| NZ_CP022528.1|WP_067500848.1|968330_968627_-|envelope-stress-response-membrane-protein-PspB |
gnl|CDD|132021 |
TIGR02976, Phage_shock_protein_B., phage shock protein B. This model describes the PspB protein of the psp (phage shock protein) operon, as found in Escherichia coli and many related species. Expression of a phage protein called secretin protein IV, and a number of other stresses including ethanol, heat shock, and defects in protein secretion trigger sigma-54-dependent expression of the phage shock regulon. PspB is both a regulator and an effector protein of the phage shock response. [Cellular processes, Adaptations to atypical conditions].
|
9.84107e-26 |
| NZ_CP022528.1|WP_082837410.1|977054_977435_+|PaaI-family-thioesterase |
gnl|CDD|239527 |
cd03443, PaaI_thioesterase, PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).
|
2.59189e-25 |
| NZ_CP022528.1|WP_067468108.1|977973_978375_+|30S-ribosome-binding-factor-RbfA |
gnl|CDD|234787 |
PRK00521, rbfA, 30S ribosome-binding factor RbfA.
|
5.1297e-35 |
| NZ_CP022528.1|WP_067468099.1|982511_982781_+|30S-ribosomal-protein-S15 |
gnl|CDD|180170 |
PRK05626, rpsO, 30S ribosomal protein S15; Reviewed.
|
3.1336e-54 |
| NZ_CP022528.1|WP_067502483.1|980803_981496_+|site-2-protease-family-protein |
gnl|CDD|100079 |
cd06158, S2P-M50_like_1, Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.
|
2.82921e-60 |
| NZ_CP022528.1|WP_094062661.1|968632_969322_-|phage-shock-protein-PspA |
gnl|CDD|274372 |
TIGR02977, phage_shock_protein_A, phage shock protein A. Members of this family are the phage shock protein PspA, from the phage shock operon. This is a narrower family than the set of PspA and its homologs, sometimes several in a genome, as described by pfam04012. PspA appears to maintain the protonmotive force under stress conditions that include overexpression of certain phage secretins, heat shock, ethanol, and protein export defects. [Cellular processes, Adaptations to atypical conditions].
|
5.38993e-84 |
| NZ_CP022528.1|WP_067468136.1|967956_968334_-|envelope-stress-response-membrane-protein-PspC |
gnl|CDD|132023 |
TIGR02978, Phage_shock_protein_C., phage shock protein C. All members of this protein family are the phage shock protein PspC. These proteins contain a PspC domain, as do other members of the larger family of proteins described by pfam04024. The phage shock regulon is restricted to the Proteobacteria and somewhat sparsely distributed there. It is expressed, under positive control of a sigma-54-dependent transcription factor, PspF, which binds and is modulated by PspA. Stresses that induce the psp regulon include phage secretin overexpression, ethanol, heat shock, and protein export defects. [Cellular processes, Adaptations to atypical conditions].
|
2.38514e-45 |
| NZ_CP022528.1|WP_067468118.1|976581_977013_+|PaaI-family-thioesterase |
gnl|CDD|239527 |
cd03443, PaaI_thioesterase, PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).
|
5.3361e-24 |
| NZ_CP022528.1|WP_094062665.1|978445_980098_-|AbgT-family-transporter |
gnl|CDD|367668 |
pfam03806, ABG_transport, AbgT putative transporter family.
|
0 |
| NZ_CP022528.1|WP_067468140.1|966975_967284_-|hypothetical-protein |
gnl|CDD|269842 |
cd14694, bZIP_NFIL3, Basic leucine zipper (bZIP) domain of Nuclear factor interleukin-3-regulated protein (NFIL3): a DNA-binding and dimerization domain. NFIL3, also called E4 promoter-binding protein 4 (E4BP4), is a Basic leucine zipper (bZIP) transcription factor that was independently identified as a transactivator of the IL3 promoter in T-cells and as a transcriptional repressor that binds to a DNA sequence site in the adenovirus E4 promoter. Its expression levels are regulated by cytokines and it plays crucial functions in the immune system. It is required for the development of natural killer cells and CD8+ conventional dendritic cells. In B-cells, NFIL3 mediates immunoglobulin heavy chain class switching that is required for IgE production, thereby influencing allergic and pathogenic immune responses. It is also involved in the polarization of T helper responses. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
|
0.000209149 |
| NZ_CP022528.1|WP_094062664.1|977431_977974_+|DUF1697-domain-containing-protein |
gnl|CDD|377954 |
pfam08002, DUF1697, Protein of unknown function (DUF1697). This family contains many hypothetical bacterial proteins.
|
1.37005e-33 |
| NZ_CP022528.1|WP_067468127.1|971056_971635_+|ribosome-maturation-protein-RimP |
gnl|CDD|237773 |
PRK14636, PRK14636, ribosome maturation protein RimP.
|
8.05158e-85 |
| NZ_CP022528.1|WP_067468123.1|973276_973990_+|DUF448-domain-containing-protein |
gnl|CDD|236401 |
PRK09190, PRK09190, RNA-binding protein.
|
6.67783e-45 |
| NZ_CP022528.1|WP_094062666.1|980200_980779_+|thymidine-kinase |
gnl|CDD|235272 |
PRK04296, PRK04296, thymidine kinase; Provisional.
|
1.15589e-99 |
| NZ_CP022528.1|WP_094062667.1|982951_985228_+|polyribonucleotide-nucleotidyltransferase |
gnl|CDD|236995 |
PRK11824, PRK11824, polynucleotide phosphorylase/polyadenylase; Provisional.
|
0 |
| NZ_CP022528.1|WP_067500842.1|971634_973296_+|transcription-termination/antitermination-protein-NusA |
gnl|CDD|236410 |
PRK09202, nusA, transcription elongation factor NusA; Validated.
|
0 |
| NZ_CP022528.1|WP_067468485.1|981492_982506_+|tRNA-pseudouridine(55)-synthase-TruB |
gnl|CDD|235442 |
PRK05389, truB, tRNA pseudouridine synthase B; Provisional.
|
6.50706e-115 |
| NZ_CP022528.1|WP_094062662.1|969844_970867_+|phage-shock-protein-operon-transcriptional-activator |
gnl|CDD|274371 |
TIGR02974, psp_operon_transcriptional_activator, psp operon transcriptional activator PspF. Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions].
|
1.14885e-175 |
