DEGS_ECOLI
ID DEGS_ECOLI Reviewed; 355 AA.
AC P0AEE3; P31137; Q2M8X8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; Synonyms=hhoB, htrH; OrderedLocusNames=b3235, JW3204;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8576052; DOI=10.1128/jb.178.4.1154-1161.1996;
RA Bass S., Gu Q., Christen A.;
RT "Multicopy suppressors of prc mutant Escherichia coli include two HtrA
RT (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA.";
RL J. Bacteriol. 178:1154-1161(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8576051; DOI=10.1128/jb.178.4.1146-1153.1996;
RA Waller P.R., Sauer R.T.;
RT "Characterization of degQ and degS, Escherichia coli genes encoding
RT homologs of the DegP protease.";
RL J. Bacteriol. 178:1146-1153(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-355.
RX PubMed=3322223; DOI=10.1007/bf00423133;
RA Vogel R.F., Entian K.-D., Mecke D.;
RT "Cloning and sequence of the mdh structural gene of Escherichia coli coding
RT for malate dehydrogenase.";
RL Arch. Microbiol. 149:36-42(1987).
RN [6]
RP IDENTIFICATION.
RA Bazan J.F., Fletterick R.J.;
RT "Structural and catalytic models of trypsin-like viral proteases.";
RL Semin. Virol. 1:311-322(1990).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-201.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10500101; DOI=10.1101/gad.13.18.2449;
RA Ades S.E., Connolly L.E., Alba B.M., Gross C.A.;
RT "The Escherichia coli sigma(E)-dependent extracytoplasmic stress response
RT is controlled by the regulated proteolysis of an anti-sigma factor.";
RL Genes Dev. 13:2449-2461(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=11442831; DOI=10.1046/j.1365-2958.2001.02475.x;
RA Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.;
RT "degS (hhoB) is an essential Escherichia coli gene whose indispensable
RT function is to provide sigma (E) activity.";
RL Mol. Microbiol. 40:1323-1333(2001).
RN [9]
RP FUNCTION IN CLEAVAGE OF RSEA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=12183368; DOI=10.1101/gad.1002302;
RA Kanehara K., Ito K., Akiyama Y.;
RT "YaeL (EcfE) activates the sigma(E) pathway of stress response through a
RT site-2 cleavage of anti-sigma(E), RseA.";
RL Genes Dev. 16:2147-2155(2002).
RN [10]
RP FUNCTION IN CLEAVAGE OF RSEA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=12183369; DOI=10.1101/gad.1008902;
RA Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.;
RT "DegS and YaeL participate sequentially in the cleavage of RseA to activate
RT the sigma(E)-dependent extracytoplasmic stress response.";
RL Genes Dev. 16:2156-2168(2002).
RN [11]
RP FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ACTIVITY REGULATION,
RP BINDING OF PEPTIDES, SUBUNIT, AND DOMAIN.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=12679035; DOI=10.1016/s0092-8674(03)00203-4;
RA Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.;
RT "OMP peptide signals initiate the envelope-stress response by activating
RT DegS protease via relief of inhibition mediated by its PDZ domain.";
RL Cell 113:61-71(2003).
RN [12]
RP FUNCTION IN CLEAVAGE OF RSEA, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=17360428; DOI=10.1073/pnas.0611567104;
RA Cezairliyan B.O., Sauer R.T.;
RT "Inhibition of regulated proteolysis by RseB.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007).
RN [13]
RP FUNCTION IN CLEAVAGE OF RSEA, AND FUNCTION AS A SENSOR.
RC STRAIN=K12;
RX PubMed=18945679; DOI=10.1074/jbc.m806603200;
RA Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.;
RT "A pair of circularly permutated PDZ domains control RseP, the S2P family
RT intramembrane protease of Escherichia coli.";
RL J. Biol. Chem. 283:35042-35052(2008).
RN [14]
RP FUNCTION IN CLEAVAGE OF RSEA, AND FUNCTION AS A SENSOR.
