NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1490642194|gb|RLC35399|]
View 

hypothetical protein DRZ76_00255 [Candidatus Nealsonbacteria bacterium]

Protein Classification

zinc metalloprotease HtpX( domain architecture ID 11980093)

zinc metalloprotease HtpX is an integral membrane metallopeptidase that plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane; also contains C-terminal transcription factor zinc-fingers

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Peptidase_M48_M56 super family cl28898
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 87-313 3.92e-48

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.


The actual alignment was detected with superfamily member cd07340:

Pssm-ID: 333718 [Multi-domain]  Cd Length: 246  Bit Score: 167.29  E-value: 3.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  87 MAQAAGARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVA 166
Cdd:cd07340    14 VLAMSGAREITRED--EPRLYNVVEELAIAAGLPMPKVYIIDDPAPNAFATGRNPEHAVIAVTTGLLEKLNRDELEGVIA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 167 HEAAHIVCGDSLLATV-------ITSLSELYEEALFKMKAALRGSRGRGSALFFLLYIVLLGM----NTLSKMLHFFLSR 235
Cdd:cd07340    92 HELSHIKNYDIRLMTIavvlvgiIALIADLALRSFFYGGGSRRRRRDGGGGGALILLILGLVLiilaPIFAQLIQLAISR 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490642194 236 QREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGARLESIFIVNPrhswLDEREGLLSIMFSTHPPIKKRINLL 313
Cdd:cd07340   172 QREYLADASAVELTRNPEGLISALEKISGDSSPLKVANSATAHLNLYFP----NPGKKSSFSSLFSTHPPIEERIKRL 245
COG3809 COG3809
Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction ...
 490-540 1.53e-09

Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only];


:

Pssm-ID: 443022  Cd Length: 59  Bit Score: 53.90  E-value: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 490 MDCPRCKQKMhrqFFVYSYPVEIERCLFCSGVWFDKQELEILQYLFENQEQ 540
Cdd:COG3809     3 MLCPKCGAPM---RVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAA 50
zf-TFIIB super family cl01565
Transcription factor zinc-finger;
415-468 1.02e-05

Transcription factor zinc-finger;


The actual alignment was detected with superfamily member COG3809:

Pssm-ID: 470253  Cd Length: 59  Bit Score: 43.12  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490642194 415 CPHCKTGLSEFSYEGVHIFKCSFCSGIFLDHDKISRILIRKDMEFCKEVKKLGE 468
Cdd:COG3809     5 CPKCGAPMRVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAARRKSFLSD 58
 
Name Accession Description Interval E-value
M48B_Htpx_like cd07340
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 87-313 3.92e-48

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: 320699 [Multi-domain]  Cd Length: 246  Bit Score: 167.29  E-value: 3.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  87 MAQAAGARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVA 166
Cdd:cd07340    14 VLAMSGAREITRED--EPRLYNVVEELAIAAGLPMPKVYIIDDPAPNAFATGRNPEHAVIAVTTGLLEKLNRDELEGVIA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 167 HEAAHIVCGDSLLATV-------ITSLSELYEEALFKMKAALRGSRGRGSALFFLLYIVLLGM----NTLSKMLHFFLSR 235
Cdd:cd07340    92 HELSHIKNYDIRLMTIavvlvgiIALIADLALRSFFYGGGSRRRRRDGGGGGALILLILGLVLiilaPIFAQLIQLAISR 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490642194 236 QREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGARLESIFIVNPrhswLDEREGLLSIMFSTHPPIKKRINLL 313
Cdd:cd07340   172 QREYLADASAVELTRNPEGLISALEKISGDSSPLKVANSATAHLNLYFP----NPGKKSSFSSLFSTHPPIEERIKRL 245
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 107-317 1.29e-40

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 145.80  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 107 KNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSL 186
Cdd:COG0501     5 YRLVEELAARAGIPMPEVYVMDSPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDILLMTLASGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 187 SELYeEALFKMKAALRGSRGRGSALFFLLYIVLLGMntLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLISEHW 266
Cdd:COG0501    85 LGLI-GFLARLLPLAFGRDRDAGLLLGLLLGILAPF--LATLIQLALSRKREYEADRAAAELTGDPDALASALRKLAGGN 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490642194 267 RGSGAEGARLESI--FIVNPRHswldereglLSIMFSTHPPIKKRINLLLNMA 317
Cdd:COG0501   162 LSIPLRRAFPAQAhaFIINPLK---------LSSLFSTHPPLEERIARLRELA 205
PRK04897 PRK04897
heat shock protein HtpX; Provisional
 62-316 8.38e-34

heat shock protein HtpX; Provisional


Pssm-ID: 235318 [Multi-domain]  Cd Length: 298  Bit Score: 130.07  E-value: 8.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  62 LIVLIAAFFIALLHWVISTNrLIEKMAqaaGARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFN 141
Cdd:PRK04897   44 IIALIIGVIYALIMIFQSTN-VVMSMN---HAREVTEEE--APELWHIVEDMAMVAQIPMPRVFIIDDPSPNAFATGSSP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 142 RRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATV-------ITSLSELYEEALFKMKAALRGSRGR-GSALFF 213
Cdd:PRK04897  118 KNAAVAVTTGLLAIMNREELEGVIGHEISHIRNYDIRLSTIavalasaITLLSDIAGRMMWWGGGSRRRDDDRdGGGLQI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 214 LLYIVLLGMNTLS----KMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGARLESIFIVNPRHSwl 289
Cdd:PRK04897  198 ILLIVSLLLLILAplaaTLIQLAISRQREYLADASSVELTRNPQGLISALEKISNSQPMKHPVDDASAALYISDPLKK-- 275

