Galactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates.

Multidrug efflux system protein; Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D- thiogalactopyranoside (IPTG) exclusi [...]

Galactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Galactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family.

Multidrug efflux system protein; Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D- thiogalactopyranoside (IPTG) exclusi [...]

Galactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates.

Multidrug efflux system protein; Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D- thiogalactopyranoside (IPTG) exclusi [...]

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

RNA polymerase, beta prime subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

30S ribosomal subunit protein S4; One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase; Belongs to the universal ribosomal protein uS4 family.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

30S ribosomal subunit protein S5; With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

RNA polymerase, beta prime subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

30S ribosomal subunit protein S4; One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase; Belongs to the universal ribosomal protein uS4 family.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

30S ribosomal subunit protein S5; With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.

30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Galactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

50S ribosomal subunit protein L19; This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.

RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.