RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

ATP-dependent RNA helicase; DEAD-box RNA helicase involved in ribosome assembly. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. May play a role in the interconversion of ribosomal RNA-folding intermediates that are further processed by DeaD or SrmB during ribosome maturation.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

50S ribosomal subunit protein L17; Requires L15 for assembly into the 50S subunit.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

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 chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

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 chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

30S ribosomal subunit protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome (By similarity); Belongs to the universal ribosomal protein uS11 family.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

30S ribosomal subunit protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. Contacts the tRNAs in the A and P sites. Belongs to the universal ribosomal protein uS13 family.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

ATP-dependent RNA helicase; DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. Acts before DeaD. Belongs to the DEAD box helicase family. SrmB subfamily.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

RNA chaperone and antiterminator, cold-inducible; Binds to and stimulates the transcription of the CCAAT- containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

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.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

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.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

GTPase involved in cell partioning and DNA repair; An abundant, essential GTPase which binds GTP, GDP and ppGpp with moderate affinity. Has high guanosine nucleotide exchange rate constants for GTP and GDP, and a relatively low GTP hydrolysis rate stimulated by the 50S ribosomal subunit. It is estimated there are 34000 molecules in log-phase cells and 5600 molecules in stationary- phase cells. Required for chromosome segregation. Plays a role in the stringent response, perhaps by sequestering 50S ribosomal subunits and decreasing protein synthesis , and a non-essential role in the late [...]

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

50S ribosomal subunit protein L17; Requires L15 for assembly into the 50S subunit.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

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.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

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.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

30S ribosomal subunit protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome (By similarity); Belongs to the universal ribosomal protein uS11 family.

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

30S ribosomal subunit protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. Contacts the tRNAs in the A and P sites. Belongs to the universal ribosomal protein uS13 family.

GTPase involved in cell partioning and DNA repair; An abundant, essential GTPase which binds GTP, GDP and ppGpp with moderate affinity. Has high guanosine nucleotide exchange rate constants for GTP and GDP, and a relatively low GTP hydrolysis rate stimulated by the 50S ribosomal subunit. It is estimated there are 34000 molecules in log-phase cells and 5600 molecules in stationary- phase cells. Required for chromosome segregation. Plays a role in the stringent response, perhaps by sequestering 50S ribosomal subunits and decreasing protein synthesis , and a non-essential role in the late [...]

Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.