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MULTISPECIES: stage IV sporulation intramembrane metalloprotease SpoIVFB [Bacillus]

Protein Classification

M50 family metallopeptidase( domain architecture ID 10150344)

M50 family metallopeptidase that cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms; belongs to the site-2 protease (S2P) class of zinc metalloproteases

EC:  3.4.24.-
Gene Ontology:  GO:0016020|GO:0008233|GO:0004222|GO:0046872
MEROPS:  M50
PubMed:  16322567|16731018|24099006|27889944

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 10-204 8.01e-54

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB.


:

Pssm-ID: 100082 [Multi-domain]  Cd Length: 208  Bit Score: 173.88  E-value: 8.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  10 KISVHPLFWVIIVIGIFTAR----------FKELLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPFGGVAELEEHGNkS 79
Cdd:cd06161    1 IILHHSWFLLLLLIAILLGPgvgpvawllgLLEALLLFLSVLLHELGHALVARRYGIRVRSITLLPFGGVAELEEEPE-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  80 LKEELVVVIAGPIQHIWMMLVGYILFEIGWLN---AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYLQAH 156
Cdd:cd06161   80 PKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGgplSSLLEFLAQVNLILGLFNLLPALPLDGGRVLRALLWRRTGYRRAT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446521630 157 EKMMQLSCVFFSVILGWQLLWN-SNNIMMWVLLIFLAISLYQEWKQRRY 204
Cdd:cd06161  160 RIAARIGQLFAILLVVLGLFLLfLGLGNLWLLLIALFIYLAAEAELRRA 208
 
Name Accession Description Interval E-value
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 10-204 8.01e-54

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB.


Pssm-ID: 100082 [Multi-domain]  Cd Length: 208  Bit Score: 173.88  E-value: 8.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  10 KISVHPLFWVIIVIGIFTAR----------FKELLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPFGGVAELEEHGNkS 79
Cdd:cd06161    1 IILHHSWFLLLLLIAILLGPgvgpvawllgLLEALLLFLSVLLHELGHALVARRYGIRVRSITLLPFGGVAELEEEPE-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  80 LKEELVVVIAGPIQHIWMMLVGYILFEIGWLN---AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYLQAH 156
Cdd:cd06161   80 PKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGgplSSLLEFLAQVNLILGLFNLLPALPLDGGRVLRALLWRRTGYRRAT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446521630 157 EKMMQLSCVFFSVILGWQLLWN-SNNIMMWVLLIFLAISLYQEWKQRRY 204
Cdd:cd06161  160 RIAARIGQLFAILLVVLGLFLLfLGLGNLWLLLIALFIYLAAEAELRRA 208
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 10-191 1.94e-30

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 112.22  E-value: 1.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  10 KISVHPLFWVIIvigiftarfkelLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPF-GGVAELEEHGnKSLKEELVVVI 88
Cdd:COG1994    4 PVRLHPSILIFA------------LALFLSVLLHELAHALVARRLGDPTAKITLNPLkGGWAKINRNF-RNPRDEALVAL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  89 AGPIQHIWMMLVGYILFEIGWLN-----AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYlqaheKMMQLS 163
Cdd:COG1994   71 AGPLANLLLALLFALLLRLLPALglgplALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLPRRTAR-----RATRLE 145

                        170       180       190
                 ....*....|....*....|....*....|
gi 446521630 164 CV--FFSVILGWQLLWNSNNIMMWVLLIFL 191
Cdd:COG1994  146 PYgfLILLLLIFLGLLLGNIWLSPLLNLLI 175
Peptidase_M50 pfam02163
Peptidase family M50;
33-105 2.56e-09

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 56.73  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630   33 LLLLFCIVLIHELGHAFAAAHYNWRIKK-------IQLLPFGGVAEL-EEHGNKSLKEELVVVIAGPIQHIWMMLVGYIL 104
Cdd:pfam02163   3 ILALGILVVVHELGHFLVARRFGVKVERfsigfyrIALIPLGGYVKMaDEFKSKSPWQRLAIALAGPLANFILAIILFAV 82


                  .
gi 446521630  105 F 105
Cdd:pfam02163  83 L 83
 
Name Accession Description Interval E-value
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 10-204 8.01e-54

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB.


