UniProtKB - P0AEE3 (DEGS_ECOLI)
Serine endoprotease DegS
degS
Functioni
A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA.
10 PublicationsMiscellaneous
Catalytic activityi
- Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. EC:3.4.21.107
Activity regulationi
Kineticsi
- KM=33 µM for RseA-YQF2 Publications
- Vmax=0.6 µmol/sec/mg enzyme2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 96 | Charge relay system3 Publications | 1 | |
Active sitei | 126 | Charge relay system3 Publications | 1 | |
Binding sitei | 184 | Substrate | 1 | |
Active sitei | 201 | Charge relay system3 Publications | 1 | |
Binding sitei | 351 | Substrate | 1 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- peptidase activity Source: EcoliWiki
- serine-type endopeptidase activity Source: EcoCyc
- serine-type peptidase activity Source: EcoliWiki
GO - Biological processi
- cellular response to misfolded protein Source: EcoCyc
- proteolysis Source: EcoliWiki
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11652-MONOMER |
BRENDAi | 3.4.21.107, 2026 |
Protein family/group databases
MEROPSi | S01.275 |
Names & Taxonomyi
Protein namesi | Recommended name: Serine endoprotease DegS (EC:3.4.21.107)Alternative name(s): Site-1 protease DegS Short name: S1P protease DegS Site-1-type intramembrane protease |
Gene namesi | Name:degS Synonyms:hhoB, htrH Ordered Locus Names:b3235, JW3204 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell inner membrane 1 Publication; Single-pass membrane protein 1 Publication
Note: It is unclear how this protein is anchored to the inner membrane, programs predict a signal sequence, but replacing the N-terminal 26 residues with a known signal sequence gives a protein unable to fully complement a disruption mutant.1 Publication
Plasma Membrane
- integral component of external side of plasma membrane Source: EcoliWiki
Other locations
- outer membrane-bounded periplasmic space Source: EcoCyc
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 4 | Cytoplasmic1 Publication | 4 | |
Transmembranei | 5 – 27 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 28 – 355 | Periplasmic1 PublicationAdd BLAST | 328 |
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 122 | D → A: Causes substantial reduction of peptidase activity. Binds activator peptides. 2 Publications | 1 | |
Mutagenesisi | 162 | Y → A: Loss of peptidase activity. Binds activator peptides. 4 Publications | 1 | |
Mutagenesisi | 162 | Y → F: Loss of 60% of peptidase activity. 4 Publications | 1 | |
Mutagenesisi | 178 | R → A: Causes substantial reduction of peptidase activity. 2 Publications | 1 | |
Mutagenesisi | 183 | P → A: Loss of peptidase activity. Also affects an interface contact between the PDZ and protease domains. 2 Publications | 1 | |
Mutagenesisi | 191 | Q → A: Loss of peptidase activity. 1 Publication | 1 | |
Mutagenesisi | 198 | H → A: Behaves like wild-type. 3 Publications | 1 | |
Mutagenesisi | 198 | H → P: Partially bypasses the requirement for peptide activation, acts synergistically with mutations that disrupt contacts between the protease and PDZ domains and with an rseB disruption. 3 Publications | 1 | |
Mutagenesisi | 201 | S → A: Does not restore RseA degradation in a degS disruption. Loss of RseA degradation. 1 Publication | 1 | |
Mutagenesisi | 227 | E → A: Loss of peptidase activity. 2 Publications | 1 | |
Mutagenesisi | 243 | K → D: Increases the basal rate of RseA cleavage 3-fold, acts synergistically with an rseB disruption. 2 Publications | 1 | |
Mutagenesisi | 256 | R → A: Dramatically increases the basal rate of RseA cleavage. 1 Publication | 1 | |
Mutagenesisi | 256 | R → D: Dramatically increases the basal rate of RseA cleavage. 1 Publication | 1 | |
Mutagenesisi | 320 | D → A: Dramatically increases the basal rate of RseA cleavage. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000026938 | 1 – 355 | Serine endoprotease DegSAdd BLAST | 355 |
Proteomic databases
jPOSTi | P0AEE3 |
PaxDbi | P0AEE3 |
PRIDEi | P0AEE3 |
Interactioni
Subunit structurei
Homotrimer.
