DEGS_ECO57
ID DEGS_ECO57 Reviewed; 355 AA.
AC P0AEE4; P31137;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Serine endoprotease DegS;
DE EC=3.4.21.107;
DE AltName: Full=Site-1 protease DegS;
DE Short=S1P protease DegS;
DE AltName: Full=Site-1-type intramembrane protease;
GN Name=degS; OrderedLocusNames=Z4594, ECs4108;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: A site-1 protease (S1P) that cleaves the peptide bond between
CC 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane
CC proteolysis (RIP) cascade. When heat shock or other environmental
CC stresses disrupt protein folding in the periplasm, DegS senses the
CC accumulation of unassembled outer membrane porins (OMP) and then
CC initiates RseA (anti sigma-E factor) degradation by cleaving its
CC periplasmic domain, making it a substrate for subsequent cleavage by
CC RseP. This cascade ultimately leads to the sigma-E-driven expression of
CC a variety of factors dealing with folding stress in the periplasm and
CC OMP assembly. Required for basal and stress-induced degradation of RseA
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC -!- ACTIVITY REGULATION: Allosterically activated by the C-terminus of
CC exposed OMP peptides (consensus Tyr-X-Phe-COOH); cleavage only occurs
CC in the presence of peptides. Inhibited when RseB is bound to RseA.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The PDZ domain probably binds peptides ending with C-terminal
CC Tyr-X-Phe sequences, which activates proteolysis. In the absence of OMP
CC peptides the PDZ domain inhibits peptidase activity (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs when an
CC extracytoplasmic signal triggers a concerted proteolytic cascade to
CC transmit information and elicit cellular responses. A membrane-spanning
CC regulatory substrate protein is first cut extracytoplasmically (site-1
CC protease, S1P, this enzyme), then within the membrane itself (site-2
CC protease, S2P), while cytoplasmic proteases finish degrading the
CC regulatory protein, liberating the effector protein (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58363.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37531.1; -; Genomic_DNA.
DR PIR; D91142; D91142.
DR RefSeq; NP_312135.1; NC_002695.1.
DR RefSeq; WP_000497723.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEE4; -.
DR SMR; P0AEE4; -.
DR STRING; 155864.EDL933_4457; -.
DR MEROPS; S01.275; -.
DR EnsemblBacteria; AAG58363; AAG58363; Z4594.
DR EnsemblBacteria; BAB37531; BAB37531; ECs_4108.
DR GeneID; 916043; -.
DR KEGG; ece:Z4594; -.
DR KEGG; ecs:ECs_4108; -.
DR PATRIC; fig|386585.9.peg.4289; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_2_2_6; -.
DR OMA; THGWVLE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011783; Pept_S1C_DegS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR TIGRFAMs; TIGR02038; protease_degS; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="Serine endoprotease DegS"
FT /id="PRO_0000043342"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..355
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 281..326
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE3"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE3"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE3"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259..264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 37581 MW; D091B4D65E8FE1CC CRC64;
MFVKLLRSVA IGLIVGAILL VAMPSLRSLN PLSTPQFDST DETPASYNLA VRRAAPAVVN
VYNRGLNTNS HNQLEIRTLG SGVIMDQRGY IITNKHVIND ADQIIVALQD GRVFEALLVG
SDSLTDLAVL KINATGGLPT IPINARRVPH IGDVVLAIGN PYNLGQTITQ GIISATGRIG
LNPTGRQNFL QTDASINHGN SGGALVNSLG ELMGINTLSF DKSNDGETPE GIGFAIPFQL
ATKIMDKLIR DGRVIRGYIG IGGREIAPLH AQGGGIDQLQ GIVVNEVSPD GPAANAGIQV
NDLIISVDNK PAISALETMD QVAEIRPGSV IPVVVMRDDK QLTLQVTIQE YPATN
