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 Publications

Miscellaneous

Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P, this enzyme), then within the membrane itself (site-2 protease, S2P), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein.

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

Allosterically activated by the C-terminus of exposed OMP peptides (consensus Tyr-X-Phe-COOH); cleavage only occurs in the presence of peptides. Inhibited when RseB is bound to RseA.5 Publications

Manual assertion based on experiment inⁱ

Ref.11
"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ACTIVITY REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN.
Ref.12
"Inhibition of regulated proteolysis by RseB."
Cezairliyan B.O., Sauer R.T.
Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLEAVAGE OF RSEA, ACTIVITY REGULATION, DOMAIN.
Ref.20
"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."
Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J., Kirk R., Hasenbein S., Ehrmann M., Clausen T.
Genes Dev. 21:2659-2670(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ACTIVITY REGULATION, BINDING OF PEPTIDE, SUBUNIT, MUTAGENESIS OF ASP-122 AND TYR-162.
Ref.21
"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Ref.22
"Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution."
Sohn J., Grant R.A., Sauer R.T.
J. Biol. Chem. 285:34039-34047(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-256 OF MUTANT ALA-162; ALA-178; ALA-191: GLN-198, MUTAGENESIS OF TYR-162; ARG-178; GLN-191 AND HIS-198, ACTIVITY REGULATION, SUBUNIT, ACTIVE SITE.

Kineticsⁱ

K_M=
33 µM for RseA-YQF
2 Publications
Manual assertion based on experiment inⁱ
- Ref.19
  "Allosteric activation of DegS, a stress sensor PDZ protease."
  Sohn J., Grant R.A., Sauer R.T.
  Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Ref.21
  "OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
  Sohn J., Grant R.A., Sauer R.T.
  Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

V_max=
0.6 µmol/sec/mg enzyme
2 Publications
Manual assertion based on experiment inⁱ
- Ref.19
  "Allosteric activation of DegS, a stress sensor PDZ protease."
  Sohn J., Grant R.A., Sauer R.T.
  Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Ref.21
  "OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
  Sohn J., Grant R.A., Sauer R.T.
  Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Sites

Feature key	Position(s)	DescriptionActions	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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protease, Serine protease

Molecular function

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG11652-MONOMER MetaCyc:EG11652-MONOMER

BioCycⁱ

EcoCyc:EG11652-MONOMER
MetaCyc:EG11652-MONOMER

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	S01.275

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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Topology

Feature key	Position(s)	DescriptionActions	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, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Small, slowly growing colonies. 5-fold decrease in basal sigma-E (RpoE) activity, loss of regular growth regulation of sigma-E. No proteolysis of full-length RseA.5 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	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 Publications

Manual assertion based on experiment inⁱ

Ref.11
"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ACTIVITY REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN.
Ref.17
"Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease."
Wilken C., Kitzing K., Kurzbauer R., Ehrmann M., Clausen T.
Cell 117:483-494(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 43-355 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF TYR-162; PRO-183 AND GLU-227, REACTION MECHANISM, SUBUNIT, ACTIVE SITE.
Ref.18
"Structural analysis of DegS, a stress sensor of the bacterial periplasm."
Zeth K.
FEBS Lett. 569:351-358(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 37-354, SUBUNIT, ACTIVE SITE.
Ref.19
"Allosteric activation of DegS, a stress sensor PDZ protease."
Sohn J., Grant R.A., Sauer R.T.
Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Ref.20
"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."
Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J., Kirk R., Hasenbein S., Ehrmann M., Clausen T.
Genes Dev. 21:2659-2670(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ACTIVITY REGULATION, BINDING OF PEPTIDE, SUBUNIT, MUTAGENESIS OF ASP-122 AND TYR-162.
Ref.21
"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Ref.22
"Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution."
Sohn J., Grant R.A., Sauer R.T.
J. Biol. Chem. 285:34039-34047(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-256 OF MUTANT ALA-162; ALA-178; ALA-191: GLN-198, MUTAGENESIS OF TYR-162; ARG-178; GLN-191 AND HIS-198, ACTIVITY REGULATION, SUBUNIT, ACTIVE SITE.

Binary interactionsⁱ

Hide details

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
Inferred from physical interactionⁱ
- Ref.19
  "Allosteric activation of DegS, a stress sensor PDZ protease."
  Sohn J., Grant R.A., Sauer R.T.
  Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Ref.21
  "OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
  Sohn J., Grant R.A., Sauer R.T.
  Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	4261915, 7 interactors
Database of interacting proteins More...DIPⁱ	DIP-39580N
IntActⁱ	P0AEE3, 3 interactors
STRINGⁱ	511145.b3235