                         250       260
                  ....*....|....*....|....*..
gi 1490642194 290 dereGLLSIMFSTHPPIKKRINLLLNM 316
Cdd:PRK04897  276 ----KGLSKLFDTHPPIEERIERLKNM 298
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 109-317 2.51e-21

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 92.11  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 109 IVDEVSVAIG--GRKIEAMVIPSAG-TNAFALQDFnRRSVIGVTEGLLARL-NRPQIEAVVAHEAAHIVCGDSLLATVIT 184
Cdd:pfam01435  10 VVERLAAAAGlpLPPWYVVVIKSSPvPNAFAYGLL-PGGRVVVTTGLLDLLeTEDELAAVLGHEIGHIKARHSVESLSIM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 185 SLSELYEEALFKMKAALRGSRGRGSALFFLLYIVLLgMNTLSKMLHFFlSRQREYRADAVGTRLTRNPLSLAEALRLISE 264
Cdd:pfam01435  89 GGLSLAQLFLALLLLGAAASGFANFGIIFLLLIGPL-AALLTLLLLPY-SRAQEYEADRLGAELMARAGYDPRALIKLWG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490642194 265 hwrgsgaEGARLESIFivnprhswldeREGLLSIMFSTHPPIKKRINLLLNMA 317
Cdd:pfam01435 167 -------EIDNNGRAS-----------DGALYPELLSTHPSLVERIAALRERA 201
COG3809 COG3809
Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction ...
 490-540 1.53e-09

Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only];


Pssm-ID: 443022  Cd Length: 59  Bit Score: 53.90  E-value: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 490 MDCPRCKQKMhrqFFVYSYPVEIERCLFCSGVWFDKQELEILQYLFENQEQ 540
Cdd:COG3809     3 MLCPKCGAPM---RVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAA 50
zf-TFIIB pfam13453
Transcription factor zinc-finger;
491-531 7.76e-06

Transcription factor zinc-finger;


Pssm-ID: 433221  Cd Length: 41  Bit Score: 43.06  E-value: 7.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1490642194 491 DCPRCKQKMHRQFFvysYPVEIERCLFCSGVWFDKQELEIL 531
Cdd:pfam13453   1 KCPKCGAELEEVER---DGVEIDYCPQCRGIWLDRGELEKL 38
COG3809 COG3809
Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction ...
 415-468 1.02e-05

Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only];


Pssm-ID: 443022  Cd Length: 59  Bit Score: 43.12  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490642194 415 CPHCKTGLSEFSYEGVHIFKCSFCSGIFLDHDKISRILIRKDMEFCKEVKKLGE 468
Cdd:COG3809     5 CPKCGAPMRVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAARRKSFLSD 58
zf-TFIIB pfam13453
Transcription factor zinc-finger;
415-452 3.85e-05

Transcription factor zinc-finger;


Pssm-ID: 433221  Cd Length: 41  Bit Score: 40.74  E-value: 3.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1490642194 415 CPHCKTGLSEFSYEGVHIFKCSFCSGIFLDHDKISRIL 452
Cdd:pfam13453   2 CPKCGAELEEVERDGVEIDYCPQCRGIWLDRGELEKLL 39
 
Name Accession Description Interval E-value
M48B_Htpx_like cd07340
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 87-313 3.92e-48

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: 320699 [Multi-domain]  Cd Length: 246  Bit Score: 167.29  E-value: 3.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  87 MAQAAGARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVA 166
Cdd:cd07340    14 VLAMSGAREITRED--EPRLYNVVEELAIAAGLPMPKVYIIDDPAPNAFATGRNPEHAVIAVTTGLLEKLNRDELEGVIA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 167 HEAAHIVCGDSLLATV-------ITSLSELYEEALFKMKAALRGSRGRGSALFFLLYIVLLGM----NTLSKMLHFFLSR 235
Cdd:cd07340    92 HELSHIKNYDIRLMTIavvlvgiIALIADLALRSFFYGGGSRRRRRDGGGGGALILLILGLVLiilaPIFAQLIQLAISR 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490642194 236 QREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGARLESIFIVNPrhswLDEREGLLSIMFSTHPPIKKRINLL 313
Cdd:cd07340   172 QREYLADASAVELTRNPEGLISALEKISGDSSPLKVANSATAHLNLYFP----NPGKKSSFSSLFSTHPPIEERIKRL 245
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 107-317 1.29e-40

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 145.80  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 107 KNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSL 186
Cdd:COG0501     5 YRLVEELAARAGIPMPEVYVMDSPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDILLMTLASGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 187 SELYeEALFKMKAALRGSRGRGSALFFLLYIVLLGMntLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLISEHW 266
Cdd:COG0501    85 LGLI-GFLARLLPLAFGRDRDAGLLLGLLLGILAPF--LATLIQLALSRKREYEADRAAAELTGDPDALASALRKLAGGN 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490642194 267 RGSGAEGARLESI--FIVNPRHswldereglLSIMFSTHPPIKKRINLLLNMA 317
Cdd:COG0501   162 LSIPLRRAFPAQAhaFIINPLK---------LSSLFSTHPPLEERIARLRELA 205
M48B_HtpX_like cd07336
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 65-316 9.91e-35

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: 320695 [Multi-domain]  Cd Length: 266  Bit Score: 131.46  E-value: 9.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  65 LIAAFFIALLHWVIS---TNRLIEKMAqaaGARPIDENDI--YHQyfknIVDEVSVAIGGRKIEAMVIPSAGTNAFALQD 139
Cdd:cd07336    18 MIIALLIALGMNFFSywfSDKIVLRMY---GARPVSEEEApeLYQ----IVEELARRAGLPMPKVYIIPSPQPNAFATGR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 140 FNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATV-------ITSLSELyeeALFKMKAALRGSRGRGSALF 212
Cdd:cd07336    91 NPEHAAVAVTTGILRLLDKDELEGVLAHELAHIKNRDILISTIaatiagaISMLANM---AQWGAIFGGRGGRDRGGNPI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 213 FLLYIVLLG--MNTLSKMLhffLSRQREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGAR--LESIFIVNPRHSw 288
Cdd:cd07336   168 GALLLAILApiAATLIQLA---ISRSREYLADETGARISGNPLALASALEKLERGAQRHPPMEANpaTAHLFIVNPLSG- 243

