DEGS_SALT1
ID DEGS_SALT1 Reviewed; 356 AA.
AC D0ZY51;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=STM14_4041;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19170886; DOI=10.1111/j.1365-2958.2009.06597.x;
RA Muller C., Bang I.S., Velayudhan J., Karlinsey J., Papenfort K., Vogel J.,
RA Fang F.C.;
RT "Acid stress activation of the sigma(E) stress response in Salmonella
RT enterica serovar Typhimurium.";
RL Mol. Microbiol. 71:1228-1238(2009).
CC -!- FUNCTION: A site-1 protease (S1P) that cleaves the peptide bond between
CC 'Val-148' and 'Ser-149' in RseA. 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 heat shock-induced degradation of
CC RseA but not for acid stress response in this strain.
CC {ECO:0000269|PubMed:19170886}.
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 -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Deletion of the PDZ domain eliminates the heat shock response
CC of the sigma-E regulon, but not the acid stress response.
CC {ECO:0000269|PubMed:19170886}.
CC -!- DISRUPTION PHENOTYPE: Loss of heat shock but not acid stress response
CC of sigma-E regulon. 10-fold decreased survival in acidified murine
CC macrophages. {ECO:0000269|PubMed:19170886}.
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; CP001363; ACY90437.1; -; Genomic_DNA.
DR RefSeq; WP_000497705.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZY51; -.
DR SMR; D0ZY51; -.
DR MEROPS; S01.275; -.
DR EnsemblBacteria; ACY90437; ACY90437; STM14_4041.
DR KEGG; seo:STM14_4041; -.
DR PATRIC; fig|588858.6.peg.3706; -.
DR HOGENOM; CLU_020120_2_2_6; -.
DR OMA; THGWVLE; -.
DR BioCyc; SENT588858:STM14_RS17805-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
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 Serine protease; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..356
FT /note="Serine endoprotease DegS"
FT /id="PRO_0000424886"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 256..341
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0AEE4"
SQ SEQUENCE 356 AA; 37795 MW; E2F7577BBE5CFEBA CRC64;
MFVKLLRSVA IGLIVGAILL AVMPSLRKIN PIAVPQFDST DETPASYNFA VRRAAPAVVN
VYNRSMNSTA HNQLEIRTLG SGVIMDQRGY IITNKHVIND ADQIIVALQD GRVFEALLVG
SDSLTDLAVL KINATGGLPT IPINTKRTPH IGDVVLAIGN PYNLGQTITQ GIISATGRIG
LNPTGRQNFL QTDASINHGN SGGALVNSLG ELMGINTLSF DKSNDGETPE GLGFAIPFQL
ATKIMDKLIR DGRVIRGYIG IGGREIAPLH AQQGSGMDPI QGIVVNEVTP NGPAALAGIQ
VNDLIISVNN KPAVSALETM DQVAEIRPGS VIPVVVMRDD KQLTFQVTVQ EYPASN
