UniProt functional annotation for P0CE47



	UniProt functional annotation for P0CE47

UniProt codes: P0CE47, P0A6N1.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.

Function: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.

Function: Plays a stimulatory role in trans-translation; binds tmRNA. {ECO:0000269|PubMed:15069072}.

Function: Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D- aminoacyl-tRNA deacylase (dtd) (By similarity). {ECO:0000250|UniProtKB:Q5SHN6}.

Function: (Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. {ECO:0000269|PubMed:816798, ECO:0000305}.

Function: (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain EC869; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). {ECO:0000269|PubMed:28223500, ECO:0000269|PubMed:28973472}.

Function: (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain NC101; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. The toxin may remodel the EF-Tu-aa-tRNA complex to displace the 3'-end of the aa-tRNA so it can enter the toxin active site and be cleaved. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). {ECO:0000269|PubMed:28223500, ECO:0000269|PubMed:28973472}.

Subunit: Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes (By similarity). {ECO:0000250|UniProtKB:P0CE48, ECO:0000255|HAMAP-Rule:MF_00118, ECO:0000269|PubMed:10625477, ECO:0000269|PubMed:17057344, ECO:0000269|PubMed:9918724, ECO:0000305}.

Subunit: (Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host ribosomal protein S1 and EF-Ts (PubMed:816798). {ECO:0000269|PubMed:816798}.

Subunit: (Microbial infection) Forms a contact-dependent growth inhibition complex of EF-Tu, CdiA-CT-EC869 and CdiI-EC869 as well as a GTP, EF-Tu, CdiA-CT-EC869 complex. {ECO:0000269|PubMed:28223500}.

Subunit: (Microbial infection) Forms a contact-dependent growth inhibition complex of CdiA-CT-NC101, CdiI-NC101 and EF-Tu; the complex is a dimer of heterotrimers. {ECO:0000269|PubMed:28973472}.

Subcellular location: Cytoplasm. Cell inner membrane; Peripheral membrane protein. Note=Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress.

Ptm: The N-terminus is blocked.

Ptm: Methylated in vivo on Lys-57 in response to nutrient starvation. {ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545}.

Ptm: Phosphorylated in vitro by phage protein doc on Thr-383. {ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965}.

Ptm: Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849), this has since been reported not to occur in vivo (PubMed:24095282). {ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965}.

Miscellaneous: Present with about 70,000 molecules/cell. {ECO:0000305|PubMed:775340}.

Miscellaneous: This chain is also used in bacteriophage Q-beta RNA polymerase. {ECO:0000269|PubMed:816798}.

Miscellaneous: The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. {ECO:0000269|PubMed:7525272}.

Miscellaneous: The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu. {ECO:0000269|PubMed:7957075}.

Similarity: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.



Function:		May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.



Function:		Plays a stimulatory role in trans-translation; binds tmRNA. {ECO:0000269\|PubMed:15069072}.



Function:		Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D- aminoacyl-tRNA deacylase (dtd) (By similarity). {ECO:0000250\|UniProtKB:Q5SHN6}.



Function:		(Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. {ECO:0000269\|PubMed:816798, ECO:0000305}.



Function:		(Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain EC869; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). {ECO:0000269\|PubMed:28223500, ECO:0000269\|PubMed:28973472}.



Function:		(Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain NC101; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. The toxin may remodel the EF-Tu-aa-tRNA complex to displace the 3'-end of the aa-tRNA so it can enter the toxin active site and be cleaved. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). {ECO:0000269\|PubMed:28223500, ECO:0000269\|PubMed:28973472}.


Subunit:		Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes (By similarity). {ECO:0000250\|UniProtKB:P0CE48, ECO:0000255\|HAMAP-Rule:MF_00118, ECO:0000269\|PubMed:10625477, ECO:0000269\|PubMed:17057344, ECO:0000269\|PubMed:9918724, ECO:0000305}.
Subunit:		(Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host ribosomal protein S1 and EF-Ts (PubMed:816798). {ECO:0000269\|PubMed:816798}.
Subunit:		(Microbial infection) Forms a contact-dependent growth inhibition complex of EF-Tu, CdiA-CT-EC869 and CdiI-EC869 as well as a GTP, EF-Tu, CdiA-CT-EC869 complex. {ECO:0000269\|PubMed:28223500}.
Subunit:		(Microbial infection) Forms a contact-dependent growth inhibition complex of CdiA-CT-NC101, CdiI-NC101 and EF-Tu; the complex is a dimer of heterotrimers. {ECO:0000269\|PubMed:28973472}.
Subcellular location:		Cytoplasm. Cell inner membrane; Peripheral membrane protein. Note=Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress.
Ptm:		The N-terminus is blocked.
Ptm:		Methylated in vivo on Lys-57 in response to nutrient starvation. {ECO:0000269\|PubMed:2022614, ECO:0000269\|PubMed:389663, ECO:0000269\|PubMed:6997043, ECO:0000269\|PubMed:7021545}.
Ptm:		Phosphorylated in vitro by phage protein doc on Thr-383. {ECO:0000269\|PubMed:19150849, ECO:0000269\|PubMed:24141193, ECO:0000269\|PubMed:8416965}.
Ptm:		Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849), this has since been reported not to occur in vivo (PubMed:24095282). {ECO:0000269\|PubMed:19150849, ECO:0000269\|PubMed:24095282, ECO:0000269\|PubMed:24141193, ECO:0000269\|PubMed:8416965}.
Miscellaneous:		Present with about 70,000 molecules/cell. {ECO:0000305\|PubMed:775340}.
Miscellaneous:		This chain is also used in bacteriophage Q-beta RNA polymerase. {ECO:0000269\|PubMed:816798}.
Miscellaneous:		The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. {ECO:0000269\|PubMed:7525272}.
Miscellaneous:		The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu. {ECO:0000269\|PubMed:7957075}.
Similarity:		Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000255\|HAMAP-Rule:MF_00118}.