                         250       260
                  ....*....|....*....|....*...
gi 1490642194 289 lderEGLLSiMFSTHPPIKKRINLLLNM 316
Cdd:cd07336   244 ----GGLAK-LFSTHPPTEERIARLRAM 266
PRK04897 PRK04897
heat shock protein HtpX; Provisional
 62-316 8.38e-34

heat shock protein HtpX; Provisional


Pssm-ID: 235318 [Multi-domain]  Cd Length: 298  Bit Score: 130.07  E-value: 8.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  62 LIVLIAAFFIALLHWVISTNrLIEKMAqaaGARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFN 141
Cdd:PRK04897   44 IIALIIGVIYALIMIFQSTN-VVMSMN---HAREVTEEE--APELWHIVEDMAMVAQIPMPRVFIIDDPSPNAFATGSSP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 142 RRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATV-------ITSLSELYEEALFKMKAALRGSRGR-GSALFF 213
Cdd:PRK04897  118 KNAAVAVTTGLLAIMNREELEGVIGHEISHIRNYDIRLSTIavalasaITLLSDIAGRMMWWGGGSRRRDDDRdGGGLQI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 214 LLYIVLLGMNTLS----KMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAEGARLESIFIVNPRHSwl 289
Cdd:PRK04897  198 ILLIVSLLLLILAplaaTLIQLAISRQREYLADASSVELTRNPQGLISALEKISNSQPMKHPVDDASAALYISDPLKK-- 275

                         250       260
                  ....*....|....*....|....*..
gi 1490642194 290 dereGLLSIMFSTHPPIKKRINLLLNM 316
Cdd:PRK04897  276 ----KGLSKLFDTHPPIEERIERLKNM 298
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 29-317 9.47e-34

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 129.74  E-value: 9.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  29 LTTYLILVILENSLVPSsvlsrrGFFFPPASHALIVLIAAFFIALLHWVIStnrliEKMAQAA-GARPIDENDIYHQYfk 107
Cdd:PRK03982    5 LKTGLLMALLTGLLYAI------GYLLGGSIGPIIAILLALIPNLISYYYS-----DKIVLASyNARIVSEEEAPELY-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 108 NIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSL- 186
Cdd:PRK03982   72 RIVERLAERANIPKPKVAIVPTQTPNAFATGRDPKHAVVAVTEGILNLLNEDELEGVIAHELTHIKNRDTLIQTIAATLa 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 187 ---SELYEEALFKM--KAALRGSRGRGSALFFLLYIVLLgmnTLSKML-HFFLSRQREYRADAVGTRLTRNPLSLAEALR 260
Cdd:PRK03982  152 gaiMYLAQWLSWGLwfGGGGRDDRNGGNPIGSLLLIILA---PIAATLiQFAISRQREFSADEGGARLTGNPLALANALQ 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1490642194 261 LISEHWRGSGAEGAR--LESIFIVNPRhswldeREGLLSIMFSTHPPIKKRINLLLNMA 317
Cdd:PRK03982  229 KLEKGVRYIPLKNGNpaTAHMFIINPF------RGQFLANLFSTHPPTEERIERLLEMA 281
PRK03072 PRK03072
heat shock protein HtpX; Provisional
 61-319 1.50e-32

heat shock protein HtpX; Provisional


Pssm-ID: 235102 [Multi-domain]  Cd Length: 288  Bit Score: 126.31  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  61 ALIVLIAAFF------IALLHWVIST-----NRliEKMAQAA-GARPIDENDIYHQYfkNIVDEVSVAIGGRKIEAMVIP 128
Cdd:PRK03072   19 ALIVFIGALFgrtglgIAVLIAVGMNayvywNS--DKLALRAmHAQPVSEVQAPAMY--RIVRELSTAARQPMPRLYISP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 129 SAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSL-------LATVITSLselyeeALFKMKAAL 201
Cdd:PRK03072   95 TAAPNAFATGRNPRNAAVCCTEGILQILNERELRGVLGHELSHVYNRDILissvagaLASVITYL------ANMAMFAGM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 202 RGSRGR--GSALFFLLYIVLLG--MNTLSKMLhffLSRQREYRADAVGTRLTRNPLSLAEALRLISehwrgSGAEGA--- 274
Cdd:PRK03072  169 FGGRRDndGPNPLALLLVSLLGpiAATVIQLA---ISRSREYQADESGAELTGDPLALASALRKIS-----GGVQAAplp 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 275 ---RLES---IFIVNPRhswldeREGLLSIMFSTHPPIKKRINLLLNMAHM 319
Cdd:PRK03072  241 pepQLASqahLMIANPF------RAGGIGRLFSTHPPMADRIARLEQMAGR 285
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 66-313 4.39e-29

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: 320697 [Multi-domain]  Cd Length: 216  Bit Score: 114.60  E-value: 4.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  66 IAAFFIALLHWVISTnRLIEKMAqaaGARPIDENdiyhQYFK--NIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRR 143
Cdd:cd07338     1 IFALIINLIQWLISP-YIINWVY---RAREPPDP----EYPWlqEIVEEVARRAGIKPPKVGIAEDPIPNAFAYGSPLTG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 144 SVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSL-SELYEEALFKMKAALRGSRGRGSALFFLLYIVLLGM 222
Cdd:cd07338    73 ARVAVTRGLLDILNRDELEAVIGHELGHIKHRDVAIMTAIGLIpSIIYYIGRSLLFSGGSSGGRNGGGALLAVGIAAFAV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 223 NTLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEALrlisehwrgsgaegARLESifivnprhswldereGLLSIMFST 302
Cdd:cd07338   153 YFLFQLLVLGFSRLREYYADAHSAKVTGNGRALQSAL--------------AKIAY---------------GYLAEIFST 203

