CP4-57 prophage; Positive regulator of the expression of the slpA gene. When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease. Part of the cryptic P4-like prophage CP4-57. Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans- translation.

HTH-type transcriptional regulator AppY; Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions.

CP4-57 prophage; Positive regulator of the expression of the slpA gene. When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease. Part of the cryptic P4-like prophage CP4-57. Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans- translation.

DLP12 prophage; Necessary for host cell lysis. It is believed to code for an endopeptidase that cleaves the amino-carboxyl cross-link between the diaminopimelic acid and D-alanine residues in the murein component of the bacterial cell wall (By similarity).

CP4-57 prophage; Positive regulator of the expression of the slpA gene. When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease. Part of the cryptic P4-like prophage CP4-57. Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans- translation.

Hha toxicity attenuator; Attenuates Hha toxicity and regulates biofilm formation. Binds to various coding and intergenic regions of genomic DNA.

CP4-57 prophage; Positive regulator of the expression of the slpA gene. When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease. Part of the cryptic P4-like prophage CP4-57. Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans- translation.

CP4-57 prophage; Antitoxin component of a type IV toxin-antitoxin (TA) system. Antitoxin that counteracts the effect of cognate toxin YpjF. Also counteracts the effect of non-cognate toxins CbtA and YfkI.

HTH-type transcriptional regulator AppY; Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions.

CP4-57 prophage; Positive regulator of the expression of the slpA gene. When overexpressed, leads to suppression of the capsule overproduction and UV sensitivity phenotypes of cells mutant for the Lon ATP-dependent protease. Part of the cryptic P4-like prophage CP4-57. Overexpression of AlpA leads to excision of the CP4-57 prophage by IntA. This inactivates ssrA (the gene upstream of the prophage) that encodes tmRNA which is required to rescue stalled ribosomes in a process known as trans- translation.

HTH-type transcriptional regulator AppY; Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions.

Modulator of gene expression, with H-NS; Down-regulates hemolysin (hly) expression in complex with H- NS. Stimulates transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repre [...]

HTH-type transcriptional regulator AppY; Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions.

DLP12 prophage; Necessary for host cell lysis. It is believed to code for an endopeptidase that cleaves the amino-carboxyl cross-link between the diaminopimelic acid and D-alanine residues in the murein component of the bacterial cell wall (By similarity).

HTH-type transcriptional regulator AppY; Induces the synthesis of acid phosphatase (AppA) and several other polypeptides (such as AppBC) during the deceleration phase of growth. It also acts as a transcriptional repressor for one group of proteins that are synthesized preferentially in exponential growth and for one group synthesized only in the stationary phase. Also involved in the stabilization of the sigma stress factor RpoS during stress conditions.

CP4-57 prophage; Antitoxin component of a type IV toxin-antitoxin (TA) system. Antitoxin that counteracts the effect of cognate toxin YpjF. Also counteracts the effect of non-cognate toxins CbtA and YfkI.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Chaperone Hsp70, with co-chaperone DnaJ; Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Modulator of gene expression, with H-NS; Down-regulates hemolysin (hly) expression in complex with H- NS. Stimulates transposition events in vivo. Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repre [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Transcriptional repressor of SOS regulon; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment .The SOS response controls an apoptotic-like death (ALD) induced (in the absence [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

DNA-binding ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Antitoxin of the ChpA-ChpR toxin-antitoxin system; Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MazF endoribonuclease toxin and neutralizes its endoribonuclease activity. Is considered to be an 'addiction' molecule as the cell dies in its absence. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium the overexpression of MazF leads to programmed cell death. Cell growth and viability are not affected when MazF and M [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

mRNA interferase toxin, antitoxin is MazE; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single- strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs. Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A. Digests 16S rRNA in vivo 43 nts upstream of the C- terminus; this remove [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Qin prophage; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. In vitro mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl- tRNA in the P site as well as on free 30S subunits. In vivo [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Antitoxin of the YoeB-YefM toxin-antitoxin system; Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that counteracts the effect of the YoeB toxin. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

Toxin of the YoeB-YefM toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription [...]

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE.

ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...]

DNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.