Pssm-ID: 100082 [Multi-domain]  Cd Length: 208  Bit Score: 173.88  E-value: 8.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  10 KISVHPLFWVIIVIGIFTAR----------FKELLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPFGGVAELEEHGNkS 79
Cdd:cd06161    1 IILHHSWFLLLLLIAILLGPgvgpvawllgLLEALLLFLSVLLHELGHALVARRYGIRVRSITLLPFGGVAELEEEPE-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  80 LKEELVVVIAGPIQHIWMMLVGYILFEIGWLN---AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYLQAH 156
Cdd:cd06161   80 PKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGgplSSLLEFLAQVNLILGLFNLLPALPLDGGRVLRALLWRRTGYRRAT 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446521630 157 EKMMQLSCVFFSVILGWQLLWN-SNNIMMWVLLIFLAISLYQEWKQRRY 204
Cdd:cd06161  160 RIAARIGQLFAILLVVLGLFLLfLGLGNLWLLLIALFIYLAAEAELRRA 208
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 10-191 1.94e-30

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 112.22  E-value: 1.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  10 KISVHPLFWVIIvigiftarfkelLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPF-GGVAELEEHGnKSLKEELVVVI 88
Cdd:COG1994    4 PVRLHPSILIFA------------LALFLSVLLHELAHALVARRLGDPTAKITLNPLkGGWAKINRNF-RNPRDEALVAL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  89 AGPIQHIWMMLVGYILFEIGWLN-----AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYlqaheKMMQLS 163
Cdd:COG1994   71 AGPLANLLLALLFALLLRLLPALglgplALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLPRRTAR-----RATRLE 145

                        170       180       190
                 ....*....|....*....|....*....|
gi 446521630 164 CV--FFSVILGWQLLWNSNNIMMWVLLIFL 191
Cdd:COG1994  146 PYgfLILLLLIFLGLLLGNIWLSPLLNLLI 175
S2P-M50_SpoIVFB_CBS cd06164
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 18-155 1.16e-24

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. In this subgroup, SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain. SpoIVFB is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown.


Pssm-ID: 100085  Cd Length: 227  Bit Score: 98.76  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  18 WVIIVIGIFTArfkelLLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPFGGVAELEEHGnKSLKEELVVVIAGPIqhiwM 97
Cdd:cd06164   39 AVAWLLGLAAA-----LLLFASVLLHELGHSLVARRYGIPVRSITLFLFGGVARLEREP-ETPGQEFVIAIAGPL----V 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446521630  98 MLVGYILFEIGWLN---------AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYR-FPYLQA 155
Cdd:cd06164  109 SLVLALLFLLLSLAlpgsgagplGVLLGYLALINLLLAVFNLLPAFPLDGGRVLRALLWRRtGDYLKA 176
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 33-155 4.81e-21

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: 87.68  E-value: 4.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  33 LLLLFCIVLIHELGHAFAAAHYNWRIKK-----------------IQLLPFGGVAELEE----HGNKSLKEELVVVIAGP 91
Cdd:cd05709    4 ILALLISVTVHELGHALVARRLGVKVARfsggftlnplkhgdpygIILIPLGGYAKPVGenprAFKKPRWQRLLVALAGP 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446521630  92 IQHIWMMLVGYILFEIGWLN-------------AELYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFPYLQA 155
Cdd:cd05709   84 LANLLLALLLLLLLLLLGGLppapvgqaassglANLLAFLALINLNLAVFNLLPIPPLDGGRILRALLEAIRGRVEE 160
S2P-M50_like_2 cd06160
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 34-191 9.47e-13

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 additional putative N- and C-terminal transmembrane spanning regions, relative to the core protein, and no PDZ domains.


Pssm-ID: 100081  Cd Length: 183  Bit Score: 65.33  E-value: 9.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  34 LLLFCIVLIHELGHAFAAAHYNWRIKKIQLLPF------GGVAELEEHgNKSLKEELVVVIAGPIQHIwmmLVGYILFEI 107
Cdd:cd06160   38 LALLAILGIHEMGHYLAARRHGVKASLPYFIPFpfigtfGAFIRMRSP-IPNRKALFDIALAGPLAGL---LLALPVLII 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630 108 GWLnaelyyFFMWNNIIILAFNLLPIWPLDGGKVLFNVLSYRFpylqahekMMQLSCVFFSVILGWQLLWNSNNIMMWVL 187
Cdd:cd06160  114 GLA------VAGWVGLLVTALNLLPVGQLDGGHIVRALFGRRV--------AALIGIGLLVALGLLALYLSFSIWLLWAL 179


                 ....
gi 446521630 188 LIFL 191
Cdd:cd06160  180 LLLI 183
Peptidase_M50 pfam02163
Peptidase family M50;
33-105 2.56e-09

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 56.73  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630   33 LLLLFCIVLIHELGHAFAAAHYNWRIKK-------IQLLPFGGVAEL-EEHGNKSLKEELVVVIAGPIQHIWMMLVGYIL 104
Cdd:pfam02163   3 ILALGILVVVHELGHFLVARRFGVKVERfsigfyrIALIPLGGYVKMaDEFKSKSPWQRLAIALAGPLANFILAIILFAV 82