                         250
                  ....*....|.
gi 1490642194 303 HPPIKKRINLL 313
Cdd:cd07338   204 HPLPAKRIQAL 214
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 85-313 4.03e-27

HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its 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 eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding 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. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320686 [Multi-domain]  Cd Length: 183  Bit Score: 107.72  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  85 EKMAQAA-GARPIDENDIYHQYfkNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEA 163
Cdd:cd07327     6 DKLVLRAmGAREVSEEEAPELH--AIVERLARRAGLPKPRVAIVDTPMPNAFATGRNPKNAAVAVTTGLLQLLNEDELEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 164 VVAHEAAHIVCGDSLLATVItslselyeealfkmkaalrgsrgrgsalffllyivllgmntlskmlhfFLSRQREYRADA 243
Cdd:cd07327    84 VLAHELSHIKNRDVLVMTLA------------------------------------------------SLSRYREFAADR 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490642194 244 VGTRLTRNPLSLAEALRLIS---EHWRGSGAEGARLESIFIVNPRHSwldereGLLSIMFSTHPPIKKRINLL 313
Cdd:cd07327   116 GSAKLTGDPLALASALMKISgsmQRIPKRDLRQVEASAFFIIPPLSG------GSLAELFSTHPPTEKRIERL 182
PRK02870 PRK02870
heat shock protein HtpX; Provisional
 27-314 9.21e-27

heat shock protein HtpX; Provisional


Pssm-ID: 235081 [Multi-domain]  Cd Length: 336  Bit Score: 110.96  E-value: 9.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  27 YFLTTYLILVILENSLVPssvLSRRGFFFPPAS-----HALI---------VLIAAFFIALLHWVISTNRLIekMAQAAG 92
Cdd:PRK02870   26 AVIATYLAIFLFIGLLVD---AIRIASEYPAASlgkalLALLtfqifptatLIMSLVAVISILVTFQNFDKI--MLSGTE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  93 ARPID--------ENDIYhqyfkNIVDEVSVAIGGRKIEAMVIPSAG-TNAFALQDFNRRSVIGVTEGLLARLNRPQIEA 163
Cdd:PRK02870  101 YKEITpenalslqERQLY-----NVVEELLVAAGLRFMPKVYIIDAPyMNAFASGYSEKSAMVAITTGLLEKLDRDELQA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 164 VVAHEAAHIVCGDSLLATVITSLSE-LYEEALFKMKAALRGSRGRGSALFFLLYIVL-LGMNTLSKMLHFFLSRQREYRA 241
Cdd:PRK02870  176 VMAHELSHIRHGDIRLTLCVGVLSNiMLIVADFLFYSFMGNRRNSGANRARMIILILrYVLPILTVLLMLFLSRTREYMA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 242 DAVGTRLTRNPLSLAEALRLIS---------EHWRGSGAEGARLESiFIVNPrhswLDEREGLLSIMFSTHPPIKKRINL 312
Cdd:PRK02870  256 DAGAVELMRDNEPMARALQKISndhaqndeqYAYKHTDHESTRRAA-YLFDP----AGISPGSLSDAFSTHPSIENRLAA 330


                  ..
gi 1490642194 313 LL 314
Cdd:PRK02870  331 LG 332
M48B_HtpX_like cd07339
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 126-314 2.82e-25

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: 320698 [Multi-domain]  Cd Length: 229  Bit Score: 104.18  E-value: 2.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 126 VIPSAGTNAFALQDfNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSL---LATVITSLSELYeeALFKMkaalr 202
Cdd:cd07339    51 YVPSRVLNAFAVGS-RKDAAIALTDGLLRRLTLRELAGVLAHEVSHIRNGDLRvmgLADLISRLTSLL--SLLGQ----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 203 gsrgrgSALFFLLYIVLLGMN--------------TLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLIsEHWRG 268
Cdd:cd07339   123 ------LLLLLNLPLLLLGEVtiswlailllilapTLSTLLQLALSRTREFDADLDAARLTGDPEGLASALAKL-ERYQG 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1490642194 269 SGaegarLESIFIV---NPRHSWLDeregllsimfsTHPPIKKRINLLL 314
Cdd:cd07339   196 GW-----WERLLLPgrrVPEPSLLR-----------THPPTEERIRRLL 228
PRK03001 PRK03001
zinc metalloprotease HtpX;
93-317 5.85e-25

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 104.72  E-value: 5.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  93 ARPIDENDiyHQYFKNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHI 172
Cdd:PRK03001   58 AQEVDENT--APQFYRMVRELAQRAGLPMPKVYLINEDQPNAFATGRNPEHAAVAATTGILRVLSEREIRGVMAHELAHV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 173 VCGDSLLATV-------ITSLselyeeALFKMKAALRGSRGRGSALFFLLYIVLLgMNTLSKMLHFFLSRQREYRADAVG 245
Cdd:PRK03001  136 KHRDILISTIsatmagaISAL------ANFAMFFGGRDENGRPVNPIAGIAVAIL-APLAASLIQMAISRAREFEADRGG 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490642194 246 TRLTRNPLSLAEALRLISEHWRGSG--AEGARLES--IFIVNPRHSwldereGLLSIMFSTHPPIKKRINLLLNMA 317
Cdd:PRK03001  209 ARISGDPQALASALDKIHRYASGIPfqAAEAHPATaqMMIINPLSG------GGLANLFSTHPSTEERIARLMAMA 278
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 86-313 4.79e-24

