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Conserved domains on  [gi|1553968308|ref|WP_128048755|]
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site-2 protease family protein [Helicobacter pylori]

Protein Classification

site-2 protease family protein( domain architecture ID 10150298)

Site-2 protease (S2P) homolog is a zinc metalloprotease which cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms, including processes as sporulation, cell division, stress response, and cell differentiation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 15-215 3.05e-49

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


:

Pssm-ID: 100079  Cd Length: 181  Bit Score: 159.25  E-value: 3.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  15 LMKILALLIAIIGHEIMHGLSAFLFGDRSAKDAKRLSLNPIRHLDMMGSVLLPALLlifqaPFLFGWAKPVPVDMRYIvs 94
Cdd:cd06158     2 LIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL-----PFLFGWAKPVPVNPRNF-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  95 QKGSLACVVVSLAGVAYNFTLAVLLASITHLSFQklginalsinELNLYQLALVTFLIQGILYNLVLGVFNSLPIPPLDG 174
Cdd:cd06158    75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPA----------FGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1553968308 175 SKALGflalHFKSAFLLEWFSKMERYGLLIVLIFLFIPPLS 215
Cdd:cd06158   145 SKILA----ALLPRRLAEAYARLEPYGFLILLALLFTGILG 181
 
Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 15-215 3.05e-49

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


Pssm-ID: 100079  Cd Length: 181  Bit Score: 159.25  E-value: 3.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  15 LMKILALLIAIIGHEIMHGLSAFLFGDRSAKDAKRLSLNPIRHLDMMGSVLLPALLlifqaPFLFGWAKPVPVDMRYIvs 94
Cdd:cd06158     2 LIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL-----PFLFGWAKPVPVNPRNF-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  95 QKGSLACVVVSLAGVAYNFTLAVLLASITHLSFQklginalsinELNLYQLALVTFLIQGILYNLVLGVFNSLPIPPLDG 174
Cdd:cd06158    75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPA----------FGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1553968308 175 SKALGflalHFKSAFLLEWFSKMERYGLLIVLIFLFIPPLS 215
Cdd:cd06158   145 SKILA----ALLPRRLAEAYARLEPYGFLILLALLFTGILG 181
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 12-219 4.73e-19

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 81.02  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  12 ITTLMKILALLIAIIGHEIMHGLSAFLFGDRSAkdakRLSLNPIRhldmmgsvllpalllifqapflFGWAKpvpVDMRY 91
Cdd:COG1994     9 PSILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNPLK----------------------GGWAK---INRNF 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  92 ivsqKGSLACVVVSLAGVAYNFTLAVLLASITHLSFqklginalsinelNLYQLALVTFLIQGILYNLVLGVFNSLPIPP 171
Cdd:COG1994    60 ----RNPRDEALVALAGPLANLLLALLFALLLRLLP-------------ALGLGPLALLLGYLALINLVLAVFNLLPIPP 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1553968308 172 LDGSKALGFLAlhfkSAFLLEWFSKMERYGLLIVLIFLFIPPLSEFFI 219
Cdd:COG1994   123 LDGGRILRALL----PRRTARRATRLEPYGFLILLLLIFLGLLLGNIW 166
 
Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 15-215 3.05e-49

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


Pssm-ID: 100079  Cd Length: 181  Bit Score: 159.25  E-value: 3.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  15 LMKILALLIAIIGHEIMHGLSAFLFGDRSAKDAKRLSLNPIRHLDMMGSVLLPALLlifqaPFLFGWAKPVPVDMRYIvs 94
Cdd:cd06158     2 LIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL-----PFLFGWAKPVPVNPRNF-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  95 QKGSLACVVVSLAGVAYNFTLAVLLASITHLSFQklginalsinELNLYQLALVTFLIQGILYNLVLGVFNSLPIPPLDG 174
Cdd:cd06158    75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPA----------FGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1553968308 175 SKALGflalHFKSAFLLEWFSKMERYGLLIVLIFLFIPPLS 215
Cdd:cd06158   145 SKILA----ALLPRRLAEAYARLEPYGFLILLALLFTGILG 181
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 15-214 1.03e-25

Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain.


Pssm-ID: 100078 [Multi-domain]  Cd Length: 180  Bit Score: 98.85  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  15 LMKILALLIAIIGHEIMHGLSAFLFGDRSAKDAKRLSLNPIRHLDMMGSVLLPalllifqapfLFGWAKPVPVDMRYivS 94
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIP----------LGGYAKPVGENPRA--F 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  95 QKGSLACVVVSLAGVAYNFTLAVLLASITHLSFqklgiNALSINELNLYQLALVTFLIQGILYNLVLGVFNSLPIPPLDG 174
Cdd:cd05709    69 KKPRWQRLLVALAGPLANLLLALLLLLLLLLLG-----GLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPPLDG 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1553968308 175 SKALGFLAlhfkSAFLLEWFSKMERYGLLIVLIFLFIPPL 214
Cdd:cd05709   144 GRILRALL----EAIRGRVEERLEAYGFAILLGLLLLLLL 179
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 12-219 4.73e-19

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 81.02  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  12 ITTLMKILALLIAIIGHEIMHGLSAFLFGDRSAkdakRLSLNPIRhldmmgsvllpalllifqapflFGWAKpvpVDMRY 91
Cdd:COG1994     9 PSILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNPLK----------------------GGWAK---INRNF 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553968308  92 ivsqKGSLACVVVSLAGVAYNFTLAVLLASITHLSFqklginalsinelNLYQLALVTFLIQGILYNLVLGVFNSLPIPP 171
Cdd:COG1994    60 ----RNPRDEALVALAGPLANLLLALLFALLLRLLP-------------ALGLGPLALLLGYLALINLVLAVFNLLPIPP 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1553968308 172 LDGSKALGFLAlhfkSAFLLEWFSKMERYGLLIVLIFLFIPPLSEFFI 219
Cdd:COG1994   123 LDGGRILRALL----PRRTARRATRLEPYGFLILLLLIFLGLLLGNIW 166
 
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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