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	39 – 41	Combined sources	3
Helixⁱ	48 – 54	Combined sources	7
Helixⁱ	55 – 57	Combined sources	3
Beta strandⁱ	58 – 64	Combined sources	7
Turnⁱ	67 – 69	Combined sources	3
Beta strandⁱ	76 – 86	Combined sources	11
Turnⁱ	87 – 89	Combined sources	3
Beta strandⁱ	90 – 94	Combined sources	5
Helixⁱ	95 – 98	Combined sources	4
Beta strandⁱ	102 – 107	Combined sources	6
Beta strandⁱ	113 – 122	Combined sources	10
Turnⁱ	123 – 126	Combined sources	4
Beta strandⁱ	127 – 131	Combined sources	5
Beta strandⁱ	153 – 159	Combined sources	7
Helixⁱ	161 – 163	Combined sources	3
Beta strandⁱ	166 – 176	Combined sources	11
Beta strandⁱ	180 – 182	Combined sources	3
Beta strandⁱ	183 – 185	Combined sources	3
Helixⁱ	186 – 188	Combined sources	3
Beta strandⁱ	190 – 192	Combined sources	3
Turnⁱ	198 – 202	Combined sources	5
Beta strandⁱ	204 – 206	Combined sources	3
Beta strandⁱ	212 – 216	Combined sources	5
Beta strandⁱ	220 – 225	Combined sources	6
Beta strandⁱ	233 – 237	Combined sources	5
Helixⁱ	238 – 251	Combined sources	14
Beta strandⁱ	261 – 265	Combined sources	5
Beta strandⁱ	271 – 274	Combined sources	4
Beta strandⁱ	276 – 278	Combined sources	3
Beta strandⁱ	282 – 287	Combined sources	6
Beta strandⁱ	289 – 291	Combined sources	3
Turnⁱ	292 – 296	Combined sources	5
Beta strandⁱ	304 – 307	Combined sources	4
Helixⁱ	315 – 323	Combined sources	9
Beta strandⁱ	330 – 339	Combined sources	10
Beta strandⁱ	341 – 347	Combined sources	7

Show more details

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

The PDZ domain probably binds peptides ending with C-terminal Tyr-X-Phe sequences, which activates proteolysis. In the absence of OMP peptides the PDZ domain inhibits peptidase activity.2 Publications

Sequence similaritiesⁱ

Belongs to the peptidase S1C family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic 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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AEE3-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:355

Mass (Da):37,581

Last modified:December 6, 2005 - v1

Checksum:ⁱD091B4D65E8FE1CC

GO

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
NCBI Reference Sequences More...RefSeqⁱ	NP_417702.1, NC_000913.3 WP_000497723.1, NZ_STEB01000012.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278
GeneIDⁱ	57728494 947865
KEGGⁱ	ecj:JW3204 eco:b3235
PATRICⁱ	fig\|1411691.4.peg.3493

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0AEE3	Serine endoprotease DegS		ECO57		355	UniRef100_P0AEE4
Peptidase Do		Escherichia coli D6-113.11		355
Peptidase Do		Escherichia coli HVH 101 (4-6859844)		355
Peptidase Do		SHISO		355
Peptidase Do		Shigella dysenteriae 1617		355
+149

Protein	Similar proteins		Species	Score	Length	Source
P0AEE3	Serine endoprotease DegS		ECO57		355	UniRef90_P0AEE4
Peptidase Do		Escherichia coli D6-113.11		355
Peptidase Do		Escherichia coli HVH 101 (4-6859844)		355
Peptidase Do		SHISO		355
Peptidase Do		Shigella dysenteriae 1617		355
+585

Protein	Similar proteins		Species	Score	Length	Source
P0AEE3	Serine endoprotease DegS		SALT1		356	UniRef50_D0ZY51
Serine endoprotease DegS		ECO57		355
Peptidase Do		SALBL		356
Peptidase Do		SALMU		356
Peptidase Do		Salmonella enterica subsp. enterica serovar Typhi str. 404ty		356
+2174

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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

MEROPSⁱ

S01.275

Proteomic databases

jPOSTⁱ	P0AEE3
PaxDbⁱ	P0AEE3
PRIDEⁱ	P0AEE3

Genome annotation databases

EnsemblBacteriaⁱ	AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278
GeneIDⁱ	57728494 947865
KEGGⁱ	ecj:JW3204 eco:b3235
PATRICⁱ	fig\|1411691.4.peg.3493

Organism-specific databases

EchoBASEⁱ	EB1605

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 MetaCyc:EG11652-MONOMER

BioCycⁱ

EcoCyc:EG11652-MONOMER
MetaCyc:EG11652-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0AEE3
Protein Ontology More...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
ProtoNetⁱ	Search...
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:	April 7, 2021
	This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P0AEE3 (DEGS_ECOLI)

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Serine endoprotease DegS

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

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<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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Enzyme and pathway databases

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Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P0AEE3

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Protein-protein interaction databases

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Sequence databases

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Functionⁱ

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GO - Biological processⁱ

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Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

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Keywords - Domainⁱ

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Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