M56 family metallopeptidase [Acetivibrio thermocellus]
MecR1 family protein( domain architecture ID 11467994)
MecR1 family protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
120-430 | 1.47e-61 | ||||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; : Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 203.74 E-value: 1.47e-61
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Name | Accession | Description | Interval | E-value | ||||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
120-430 | 1.47e-61 | ||||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 203.74 E-value: 1.47e-61
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Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
6-281 | 4.43e-54 | ||||||
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: 182.67 E-value: 4.43e-54
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
119-285 | 1.01e-48 | ||||||
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: 165.20 E-value: 1.01e-48
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Name | Accession | Description | Interval | E-value | ||||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
120-430 | 1.47e-61 | ||||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 203.74 E-value: 1.47e-61
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Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
6-281 | 4.43e-54 | ||||||
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: 182.67 E-value: 4.43e-54
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
119-285 | 1.01e-48 | ||||||
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: 165.20 E-value: 1.01e-48
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DUF4825 | pfam16107 | Domain of unknown function (DUF4825); This domain forms the N-terminal, extracellular domain ... |
324-423 | 1.30e-33 | ||||||
Domain of unknown function (DUF4825); This domain forms the N-terminal, extracellular domain of some homologs of Staph BlaR1 proteases, where it replaces the penicillin-binding domain of BlaR1. It is also found in many uncharacterized proteins in a broad range of bacteria. Its association with BlaR1 homologs suggests it may be involved in substrate-, possibly antibiotic-binding, but this prediction has not been verified experimentally. Pssm-ID: 435140 Cd Length: 95 Bit Score: 121.98 E-value: 1.30e-33
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M56_BlaR1_MecR1_like | cd07326 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
162-283 | 4.42e-12 | ||||||
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: 320685 [Multi-domain] Cd Length: 165 Bit Score: 64.25 E-value: 4.42e-12
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M56_like | cd07329 | Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ... |
161-268 | 4.87e-08 | ||||||
Peptidase M56-like, integral membrane metallopeptidase in bacteria; 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 beta-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: 320688 [Multi-domain] Cd Length: 188 Bit Score: 52.84 E-value: 4.87e-08
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Blast search parameters | ||||
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