Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Translation elongation factor EF-Tu 1; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Plays a stimulatory role in trans-translation; binds tmRNA. (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. (Microbial infe [...]

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Translation elongation factor EF-Tu 2; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Plays a stimulatory role in trans-translation, binds tmRNA. (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. The GTPase acti [...]

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

GTP-binding protein; A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity. Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides. Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleoti [...]

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

GTP-binding protein; A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity. Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides. Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleoti [...]

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

GTP-binding protein; A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity. Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides. Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleoti [...]

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Back-translocating elongation factor EF4, GTPase; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner; Belongs to the TRAFAC class translation factor GTPase superfam [...]

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

Peptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.

selenocysteinyl-tRNA-specific translation factor; Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.

GTP-binding protein; A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity. Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides. Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleoti [...]

Translation elongation factor EF-Tu 1; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Plays a stimulatory role in trans-translation; binds tmRNA. (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. (Microbial infe [...]

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Translation elongation factor EF-Tu 1; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Plays a stimulatory role in trans-translation; binds tmRNA. (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. (Microbial infe [...]

Translation elongation factor EF-Tu 2; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. Plays a stimulatory role in trans-translation, binds tmRNA. (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. The GTPase acti [...]