6C694291B545|rplGB] and [gene|0E4CB387626F53E5F60C7639D525B57D50C65C03|rpsL] by [protein|872CCB5A49C9000BD95E4B0472556D5F60F7D7A4|RNase Y], this requires the [protein|EE52DFA35B935E551871D079A9BE877DB2001A3B|ricA]-[protein|6C9A092F38739A3759793EF8B496569CD02C2E3F|ricF]-[protein|EBD15C174A03B7FCDFFE4C5DB5D86E93F1B9CAC4|ricT] complex [Pubmed|29794222]
regulatory mechanism
stringent response: negative regulation, [pubmed|11948165], in [regulon|other_regulator:stringent response|stringent response]
Biological materials
two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system ([wiki|BACTH]), available in [wiki|Jörg Stülke]'s lab
References
Reviews
Original Publications
Page visits: 8637
Time of last update: 2024-12-22 01:58:48
Author of last update: Jstuelk