Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:6.3.4.6 (
urease
)
7,490
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The DNA sequence has been determined upstream of the amiE structural gene in the amidase operon of Rhodococcus sp. R312 and a new ORF (amiS2) identified. The amiS2 gene encodes a potential 206 amino acid (aa) protein containing a high proportion of hydrophobic residues. The AmiS2 protein possesses high homology to the ORFP3, amiS and ureI gene products from the Mycobacterium smegmatis (Ms) acetamidase operon, Pseudomonas aeruginosa (Pa) amidase operon and Helicobacter pylori (Hp)
urease
operon, respectively. Hydropathic analysis and secondary structure prediction of AmiS2 suggested the presence of seven potential transmembrane (TM) alpha-helices. Sequence analysis of the amiB2 gene, located downstream of the Rhodococcus sp. R312 amiE gene, showed that it encoded a 351-aa protein containing a potential ATP-binding motif. AmiB2 showed significant homology with the ATP-binding subunit of the bacterial
Clp protease
and high homology with the amiB product located within the Pa amidase operon. AmiB2 and AmiS2 appear to be two components of a recently identified novel family of ABC transporters (Wilson et al., 1995) and might be responsible for the adsorption of amidase substrates or release of their hydrolysis products.
...
PMID:Amide metabolism: a putative ABC transporter in Rhodococcus sp. R312. 898 91
In living cells intracellular proteolysis is crucial for protein homeostasis, and
ClpP
proteases are conserved between eubacteria and the organelles of eukaryotic cells. In Staphylococcus aureus,
ClpP
associates to the substrate specificity factors, ClpX and ClpC forming two
ClpP
proteases, ClpXP and ClpCP. To address how individual
ClpP
proteases impact cell physiology, we constructed a S. aureus mutant expressing ClpX with an I
265
E substitution in the
ClpP
recognition tripeptide of ClpX. This mutant cannot degrade established ClpXP substrates confirming that the introduced amino acid substitution abolishes ClpXP activity. Phenotypic characterization of this mutant showed that ClpXP activity controls cell size and is required for growth at low temperature. Cells expressing the ClpX
I265E
variant, in contrast to cells lacking
ClpP
, are not sensitive to heat-stress and do not accumulate protein aggregates showing that ClpXP is dispensable for degradation of unfolded proteins in S. aureus. Consistent with this finding, transcriptomic profiling revealed strong induction of genes responding to protein folding stress in cells devoid of
ClpP
, but not in cells lacking only ClpXP. In the latter cells, highly upregulated loci include the
urease
operon, the pyrimidine biosynthesis operon, the betA-betB operon, and the pathogenicity island, SaPI5, while virulence genes were dramatically down-regulated.
...
PMID:The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus. 2892 69