RX PubMed=19706448; DOI=10.1073/pnas.0903289106;
RA Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.;
RT "Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino
RT acid following DegS cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009).
RN [15]
RP FUNCTION AS A REGULATORY PROTEASE.
RX PubMed=19695325; DOI=10.1016/j.resmic.2009.07.012;
RA Meltzer M., Hasenbein S., Mamant N., Merdanovic M., Poepsel S., Hauske P.,
RA Kaiser M., Huber R., Krojer T., Clausen T., Ehrmann M.;
RT "Structure, function and regulation of the conserved serine proteases DegP
RT and DegS of Escherichia coli.";
RL Res. Microbiol. 160:660-666(2009).
RN [16]
RP MUTAGENESIS OF HIS-198 AND LYS-243.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=21245315; DOI=10.1073/pnas.1019277108;
RA Chaba R., Alba B.M., Guo M.S., Sohn J., Ahuja N., Sauer R.T., Gross C.A.;
RT "Signal integration by DegS and RseB governs the sigma-E-mediated envelope
RT stress response in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2106-2111(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 43-355 IN COMPLEX WITH ANALOGS
RP SUBSTRATE, MUTAGENESIS OF TYR-162; PRO-183 AND GLU-227, REACTION MECHANISM,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=15137941; DOI=10.1016/s0092-8674(04)00454-4;
RA Wilken C., Kitzing K., Kurzbauer R., Ehrmann M., Clausen T.;
RT "Crystal structure of the DegS stress sensor: How a PDZ domain recognizes
RT misfolded protein and activates a protease.";
RL Cell 117:483-494(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 37-354, SUBUNIT, AND ACTIVE SITE.
RX PubMed=15225661; DOI=10.1016/j.febslet.2004.06.012;
RA Zeth K.;
RT "Structural analysis of DegS, a stress sensor of the bacterial periplasm.";
RL FEBS Lett. 569:351-358(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178,
RP MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243;
RP ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17981123; DOI=10.1016/j.cell.2007.08.044;
RA Sohn J., Grant R.A., Sauer R.T.;
RT "Allosteric activation of DegS, a stress sensor PDZ protease.";
RL Cell 131:572-583(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS
RP SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ACTIVITY
RP REGULATION, BINDING OF PEPTIDE, SUBUNIT, AND MUTAGENESIS OF ASP-122 AND
RP TYR-162.
RX PubMed=17938245; DOI=10.1101/gad.445307;
RA Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J.,
RA Kirk R., Hasenbein S., Ehrmann M., Clausen T.;
RT "Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps
RT the protease inactive in the resting state and allows integration of
RT different OMP-derived stress signals upon folding stress.";
RL Genes Dev. 21:2659-2670(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN
RP COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=19836340; DOI=10.1016/j.str.2009.07.017;
RA Sohn J., Grant R.A., Sauer R.T.;
RT "OMP peptides activate the DegS stress-sensor protease by a relief of
RT inhibition mechanism.";
RL Structure 17:1411-1421(2009).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-256 OF MUTANT ALA-162;
RP ALA-178; ALA-191: GLN-198, MUTAGENESIS OF TYR-162; ARG-178; GLN-191 AND
RP HIS-198, ACTIVITY REGULATION, SUBUNIT, AND ACTIVE SITE.
RX PubMed=20739286; DOI=10.1074/jbc.m110.135541;
RA Sohn J., Grant R.A., Sauer R.T.;
RT "Allostery is an intrinsic property of the protease domain of DegS:
RT implications for enzyme function and evolution.";
RL J. Biol. Chem. 285:34039-34047(2010).
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
CC RseA. {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:11442831,
CC ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369,
CC ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:17360428,
CC ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:18945679,
CC ECO:0000269|PubMed:19695325, ECO:0000269|PubMed:19706448}.