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its 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 eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding 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. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320694 [Multi-domain]  Cd Length: 240  Bit Score: 100.73  E-value: 4.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  86 KMA-QAAGARPIDE--NDIYHQYFkNIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIE 162
Cdd:cd07335    14 WMAkRAMGVKVIDNpsNEKERWLV-ETVAELARKAGIKMPEVGIYPSPDVNAFATGPSRNNSLVAVSTGLLDNMSEDEVE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 163 AVVAHEAAHIVCGD----SLLATVITS----LSELYEEALFKmkaALRGSRGRGSALFFLLYIVL---LGMntLSKMLHF 231
Cdd:cd07335    93 AVLAHEISHIANGDmvtmTLLQGVVNTfvifLSRIIALIIDS---FLSGDENGSGIGYFLVVIVLeivLGI--LASLVVM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 232 FLSRQREYRADAVGTRLTRNPlSLAEAL-RLISEHWRgsgAEGARLESIFIVNPRHSwldereGLLSImFSTHPPIKKRI 310
Cdd:cd07335   168 WFSRKREFRADAGGAKLTGKE-KMIAALeRLKQISER---PESEDDVAAAIKISRGS------GFLRL-FSTHPPLEERI 236


                  ...
gi 1490642194 311 NLL 313
Cdd:cd07335   237 AAL 239
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 62-310 1.70e-21

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 95.00  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  62 LIVLIAAFFiALLHWVIStnrliEKMAQAA-GARPIDENDI--YHQyfknIVDEVSVAIGGRKIEAMVIPSAGTNAFALQ 138
Cdd:PRK02391   41 LIVVIAGGF-LLAQYFFS-----DKLALWSmGARIVSEDEYpeLHA----MVERLCALADLPKPRVAVADSDVPNAFATG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 139 DFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSLSELyeeALFKMKAALRGS------RGRGSALF 212
Cdd:PRK02391  111 RSPKNAVVCVTTGLMRRLDPDELEAVLAHELSHVKNRDVAVMTIASFLSTI---AFLIVRWGFYFGgfggrgGGGGGGGI 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 213 FLLYIVLLGMNTLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEALRLIS--------EHWRgsGAEGArlESIFIVnP 284
Cdd:PRK02391  188 LVVILVSLVVWAISFLLIRALSRYREFAADRGAAIITGRPSALASALMKISgrmdrvptEDLR--EAEGM--NAFFII-P 262

                         250       260
                  ....*....|....*....|....*.
gi 1490642194 285 RHSwlderEGLLSIMFSTHPPIKKRI 310
Cdd:PRK02391  263 ALS-----GGSLGRLFSTHPPLEKRI 283
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 109-317 2.51e-21

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 92.11  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 109 IVDEVSVAIG--GRKIEAMVIPSAG-TNAFALQDFnRRSVIGVTEGLLARL-NRPQIEAVVAHEAAHIVCGDSLLATVIT 184
Cdd:pfam01435  10 VVERLAAAAGlpLPPWYVVVIKSSPvPNAFAYGLL-PGGRVVVTTGLLDLLeTEDELAAVLGHEIGHIKARHSVESLSIM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 185 SLSELYEEALFKMKAALRGSRGRGSALFFLLYIVLLgMNTLSKMLHFFlSRQREYRADAVGTRLTRNPLSLAEALRLISE 264
Cdd:pfam01435  89 GGLSLAQLFLALLLLGAAASGFANFGIIFLLLIGPL-AALLTLLLLPY-SRAQEYEADRLGAELMARAGYDPRALIKLWG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490642194 265 hwrgsgaEGARLESIFivnprhswldeREGLLSIMFSTHPPIKKRINLLLNMA 317
Cdd:pfam01435 167 -------EIDNNGRAS-----------DGALYPELLSTHPSLVERIAALRERA 201
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 126-314 1.26e-20

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: 89.82  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 126 VIPSAGTNAFALqDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSL-LATVITSLSELYEEALFkmkAALRGS 204
Cdd:cd07329    16 VVDSDVPNAFAV-GRSRGPTVVVTTGLLDLLDDDELEAVLAHELAHLKRRDVLvLLLFDPLLLLVVGLLLF---LSLFIF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 205 RGRGSALFFLLYIVLLGMNTLSKMLHFFLSRQREYRADAVgtRLTRNPLSLAEALRLISEhwrGSGAEGARLESIFIVNP 284
Cdd:cd07329    92 ELLGFFFQPLLFLAFFALLRLAELLADALAVARTSAARRA--RLTGLPAALASALEKIED---ASDRALEAGLVLPALAA 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1490642194 285 RHSWLDeregllsimFSTHPPIKKRINLLL 314
Cdd:cd07329   167 DASSLE---------KTDHPPLEERVERLL 187
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 92-317 4.19e-20

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 91.23  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  92 GARPIDENDIyHQYFKNIVDevsvaIGGRKIEAM----VIPSAGTNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAH 167
Cdd:PRK01345   57 GAQEVDERSA-PELYRMVRD-----LARRAGLPMpkvyIIDNPQPNAFATGRNPENAAVAATTGLLQRLSPEEVAGVMAH 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 168 EAAHIVCGDSLLATVITSL----SELYEEALFkmkaaLRGSRGRGSALF-FLLYIVLLGMNTLSKML-HFFLSRQREYRA 241
Cdd:PRK01345  131 ELAHVKNRDTLTMTITATLagaiSMLANFAFF-----FGGNRENNNGPLgLVGTLAAMIVAPLAAMLvQMAISRTREYAA 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 242 DAVGTRLTRNPLSLAEALRLISEHWRGSGAEGArlES------IFIVNPRHSwlderEGLLSiMFSTHPPIKKRINLLLN 315
Cdd:PRK01345  206 DRRGAEICGNPLWLASALGKIERGAHGVPNEEA--ERnpatahMFIINPLSG-----EGMDN-LFSTHPATENRIAALQR 277