                  .
gi 446521630  105 F 105
Cdd:pfam02163  83 L 83
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 81-152 1.12e-07

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: 50.62  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  81 KEELVVVIAGPIQHIWMMLVGYILF---------EIGWLNAELYYFFMWNnIIILAFNLLPIWPLDGGKVLFNVLSYRFP 151
Cdd:cd06158   79 RGMLLVSLAGPLSNLLLALLFALLLrllpafggvVASFLFLMLAYGVLIN-LVLAVFNLLPIPPLDGSKILAALLPRRLA 157


                 .
gi 446521630 152 Y 152
Cdd:cd06158  158 E 158
S2P-M50_PDZ_Arch cd06159
Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS ...
 15-171 1.22e-06

Uncharacterized Archaeal 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 appears to be limited to Archaeal S2P/M50s homologs with additional putative N-terminal transmembrane spanning regions, relative to the core protein, and either one or two PDZ domains present.


Pssm-ID: 100080 [Multi-domain]  Cd Length: 263  Bit Score: 48.83  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  15 PLFWVIIVIGIFTArfkellllfciVLIHELGHAFAAAHYNWRIKKIQLL----PFGGVAEL--EEHGNKSLKEELVVVI 88
Cdd:cd06159  107 FIPLPYGIIALVVG-----------VVVHELSHGILARVEGIKVKSGGLLlliiPPGAFVEPdeEELNKADRRIRLRIFA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  89 AGPIQHIWMMLVGYILFEIGWLnaelyyffMWNNIIILAFNLLPIWPLDGGKVL---FNVLSYRFPYLQAHEKMMQLSCV 165
Cdd:cd06159  176 AGVTANFVVALIAFALFFLYWI--------FWINFLLGLFNCLPAIPLDGGHVFrdlLEALLRRFPSEKAERVVNAITYY 247


                 ....*.
gi 446521630 166 FFSVIL 171
Cdd:cd06159  248 LSSLVL 253
S2P-M50_PDZ_RseP-like cd06163
RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave ...
 16-146 1.36e-06

RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses. Also included in this group are such homologs as Bacillus subtilis YluC, Mycobacterium tuberculosis Rv2869c S2P, and Bordetella bronchiseptica HurP. Rv2869c S2P appears to have a role in the regulation of prokaryotic lipid biosynthesis and membrane composition and YluC of Bacillus has a role in transducing membrane stress. This group includes bacterial and eukaryotic S2P/M50s homologs with either one or two PDZ domains present. PDZ domains are believed to have a regulatory role. The RseP PDZ domain is required for the inhibitory reaction that prevents cleavage of its substrate, RseA.


Pssm-ID: 100084 [Multi-domain]  Cd Length: 182  Bit Score: 47.41  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  16 LFWVIIVIGIftarfkellllfcIVLIHELGHAFAAAHYN--------------WRIKK------IQLLPFGG------- 68
Cdd:cd06163    1 ILAFILVLGI-------------LIFVHELGHFLVAKLFGvkveefsigfgpklFSFKKgeteysISAIPLGGyvkmlge 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  69 ----VAELEEHG----NKSLKEELVVVIAGPIQHIwmmLVGYILFEIgwlnaeLYYFFMWNNIIILAFNLLPIWPLDGGK 140
Cdd:cd06163   68 dpeeEADPEDDPrsfnSKPVWQRILIVFAGPLANF---LLAIVLFAV------LLSFLALLSINLGILNLLPIPALDGGH 138


                 ....*.
gi 446521630 141 VLFNVL 146
Cdd:cd06163  139 LLFLLI 144
Peptidase_M50 pfam02163
Peptidase family M50;
104-171 3.10e-06

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 47.49  E-value: 3.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446521630  104 LFEIGWLNaeLYYFFMWNNIIILAFNLLPIWPLDGGKVLFNVL---SYRFPYLQAHEKMMQLScVFFSVIL 171
Cdd:pfam02163 224 AAEAGLIA--FLYFLALINLNLGIFNLLPVPPLDGGHILRALLeaiRGKPLSERAEEIALRVG-LALLLLL 291
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 16-105 5.46e-03

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 37.76  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446521630  16 LFWVIIVIGIftarfkellllfcIVLIHELGHaFAAAHYN---------------WRIKK------IQLLPFGG------ 68
Cdd:COG0750    7 ILAFILVLGV-------------LVFVHELGH-FLVARLFgvkveefsigfgpklFSKKRgeteygIRAIPLGGyvkmag 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446521630  69 ------VAELEEHG---NKSLKEELVVVIAGPIQHIwmmLVGYILF 105
Cdd:COG0750   73 mdpeseVAPEDDPRafnSKPVWQRLIIVLAGPLANF---LLAIVLF 115
 
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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