7 PublicationsBinary interactionsi
P0AEE3
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-1132101,EBI-1132101 |
rseA [P0AFX7] | 7 | EBI-1132101,EBI-1117560 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4261915, 7 interactors |
DIPi | DIP-39580N |
IntActi | P0AEE3, 3 interactors |
STRINGi | 511145.b3235 |
Structurei
Secondary structure
3D structure databases
SMRi | P0AEE3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AEE3 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 281 – 326 | PDZPROSITE-ProRule annotationAdd BLAST | 46 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 259 – 264 | Substrate binding | 6 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG0265, Bacteria |
HOGENOMi | CLU_020120_2_2_6 |
InParanoidi | P0AEE3 |
PhylomeDBi | P0AEE3 |
Family and domain databases
Gene3Di | 2.30.42.10, 1 hit 2.40.10.10, 2 hits |
InterProi | View protein in InterPro IPR001478, PDZ IPR036034, PDZ_sf IPR011783, Pept_S1C_DegS IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001940, Peptidase_S1C |
Pfami | View protein in Pfam PF13180, PDZ_2, 1 hit |
PRINTSi | PR00834, PROTEASES2C |
SMARTi | View protein in SMART SM00228, PDZ, 1 hit |
SUPFAMi | SSF50156, SSF50156, 1 hit SSF50494, SSF50494, 1 hit |
TIGRFAMsi | TIGR02038, protease_degS, 1 hit |
PROSITEi | View protein in PROSITE PS50106, PDZ, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MFVKLLRSVA IGLIVGAILL VAMPSLRSLN PLSTPQFDST DETPASYNLA
60 70 80 90 100
VRRAAPAVVN VYNRGLNTNS HNQLEIRTLG SGVIMDQRGY IITNKHVIND
110 120 130 140 150
ADQIIVALQD GRVFEALLVG SDSLTDLAVL KINATGGLPT IPINARRVPH
160 170 180 190 200
IGDVVLAIGN PYNLGQTITQ GIISATGRIG LNPTGRQNFL QTDASINHGN
210 220 230 240 250
SGGALVNSLG ELMGINTLSF DKSNDGETPE GIGFAIPFQL ATKIMDKLIR
260 270 280 290 300
DGRVIRGYIG IGGREIAPLH AQGGGIDQLQ GIVVNEVSPD GPAANAGIQV
310 320 330 340 350
NDLIISVDNK PAISALETMD QVAEIRPGSV IPVVVMRDDK QLTLQVTIQE
YPATN
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 253 | R → A in M24777 (PubMed:3322223).Curated | 1 | |
Sequence conflicti | 307 | V → E in M24777 (PubMed:3322223).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U15661 Genomic DNA Translation: AAC43993.1 U32495 Genomic DNA Translation: AAC44006.1 U18997 Genomic DNA Translation: AAA58037.1 U00096 Genomic DNA Translation: AAC76267.1 AP009048 Genomic DNA Translation: BAE77278.1 M24777 Unassigned DNA No translation available. |
PIRi | JC6052 |
RefSeqi | NP_417702.1, NC_000913.3 WP_000497723.1, NZ_STEB01000012.1 |
Genome annotation databases
EnsemblBacteriai | AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278 |
GeneIDi | 947865 |
KEGGi | ecj:JW3204 eco:b3235 |
PATRICi | fig|1411691.4.peg.3493 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U15661 Genomic DNA Translation: AAC43993.1 U32495 Genomic DNA Translation: AAC44006.1 U18997 Genomic DNA Translation: AAA58037.1 U00096 Genomic DNA Translation: AAC76267.1 AP009048 Genomic DNA Translation: BAE77278.1 M24777 Unassigned DNA No translation available. |
PIRi | JC6052 |
RefSeqi | NP_417702.1, NC_000913.3 WP_000497723.1, NZ_STEB01000012.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1SOT | X-ray | 2.30 | A/B/C | 43-355 | [»] | |
