cell death peptidase Lit [Escherichia coli str. K-12 substr. MG1655]
Protein Classification
PRK09672 family protein( domain architecture ID 10013311)
PRK09672 family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK09672 | PRK09672 | phage exclusion protein Lit; Provisional |
1-293 | 2.53e-124 | |||||
phage exclusion protein Lit; Provisional : Pssm-ID: 236611 Cd Length: 305 Bit Score: 357.20 E-value: 2.53e-124
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| PRK09672 | PRK09672 | phage exclusion protein Lit; Provisional |
1-293 | 2.53e-124 | |||||
phage exclusion protein Lit; Provisional Pssm-ID: 236611 Cd Length: 305 Bit Score: 357.20 E-value: 2.53e-124
|
|||||||||
| Peptidase_U49 | pfam10463 | Peptidase U49; This family contains Lit peptidase from Escherichia coli. Lit protease ... |
61-258 | 1.52e-112 | |||||
Peptidase U49; This family contains Lit peptidase from Escherichia coli. Lit protease functions in bacterial cell death in response to infection by bacteriophage T4. Following binding of Gol peptide to domains II and III of elongation factor Tu, the Lit peptidase cleaves domain I of the elongation factor. This prevents binding of guanine nucleotides, shuts down translation and leads to cell death. Pssm-ID: 402201 Cd Length: 198 Bit Score: 323.46 E-value: 1.52e-112
|
|||||||||
| M48C_bepA_like | cd07333 | Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ... |
155-239 | 3.44e-05 | |||||
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture. Pssm-ID: 320692 [Multi-domain] Cd Length: 174 Bit Score: 43.63 E-value: 3.44e-05
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| PRK09672 | PRK09672 | phage exclusion protein Lit; Provisional |
1-293 | 2.53e-124 | |||||
phage exclusion protein Lit; Provisional Pssm-ID: 236611 Cd Length: 305 Bit Score: 357.20 E-value: 2.53e-124
|
|||||||||
| Peptidase_U49 | pfam10463 | Peptidase U49; This family contains Lit peptidase from Escherichia coli. Lit protease ... |
61-258 | 1.52e-112 | |||||
Peptidase U49; This family contains Lit peptidase from Escherichia coli. Lit protease functions in bacterial cell death in response to infection by bacteriophage T4. Following binding of Gol peptide to domains II and III of elongation factor Tu, the Lit peptidase cleaves domain I of the elongation factor. This prevents binding of guanine nucleotides, shuts down translation and leads to cell death. Pssm-ID: 402201 Cd Length: 198 Bit Score: 323.46 E-value: 1.52e-112
|
|||||||||
| M48C_bepA_like | cd07333 | Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ... |
155-239 | 3.44e-05 | |||||
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture. Pssm-ID: 320692 [Multi-domain] Cd Length: 174 Bit Score: 43.63 E-value: 3.44e-05
|
|||||||||
| M48C_Oma1-like | cd07324 | Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ... |
154-239 | 1.17e-04 | |||||
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins. Pssm-ID: 320683 [Multi-domain] Cd Length: 142 Bit Score: 41.40 E-value: 1.17e-04
|
|||||||||
| Blast search parameters | ||||
|