                  ..
gi 1490642194 316 MA 317
Cdd:PRK01345  278 MA 279
PRK05457 PRK05457
protease HtpX;
75-316 7.86e-19

protease HtpX;


Pssm-ID: 235478 [Multi-domain]  Cd Length: 284  Bit Score: 86.77  E-value: 7.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  75 HWVISTnrlIEKMAQAAG-ARPidENDIYHqyfknivdevsvaiggrkieamvipSAGTNAFALQDFNRRSVIGVTEGLL 153
Cdd:PRK05457   77 RWLVET---VARQARQAGiGMP--EVAIYH-------------------------SPEINAFATGASKNNSLVAVSTGLL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 154 ARLNRPQIEAVVAHEAAHIVCGD----SLLATVITS----LSELYeeALFKMKAALRGSRGRGSAlFFLLYIVL---LGM 222
Cdd:PRK05457  127 QNMSRDEVEAVLAHEISHIANGDmvtmTLIQGVVNTfvifLSRII--AQIVDRFVSGNEEGNGIG-YFIVSIVLeivFGI 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 223 ntLSKMLHFFLSRQREYRADAVGTRLT-RNPlsLAEAL-RLISEHwrgsgaEGARLESI--FIVNPRHSWLDeregllsi 298
Cdd:PRK05457  204 --LASIIVMWFSRHREFRADAGGAKLAgREK--MIAALqRLKTSY------EPQLPGSMaaFGINGKSGLSE-------- 265

                         250
                  ....*....|....*...
gi 1490642194 299 MFSTHPPIKKRINLLLNM 316
Cdd:PRK05457  266 LFMSHPPLEKRIAALRSG 283
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 64-310 1.12e-16

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: 78.51  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  64 VLIAAFFIALLHWVISTNRLIEKMAQAAGARP--IDENDIYHQYFKNIVDEVSVAIggRKIEAMVIPSAGTNAFALQdfn 141
Cdd:cd07337     1 LLLVAILIGISPFGESILRALSGCRIRRGARKptRRELEEINPELEDKARRLGPDP--EKVKLFISDDEYPNAFALG--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 142 rRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSLSELyeealfkmkaalrgsrgrgSALFFLLYIVLLg 221
Cdd:cd07337    76 -RNTICVTKGLLDLLDYEELKGILAHELGHLSHKDTDYLLLIFVLLLL-------------------AAIWTKLGTLLI- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 222 mNTLSKMLHFFLSRQREYRADAVGTRLTRNPLsLAEALRlisehwrgsgaegaRLESIFivnprhswlDEREGLLSIMFS 301
Cdd:cd07337   135 -FVWIRLLVMFSSRKAEYRADAFAVKIGYGEG-LRSALD--------------QLREYE---------DAPKGFLAALYS 189


                  ....*....
gi 1490642194 302 THPPIKKRI 310
Cdd:cd07337   190 THPPTEKRI 198
PRK01265 PRK01265
heat shock protein HtpX; Provisional
 52-313 8.32e-14

heat shock protein HtpX; Provisional


Pssm-ID: 234931 [Multi-domain]  Cd Length: 324  Bit Score: 72.47  E-value: 8.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  52 GFFFPPASHALIV---LIAAFFIALLHWVISTnRLIEKMAQAAGARPideNDIYHQYFKNIVDEVSVAIGGRKIEAMVIP 128
Cdd:PRK01265   32 YYAFGAQFGVGLIlgiLIFVFFLNIIQWLFGP-YMINAAYRTVEVTP---TDPVYGWLYSIVAEVAKYNGIRVPKVYIAD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 129 SAGTNAFALQD--FNRRsvIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDS--LLAT-VITSLSELYEEALF--KMKAAL 201
Cdd:PRK01265  108 VPFPNAFAYGSpiAGKR--IAITLPLLKILNRDEIKAVAGHELGHLKHRDVelLMAIgLIPTLIYYLGYSLFwgGMFGGG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 202 RGSRGRGSALFFLLYIVLLGMNTLSKMLHFFLSRQREYRADaVGTRLT-----RN-PLSLAEALR----LISEHWRGSGA 271
Cdd:PRK01265  186 GGGRGNNGGLLFLIGIALMAVSFVFNLLVLSINRMREAYAD-VNSALTvpggaENlQTALAKITLsmdpGALERFKKKST 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490642194 272 EGARLESIFIVNPRHS------------WLDEREGLLSIMFSTHPPIKKRINLL 313
Cdd:PRK01265  265 TNQMASMLFFSNAIEEvptwdarelveyWKTTKVPWYADIFSDHPHPAKRIQLL 318
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 108-315 3.13e-13

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: 68.41  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 108 NIVDEVSVAIG-GRKIEAMVIPSAGTNAFALQdFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSL 186
Cdd:cd07325    17 ALLVEACRILGlKKVPELYVYQSPVLNAFALG-FEGRPFIVLNSGLVELLDDDELRFVIGHELGHIKSGHVLYRTLLLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 187 SELyeealfkmkAALRGSRGRGSALFFLLYivllgmntlskmlhfFLSRQREYRADAVGTRLTRNPLSLAEALRLISehw 266
Cdd:cd07325    96 LLL---------GELIGILLLSSALPLALL---------------AWSRAAEYSADRAGLLVCQDPEAAIRALMKLA--- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490642194 267 rGSGAEGARLESIFIVNPRHSWLDEREGL---LSIMFSTHPPIKKRINLLLN 315
Cdd:cd07325   149 -GGSKLLKDVNNIEYFLEEEAQADALDGFfkwLSELLSTHPFLVKRAAELLR 199
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 82-313 3.11e-12

M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48-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.