1SOZ | X-ray | 2.40 | A/B/C | 43-355 | [»] | |
1TE0 | X-ray | 2.20 | A/B | 37-354 | [»] | |
1VCW | X-ray | 3.05 | A/B/C | 43-355 | [»] | |
2QF0 | X-ray | 2.50 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
2QF3 | X-ray | 2.04 | A/B/C | 27-256 | [»] | |
2QGR | X-ray | 2.70 | A | 27-256 | [»] | |
2R3U | X-ray | 2.60 | A/B/C | 43-252 | [»] | |
2R3Y | X-ray | 2.50 | A/B/C | 43-355 | [»] | |
2RCE | X-ray | 2.35 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
3B8J | X-ray | 2.51 | A | 27-256 | [»] | |
3GCN | X-ray | 3.00 | A | 27-355 | [»] | |
3GCO | X-ray | 2.80 | A | 27-355 | [»] | |
3GDS | X-ray | 2.85 | A | 27-355 | [»] | |
3GDU | X-ray | 3.00 | A/B/C | 27-355 | [»] | |
3GDV | X-ray | 2.49 | A/B/C | 27-355 | [»] | |
3LGI | X-ray | 1.65 | A/B/C | 27-256 | [»] | |
3LGT | X-ray | 2.68 | A | 27-256 | [»] | |
3LGU | X-ray | 2.46 | A | 27-256 | [»] | |
3LGV | X-ray | 2.73 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
3LGW | X-ray | 2.50 | A | 27-256 | [»] | |
3LGY | X-ray | 2.70 | A | 27-256 | [»] | |
3LH1 | X-ray | 2.51 | A | 27-256 | [»] | |
3LH3 | X-ray | 2.35 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
4RQY | X-ray | 2.20 | A/B | 37-355 | [»] | |
4RQZ | X-ray | 2.40 | A/B/C | 43-355 | [»] | |
4RR0 | X-ray | 3.05 | A/B/C | 43-355 | [»] | |
4RR1 | X-ray | 2.30 | A/B/C | 43-355 | [»] | |
6EW9 | X-ray | 2.20 | A/B/C | 43-355 | [»] | |
SMRi | P0AEE3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261915, 7 interactors |
DIPi | DIP-39580N |
IntActi | P0AEE3, 3 interactors |
STRINGi | 511145.b3235 |
Protein family/group databases
MEROPSi | S01.275 |
Proteomic databases
jPOSTi | P0AEE3 |
PaxDbi | P0AEE3 |
PRIDEi | P0AEE3 |
Genome annotation databases
EnsemblBacteriai | AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278 |
GeneIDi | 947865 |
KEGGi | ecj:JW3204 eco:b3235 |
PATRICi | fig|1411691.4.peg.3493 |
Organism-specific databases
EchoBASEi | EB1605 |
Phylogenomic databases
eggNOGi | COG0265, Bacteria |
HOGENOMi | CLU_020120_2_2_6 |
InParanoidi | P0AEE3 |
PhylomeDBi | P0AEE3 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11652-MONOMER |
BRENDAi | 3.4.21.107, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0AEE3 |
PROi | PR:P0AEE3 |
Family and domain databases
Gene3Di | 2.30.42.10, 1 hit 2.40.10.10, 2 hits |
InterProi | View protein in InterPro IPR001478, PDZ IPR036034, PDZ_sf IPR011783, Pept_S1C_DegS IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001940, Peptidase_S1C |
Pfami | View protein in Pfam PF13180, PDZ_2, 1 hit |
PRINTSi | PR00834, PROTEASES2C |
SMARTi | View protein in SMART SM00228, PDZ, 1 hit |
SUPFAMi | SSF50156, SSF50156, 1 hit SSF50494, SSF50494, 1 hit |
TIGRFAMsi | TIGR02038, protease_degS, 1 hit |
PROSITEi | View protein in PROSITE PS50106, PDZ, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DEGS_ECOLI | |
Accessioni | P0AEE3Primary (citable) accession number: P0AEE3 Secondary accession number(s): P31137, Q2M8X8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 6, 2005 |
Last sequence update: | December 6, 2005 | |
Last modified: | February 23, 2022 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families