peptidase M56 (plasmid) [Clostridioides difficile]
M56 family metallopeptidase( domain architecture ID 1009010)
M56 family metallopeptidase that includes transmembrane proteins BlaR1 and MecR1, consisting of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 super family | cl29776 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
10-267 | 4.87e-45 | |||||
BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which mediate staphylococcal resistance to beta-lactam antibiotics) is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. homologs to this peptidase domain, which corresponds to Merops family M56, are also found in a number of other bacterial genome sequences. The actual alignment was detected with superfamily member pfam05569: Pssm-ID: 428523 Cd Length: 296 Bit Score: 155.32 E-value: 4.87e-45
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Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
10-267 | 4.87e-45 | |||||
BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which mediate staphylococcal resistance to beta-lactam antibiotics) is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. homologs to this peptidase domain, which corresponds to Merops family M56, are also found in a number of other bacterial genome sequences. Pssm-ID: 428523 Cd Length: 296 Bit Score: 155.32 E-value: 4.87e-45
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MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
85-277 | 2.46e-41 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 146.73 E-value: 2.46e-41
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
84-266 | 1.08e-39 | |||||
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized. Pssm-ID: 320700 [Multi-domain] Cd Length: 187 Bit Score: 137.85 E-value: 1.08e-39
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Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
10-267 | 4.87e-45 | |||||
BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which mediate staphylococcal resistance to beta-lactam antibiotics) is regulated by a signal-transducing integral membrane protein and a transcriptional repressor. The signal transducer is a fusion protein with penicillin-binding and zinc metalloprotease domains. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. homologs to this peptidase domain, which corresponds to Merops family M56, are also found in a number of other bacterial genome sequences. Pssm-ID: 428523 Cd Length: 296 Bit Score: 155.32 E-value: 4.87e-45
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MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
85-277 | 2.46e-41 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 146.73 E-value: 2.46e-41
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
84-266 | 1.08e-39 | |||||
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized. Pssm-ID: 320700 [Multi-domain] Cd Length: 187 Bit Score: 137.85 E-value: 1.08e-39
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Blast search parameters | ||||
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