Pssm-ID: 320687 [Multi-domain]  Cd Length: 160  Bit Score: 64.50  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  82 RLIEKMAQAAGARPIDEndIYhqyfknIVDEVsvaiggrkieamvipsagtNAFALQD---FNRRSVIGVTEGLLARLNR 158
Cdd:cd07328    30 ALVDELAAALGAPPPDE--VV------LTADV-------------------NASVTELgllLGRRGLLTLGLPLLAALSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 159 PQIEAVVAHEAAHIVCGDSLLAtvitslselyeealfkmkaalrgsrgrgsalffllyivllgmntlskmlHFFLSRQRE 238
Cdd:cd07328    83 EELRAVLAHELGHFANGDTRLG-------------------------------------------------AWILSRRAE 113

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490642194 239 YRADAVGTRLTrNPLSLAEALRLISEHWRGSgaegarlesifivnprhswlderegllsiMFSTHPPIKKRINLL 313
Cdd:cd07328   114 YEADRVAARVA-GSAAAASALRKLAARRPSS-----------------------------PDDTHPPLAERLAAL 158
COG3809 COG3809
Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction ...
 490-540 1.53e-09

Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only];


Pssm-ID: 443022  Cd Length: 59  Bit Score: 53.90  E-value: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 490 MDCPRCKQKMhrqFFVYSYPVEIERCLFCSGVWFDKQELEILQYLFENQEQ 540
Cdd:COG3809     3 MLCPKCGAPM---RVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAA 50
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 129-313 2.30e-09

Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing.


Pssm-ID: 320702 [Multi-domain]  Cd Length: 405  Bit Score: 59.42  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 129 SAGTNAFalqdF-----NRRSVIGVTegLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITS---------LSELYEEAL 194
Cdd:cd07343   234 STHSNAY----FtgfgkNKRIVLFDT--LLEQLTEDEILAVLAHELGHWKHGHILKGLILSQlllflgfylFGLLLNNPS 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 195 FKMKAALRGSRGRGSALFFLLYIVLLgmNTLSKMLHFFLSRQREYRADAVGTRLTRNPlSLAEAL-RLISEHWrgsgaeg 273
Cdd:cd07343   308 LYRAFGFFGPSDQPALIGFLLLLSPL--SFLLSPLMNALSRKFEYEADAFAVELGYGE-ALISALvKLSKDNL------- 377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1490642194 274 arlesifiVNPRHSWlderegLLSIMFSTHPPIKKRINLL 313
Cdd:cd07343   378 --------SNLTPDP------LYSAFHYSHPPLLERIAAL 403
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 126-315 6.23e-08

Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins.


Pssm-ID: 320683 [Multi-domain]  Cd Length: 142  Bit Score: 51.80  E-value: 6.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 126 VIPSAGTNAFALQDfnrrSVIGVTEGLLARLNRP-QIEAVVAHEAAHIVCGDSLlatvitslselyeealfkmkaalrgs 204
Cdd:cd07324    24 VVDDPSINAFALPG----GYIFVTTGLLLLLESEdELAAVLAHEIGHVTLRHIA-------------------------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 205 rgRGSALFfllyivllgmntlskmlhfflSRQREYRADAVGTRLTR----NPLSLAEALRLISEhwrgsgaegarlesif 280
Cdd:cd07324    74 --RQLERY---------------------SRDQEREADRLGLQLLAragyDPRGMARFFERLAR---------------- 114

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1490642194 281 ivnprhsWLDEREGLLSIMFSTHPPIKKRINLLLN 315
Cdd:cd07324   115 -------QEGLSGSRLPEFLSTHPLTAERIAALRA 142
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 134-259 4.22e-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: 50.00  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 134 AFALqdFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVITSLSelyeealfkmkaalrgsrgrgSALFF 213
Cdd:cd07326    39 AFCL--GGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDPLLLLLASALA---------------------RALPF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1490642194 214 LLyivllgmntLSKMLHFFLSRQREYRADAVGTRLTrNPLSLAEAL 259
Cdd:cd07326    96 LP---------LLRRLAAAYRLLRELAADDAAARRV-GPRALASAL 131
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 148-315 8.08e-07

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.


Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 51.13  E-value: 8.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 148 VTEGLLARLNRPQIEAVVAHEAAHI-----------VCGDSLLATVITSLSELYEEALFKMKAALRGSRGRG--SALFFL 214
Cdd:cd07345   192 ITDALLDSLSPEELEAVLAHEIGHVkkrhlllyllfFLGFILLLALLSLLLSLLLLLLLPLLILLLGSSAEIllTLLLAL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 215 LYIVLLgmntlskMLHF-----FLSRQREYRADAVGTRLTRNPLSLAEALRLISEHWRGSGAegarlesifivnpRHSWl 289
Cdd:cd07345   272 PLLLLL-------VLYFrfvfgFFSRNFERQADLYALRALGSAEPLISALEKIAELSGNSRD-------------KPSW- 330

                         170       180
                  ....*....|....*....|....*.
gi 1490642194 290 deregllsimfsTHPPIKKRINLLLN 315
Cdd:cd07345   331 ------------HHFSIAQRIAFLEK 344
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 89-310 5.85e-06

Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320690 [Multi-domain]  Cd Length: 187  Bit Score: 47.19  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  89 QAAGARPIDENDIYHQYFKNIVDEVsvaiggrkieaMVIPSAGTNAFALqdFNRRsvIGVTEGLLARL-NRPQIEAVVAH 167
Cdd:cd07331     2 RRVAARLIAAAGDDPPQSAGWDWEV-----------HVIDSPEVNAFVL--PGGK--IFVFTGLLPVAkNDDELAAVLGH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 168 EAAHIVCGDSLlatvitslselyeEALFKMKAALRGSRGRGSALFFLlyIVLLGMNTLSKMLHFFL----SRQREYRADA 243
Cdd:cd07331    67 EIAHALARHSA-------------ERMSQQKLLQLLLLLLLAALGAS--LAGLALGLLGLGAQLGLllpySRKQELEADR 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 244 VGTRL-TR---NPlslAEALRLisehWRGSGAegarlesifivnprhswLDEREGLLSIMfSTHPPIKKRI 310
Cdd:cd07331   132 IGLQLmAKagyDP---RAAVTF----WEKMAA-----------------AEGGGKPPEFL-STHPSSETRI 177
zf-TFIIB pfam13453
Transcription factor zinc-finger;
491-531 7.76e-06

