MULTISPECIES: M56 family metallopeptidase [Bacillus]
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 ... |
17-324 | 2.11e-61 | |||||
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: 199.23 E-value: 2.11e-61
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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 ... |
17-324 | 2.11e-61 | |||||
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: 199.23 E-value: 2.11e-61
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MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
135-378 | 2.31e-59 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 195.65 E-value: 2.31e-59
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
135-328 | 1.06e-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: 162.88 E-value: 1.06e-48
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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 ... |
17-324 | 2.11e-61 | |||||
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: 199.23 E-value: 2.11e-61
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MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
135-378 | 2.31e-59 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 195.65 E-value: 2.31e-59
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
135-328 | 1.06e-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: 162.88 E-value: 1.06e-48
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M56_BlaR1_MecR1_like | cd07326 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
199-321 | 4.91e-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: 63.48 E-value: 4.91e-12
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M48_Ste24p_like | cd07325 | M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ... |
163-276 | 2.16e-03 | |||||
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 family Ste24p-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Some members also contain ankyrin domains which occur in very diverse families of proteins and mediate protein-protein interactions. Pssm-ID: 320684 [Multi-domain] Cd Length: 199 Bit Score: 38.74 E-value: 2.16e-03
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HtpX | COG0501 | Zn-dependent protease with chaperone function [Posttranslational modification, protein ... |
199-270 | 3.60e-03 | |||||
Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440267 [Multi-domain] Cd Length: 210 Bit Score: 38.33 E-value: 3.60e-03
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Blast search parameters | ||||
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