regulatory protein BlaR1 [Staphylococcus aureus]
M56 family metallopeptidase( domain architecture ID 11467994)
M56 family metallopeptidase is an integral membrane metallopeptidase, containing a zinc-binding HEXXH motif; it allows bacteria to respond to presence of beta-lactam antibiotics by expression of beta-lactamases and penicillin-binding proteins; similar to transmembrane proteins BlaR1 and MecR1
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
110-324 | 1.12e-31 | ||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; : Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 121.31 E-value: 1.12e-31
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Name | Accession | Description | Interval | E-value | |||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
110-324 | 1.12e-31 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 121.31 E-value: 1.12e-31
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Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
27-298 | 1.31e-23 | |||||
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: 98.31 E-value: 1.31e-23
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
109-302 | 2.50e-22 | |||||
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: 92.39 E-value: 2.50e-22
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Name | Accession | Description | Interval | E-value | |||||
MecR1 | COG4219 | Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ... |
110-324 | 1.12e-31 | |||||
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms]; Pssm-ID: 443363 [Multi-domain] Cd Length: 337 Bit Score: 121.31 E-value: 1.12e-31
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Peptidase_M56 | pfam05569 | BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ... |
27-298 | 1.31e-23 | |||||
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: 98.31 E-value: 1.31e-23
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M56_BlaR1_MecR1_like | cd07341 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
109-302 | 2.50e-22 | |||||
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: 92.39 E-value: 2.50e-22
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M56_BlaR1_MecR1_like | cd07326 | Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ... |
198-248 | 9.82e-07 | |||||
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: 48.07 E-value: 9.82e-07
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M48B_HtpX_like | cd07337 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ... |
194-248 | 6.44e-03 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Pssm-ID: 320696 [Multi-domain] Cd Length: 203 Bit Score: 37.29 E-value: 6.44e-03
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Blast search parameters | ||||
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