M56 family metallopeptidase [Listeria monocytogenes]
M56 family metallopeptidase( domain architecture ID 12063881)
M56 family metallopeptidase with similarity to integral membrane zinc metallopeptidases BlaR1 and MecR1
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
6-296 | 7.47e-114 | |||||
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: 332.51 E-value: 7.47e-114
|
|||||||||
Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
6-296 | 7.47e-114 | |||||
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: 332.51 E-value: 7.47e-114
|
|||||||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
109-326 | 4.13e-53 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 178.32 E-value: 4.13e-53
|
|||||||||
M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
105-299 | 1.84e-44 | |||||
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: 150.94 E-value: 1.84e-44
|
|||||||||
Name | Accession | Description | Interval | E-value | |||||
Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
6-296 | 7.47e-114 | |||||
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: 332.51 E-value: 7.47e-114
|
|||||||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
109-326 | 4.13e-53 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 178.32 E-value: 4.13e-53
|
|||||||||
M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
105-299 | 1.84e-44 | |||||
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: 150.94 E-value: 1.84e-44
|
|||||||||
M56_BlaR1_MecR1_like | cd07326 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
174-269 | 8.27e-08 | |||||
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: 51.15 E-value: 8.27e-08
|
|||||||||
M56_like | cd07329 | Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ... |
145-269 | 1.51e-04 | |||||
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: 42.05 E-value: 1.51e-04
|
|||||||||
Blast search parameters | ||||
|