Transcription factor zinc-finger;


Pssm-ID: 433221  Cd Length: 41  Bit Score: 43.06  E-value: 7.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1490642194 491 DCPRCKQKMHRQFFvysYPVEIERCLFCSGVWFDKQELEIL 531
Cdd:pfam13453   1 KCPKCGAELEEVER---DGVEIDYCPQCRGIWLDRGELEKL 38
COG3809 COG3809
Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction ...
 415-468 1.02e-05

Predicted nucleic acid-binding protein, contains Zn-finger domain [General function prediction only];


Pssm-ID: 443022  Cd Length: 59  Bit Score: 43.12  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490642194 415 CPHCKTGLSEFSYEGVHIFKCSFCSGIFLDHDKISRILIRKDMEFCKEVKKLGE 468
Cdd:COG3809     5 CPKCGAPMRVVERSGVEIDYCPSCGGVWLDRGELEKLLEAEEAGAARRKSFLSD 58
zf-TFIIB pfam13453
Transcription factor zinc-finger;
415-452 3.85e-05

Transcription factor zinc-finger;


Pssm-ID: 433221  Cd Length: 41  Bit Score: 40.74  E-value: 3.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1490642194 415 CPHCKTGLSEFSYEGVHIFKCSFCSGIFLDHDKISRIL 452
Cdd:pfam13453   2 CPKCGAELEEVERDGVEIDYCPQCRGIWLDRGELEKLL 39
M56_BlaR1_MecR1_like cd07341
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 142-259 2.47e-03

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: 39.24  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 142 RRSVIGVTEGLLARlNRPQIEAVVAHEAAHIVCGDSLLATVITSLselyeEALFkmkaalrgsrgrgsalFFllyivllg 221
Cdd:cd07341    65 FRPVILLPEGLLEG-SPEELRAILLHELAHIRRRDLLVNLLQRLL-----EALF----------------WF-------- 114

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490642194 222 mNTLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEAL 259
Cdd:cd07341   115 -NPLVWLLSRRLRLERELACDEAVLAALGDKEDYAEAL 151
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 63-259 4.59e-03

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


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 39.26  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  63 IVLIAAFFIALLHWVISTNRLIEKmaqaagARPIDENDIYHqyfknIVDEVSVAIGGRKIEAMVIPSAGTNAFALQDFNR 142
Cdd:COG4219     2 LAGVLLLLLRLLISLLRLRRLLRR------ARPVTDEELLE-----LLERLARRLGIRRPVRLLESDRITSPFSFGLLRP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 143 RSVIGVTeglLARLNRPQIEAVVAHEAAHIVCGDS---LLATVITSLselyeealfkmkaalrgsrgrgsaLFFllyivl 219
Cdd:COG4219    71 VILLPAG---LEELSEEELEAILAHELAHIRRRDLldnLLAELLLAL------------------------FWF------ 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1490642194 220 lgmNTLSKMLHFFLSRQREYRADAVGTRLTRNPLSLAEAL 259
Cdd:COG4219   118 ---NPLVWLARRRLRLDRELACDAAVLKAGGDRKAYAETL 154
M48A_Ste24p cd07330
Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This ...
 29-314 6.15e-03

Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This family of M48 CaaX prenyl protease 1-like family includes a number of well characterized genes such as those found in Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24), yeast Ste24p and human (Hs Ste24p) as well as several uncharacterized genes such as YhfN, some of which also containing tetratricopeptide (TPR) repeats. All members of this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. The gene ZmpSte24, also known as FACE-1 in humans, a member of this family, is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes while mutations in the protein lead to diseases of lamin processing (laminopathies), such as premature aging disease progeria and metabolic disorders. Some of these mutations map to the peptide-binding site.


Pssm-ID: 320689 [Multi-domain]  Cd Length: 285  Bit Score: 38.96  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194  29 LTTYLILVILENSLVPSSVLSRRGFFFPpashaLIVLIAAFFIALLHWVISTNRLIEKmaqAAGARPIDENDIyhqyfKN 108
Cdd:cd07330    53 LLTVGLLVALPVSALLLPFEEPGGGAWW-----LGEWLAWLFYLFWRWKLSPFYAQFW---KRRSRPLANGEL-----RE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 109 IVDEVSVAIGGRKIEAMVIPSAG-----TNAFALQDFNRRSVIGVTEGLLARLNRPQIEAVVAHEAAHIVCGDSLLATVI 183
Cdd:cd07330   120 RIESMMNREGFGCAEILKVELSGgsmihANAYFPGSGKRRRVVVFADALVSLMTPDELLAVIAHELGHVKHHHHLFRLAA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490642194 184 TSLselyeealfkmkaalrgsrgrGSALFFLLYIVLLgmnTLSKMLHFFlSRQREYRADAVGTRLTRNPlSLAEALrlis 263
Cdd:cd07330   200 SQA---------------------VSFIVCALFILIY---PLRFLLNFF-ARRFEYQADAYAAKLAGAD-ALISAL---- 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490642194 264 ehwrgsgaegARLESIFIVNPRHSWlderegLLSIMFSTHPPIKKRINLLL 314
Cdd:cd07330   250 ----------VKLHRDNLTTLTPSR------LYSLWHYSHPHAAMRVAHLL 284
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH