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Conserved domains on  [gi|446794665|ref|WP_000871921|]
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MULTISPECIES: M56 family metallopeptidase [Bacillus]

Protein Classification

M56 family metallopeptidase( domain architecture ID 11574413)

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; includes transmembrane proteins BlaR1 and MecR1

Gene Ontology:  GO:0008233|GO:0046872|GO:0016020
MEROPS:  M56
PubMed:  11239156

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 78-236 1.04e-40

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: 138.21  E-value: 1.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  78 WRQFFYSKRLQK-----VLIPFIRKGKQIYILPTAEVAAFTIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDP 152
Cdd:cd07326    1 VRRLRRRRRLRRlllllLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 153 LKLFCFTLLAEGMMYIPVLKGLLQRYHTYQELAADKYAMQKMeSSFELGSALLKLIKIKTMENRCVTASFAKTAIN-LRI 231
Cdd:cd07326   81 LLLLLASALARALPFLPLLRRLAAAYRLLRELAADDAAARRV-GPRALASALLKLARAGAPAAPAGALAFAGAAVNeARI 159


                 ....*
gi 446794665 232 EQVLN 236
Cdd:cd07326  160 RRLLD 164
 
Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 78-236 1.04e-40

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: 138.21  E-value: 1.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  78 WRQFFYSKRLQK-----VLIPFIRKGKQIYILPTAEVAAFTIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDP 152
Cdd:cd07326    1 VRRLRRRRRLRRlllllLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 153 LKLFCFTLLAEGMMYIPVLKGLLQRYHTYQELAADKYAMQKMeSSFELGSALLKLIKIKTMENRCVTASFAKTAIN-LRI 231
Cdd:cd07326   81 LLLLLASALARALPFLPLLRRLAAAYRLLRELAADDAAARRV-GPRALASALLKLARAGAPAAPAGALAFAGAAVNeARI 159


                 ....*
gi 446794665 232 EQVLN 236
Cdd:cd07326  160 RRLLD 164
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 62-267 1.65e-13

Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms];


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 69.31  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  62 IAGFLLLTVFIVcKRIWRQFFYSKRLQKVLIPFIRK-----------GKQIYILPTAEVAA-FTIGLFRPKVVISKGMiQ 129
Cdd:COG4219    2 LAGVLLLLLRLL-ISLLRLRRLLRRARPVTDEELLEllerlarrlgiRRPVRLLESDRITSpFSFGLLRPVILLPAGL-E 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 130 TFSDEEMDAIIFHEEYHQNNHDPLKLFCFTLLAEGMMYIPVLKGLLQRYHTYQELAADKYAMQKMESSFELGSALLKLIK 209
Cdd:COG4219   80 ELSEEELEAILAHELAHIRRRDLLDNLLAELLLALFWFNPLVWLARRRLRLDRELACDAAVLKAGGDRKAYAETLLKLAE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446794665 210 IKTMENRCVTASFAKTAINLRIEQVLNEKvvkltiplhTNSVYVTLGLFCMSVVLIVG 267
Cdd:COG4219  160 RRSQPALALAFGGSKSTLKKRIKMLLKSK---------SKRRSRLKLLLALLLALLLA 208
Peptidase_M56 pfam05569
BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ...
 95-232 1.53e-04

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: 42.46  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665   95 IRKGKQIYILPTAEVAAFtIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDPLklfcFTLLAEGMMYI----PV 170
Cdd:pfam05569 153 IKRPITISLSSNIDSPAV-LGLWKPRIVLPADFDTRLSGEEIDYILAHELSHLKRGDLI----INLLVAVLQCLhwfnPL 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446794665  171 LKGLLQRYHTYQELAADKYAMQKMESS--FELGSALLKLIKIKTMENR---CVTASFAKTAINLRIE 232
Cdd:pfam05569 228 VHLAFRKIRIDQELACDAAVLARLHPHerKEYGRTLLKLLAGPSNHIVpvaCVWLAGAKSALKERIM 294
 
Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 78-236 1.04e-40

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: 138.21  E-value: 1.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  78 WRQFFYSKRLQK-----VLIPFIRKGKQIYILPTAEVAAFTIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDP 152
Cdd:cd07326    1 VRRLRRRRRLRRlllllLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 153 LKLFCFTLLAEGMMYIPVLKGLLQRYHTYQELAADKYAMQKMeSSFELGSALLKLIKIKTMENRCVTASFAKTAIN-LRI 231
Cdd:cd07326   81 LLLLLASALARALPFLPLLRRLAAAYRLLRELAADDAAARRV-GPRALASALLKLARAGAPAAPAGALAFAGAAVNeARI 159


                 ....*
gi 446794665 232 EQVLN 236
Cdd:cd07326  160 RRLLD 164
M56_BlaR1_MecR1_like cd07341
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 60-238 5.11e-16

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: 73.90  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  60 IIIAGFLLLTVFIVCKriWRQFFYSKRLQKVLIPF----------IRKGKQIYILPTAEVAaFTIGLFRPKVVISKGMIq 129
Cdd:cd07341    1 IWLAGALLLLLRLLRG--LLRLRRLRRRAEPVPDSlllelarrlgLRRSVRLSVSALVASP-MVVGLFRPVILLPEGLL- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 130 TFSDEEMDAIIFHEEYHQNNHDPL-KLFCftLLAEGMM-YIPVLKGLLQRYHTYQELAADKYAMQKMESSFELGSALLKL 207
Cdd:cd07341   77 EGSPEELRAILLHELAHIRRRDLLvNLLQ--RLLEALFwFNPLVWLLSRRLRLERELACDEAVLAALGDKEDYAEALLRL 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446794665 208 IKIKTMENRCVTASFAKTAINL--RIEQVLNEK 238
Cdd:cd07341  155 AERRSQPPPALALALAGSKSLLkrRIKRILKKK 187
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 62-267 1.65e-13

Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms];


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 69.31  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  62 IAGFLLLTVFIVcKRIWRQFFYSKRLQKVLIPFIRK-----------GKQIYILPTAEVAA-FTIGLFRPKVVISKGMiQ 129
Cdd:COG4219    2 LAGVLLLLLRLL-ISLLRLRRLLRRARPVTDEELLEllerlarrlgiRRPVRLLESDRITSpFSFGLLRPVILLPAGL-E 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 130 TFSDEEMDAIIFHEEYHQNNHDPLKLFCFTLLAEGMMYIPVLKGLLQRYHTYQELAADKYAMQKMESSFELGSALLKLIK 209
Cdd:COG4219   80 ELSEEELEAILAHELAHIRRRDLLDNLLAELLLALFWFNPLVWLARRRLRLDRELACDAAVLKAGGDRKAYAETLLKLAE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446794665 210 IKTMENRCVTASFAKTAINLRIEQVLNEKvvkltiplhTNSVYVTLGLFCMSVVLIVG 267
Cdd:COG4219  160 RRSQPALALAFGGSKSTLKKRIKMLLKSK---------SKRRSRLKLLLALLLALLLA 208
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 100-207 2.78e-08

Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 52.96  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 100 QIYILPTAEVAAFTIGLFR--PKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDPLKLFCFTLLAEGMMYI--------- 168
Cdd:COG0501   21 EVYVMDSPAPNAFATGRGPnnARIVVTDGLLELLDRDELEAVLAHELGHIKNGDILLMTLASGLLGLIGFLarllplafg 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446794665 169 -----------------PVLKGLLQRYHT-YQELAADKYAMQKMESSFELGSALLKL 207
Cdd:COG0501  101 rdrdaglllglllgilaPFLATLIQLALSrKREYEADRAAAELTGDPDALASALRKL 157
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 101-207 2.22e-06

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: 47.22  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665 101 IYILPTAEVAAFTIGLF-RPKVVISKGMIQTFSDEEMDAIIFHEEYH-QNNHdplkLFCFTLLAEGMM---------YIP 169
Cdd:cd07325   34 LYVYQSPVLNAFALGFEgRPFIVLNSGLVELLDDDELRFVIGHELGHiKSGH----VLYRTLLLLLLLlgeligillLSS 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446794665 170 VLKGLLQRYHTYQELAADKYAM---QKMESSFelgSALLKL 207
Cdd:cd07325  110 ALPLALLAWSRAAEYSADRAGLlvcQDPEAAI---RALMKL 147
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 98-208 5.26e-06

Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases; This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and 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. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320682 [Multi-domain]  Cd Length: 94  Bit Score: 43.98  E-value: 5.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  98 GKQIYILPTAEVAAFTIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHdplklfcftllaegmmyipvlkgllqr 177
Cdd:cd05843   17 LDKVVVVPGSVPNAFFTGGANKRVVLTTALLELLSEEELAAVIAHELGHFKAH--------------------------- 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446794665 178 yhtyqELAADKYAmQKMESSFELGSALLKLI 208
Cdd:cd05843   70 -----EYQADNVG-ARLFGKNELDAALLKLI 94
Peptidase_M56 pfam05569
BlaR1 peptidase M56; Production of beta-Lactamase and penicillin-binding protein 2a (which ...
 95-232 1.53e-04

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: 42.46  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665   95 IRKGKQIYILPTAEVAAFtIGLFRPKVVISKGMIQTFSDEEMDAIIFHEEYHQNNHDPLklfcFTLLAEGMMYI----PV 170
Cdd:pfam05569 153 IKRPITISLSSNIDSPAV-LGLWKPRIVLPADFDTRLSGEEIDYILAHELSHLKRGDLI----INLLVAVLQCLhwfnPL 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446794665  171 LKGLLQRYHTYQELAADKYAMQKMESS--FELGSALLKLIKIKTMENR---CVTASFAKTAINLRIE 232
Cdd:pfam05569 228 VHLAFRKIRIDQELACDAAVLARLHPHerKEYGRTLLKLLAGPSNHIVpvaCVWLAGAKSALKERIM 294
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 57-190 1.18e-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: 39.22  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446794665  57 LIRIIIAG------FLLLTVFIVCKRIWRQ------FFYSKRLQKVLIPFIRKGKQ--IYILPTAEVAAFTIGlfRPKVV 122
Cdd:cd07337    3 LVAILIGIspfgesILRALSGCRIRRGARKptrrelEEINPELEDKARRLGPDPEKvkLFISDDEYPNAFALG--RNTIC 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446794665 123 ISKGMIQTFSDEEMDAIIFHEEYHQNNHDPLKLFCFTLLAeGMMYIPVLKGLLQRYHT----------YQELAADKYA 190
Cdd:cd07337   81 VTKGLLDLLDYEELKGILAHELGHLSHKDTDYLLLIFVLL-LLAAIWTKLGTLLIFVWirllvmfssrKAEYRADAFA 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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