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 {ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:17360428,
CC ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:19836340,
CC ECO:0000269|PubMed:20739286}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for RseA-YQF {ECO:0000269|PubMed:17981123,
CC ECO:0000269|PubMed:19836340};
CC Vmax=0.6 umol/sec/mg enzyme {ECO:0000269|PubMed:17981123,
CC ECO:0000269|PubMed:19836340};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12679035,
CC ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661,
CC ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:17981123,
CC ECO:0000269|PubMed:19836340, ECO:0000269|PubMed:20739286}.
CC -!- INTERACTION:
CC P0AEE3; P0AEE3: degS; NbExp=3; IntAct=EBI-1132101, EBI-1132101;
CC P0AEE3; P0AFX7: rseA; NbExp=7; IntAct=EBI-1132101, EBI-1117560;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:11442831}; Single-pass membrane protein
CC {ECO:0000305|PubMed:11442831}. Note=It is unclear how this protein is
CC anchored to the inner membrane, programs predict a signal sequence, but
CC replacing the N-terminal 26 residues with a known signal sequence gives
CC a protein unable to fully complement a disruption mutant.
CC {ECO:0000269|PubMed:11442831}.
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.
CC {ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:17360428}.
CC -!- DISRUPTION PHENOTYPE: Small, slowly growing colonies. 5-fold decrease
CC in basal sigma-E (RpoE) activity, loss of regular growth regulation of
CC sigma-E. No proteolysis of full-length RseA.
CC {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:11442831,
CC ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369,
CC ECO:0000269|PubMed:8576051}.
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.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; U15661; AAC43993.1; -; Genomic_DNA.
DR EMBL; U32495; AAC44006.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58037.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76267.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77278.1; -; Genomic_DNA.
DR EMBL; M24777; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; JC6052; JC6052.
DR RefSeq; NP_417702.1; NC_000913.3.
DR RefSeq; WP_000497723.1; NZ_STEB01000012.1.
DR PDB; 1SOT; X-ray; 2.30 A; A/B/C=43-355.
DR PDB; 1SOZ; X-ray; 2.40 A; A/B/C=43-355.
DR PDB; 1TE0; X-ray; 2.20 A; A/B=37-354.
DR PDB; 1VCW; X-ray; 3.05 A; A/B/C=43-355.
DR PDB; 2QF0; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I=27-256.
DR PDB; 2QF3; X-ray; 2.04 A; A/B/C=27-256.
DR PDB; 2QGR; X-ray; 2.70 A; A=27-256.
DR PDB; 2R3U; X-ray; 2.60 A; A/B/C=43-252.
DR PDB; 2R3Y; X-ray; 2.50 A; A/B/C=43-355.
DR PDB; 2RCE; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I=27-256.
DR PDB; 3B8J; X-ray; 2.51 A; A=27-256.
DR PDB; 3GCN; X-ray; 3.00 A; A=27-355.
DR PDB; 3GCO; X-ray; 2.80 A; A=27-355.
DR PDB; 3GDS; X-ray; 2.85 A; A=27-355.
DR PDB; 3GDU; X-ray; 3.00 A; A/B/C=27-355.
DR PDB; 3GDV; X-ray; 2.49 A; A/B/C=27-355.
DR PDB; 3LGI; X-ray; 1.65 A; A/B/C=27-256.
DR PDB; 3LGT; X-ray; 2.68 A; A=27-256.
DR PDB; 3LGU; X-ray; 2.46 A; A=27-256.
DR PDB; 3LGV; X-ray; 2.73 A; A/B/C/D/E/F/G/H/I=27-256.
DR PDB; 3LGW; X-ray; 2.50 A; A=27-256.
DR PDB; 3LGY; X-ray; 2.70 A; A=27-256.
DR PDB; 3LH1; X-ray; 2.51 A; A=27-256.
DR PDB; 3LH3; X-ray; 2.35 A; A/B/C/D/E/F/G/H/I=27-256.
DR PDB; 4RQY; X-ray; 2.20 A; A/B=37-355.
DR PDB; 4RQZ; X-ray; 2.40 A; A/B/C=43-355.
DR PDB; 4RR0; X-ray; 3.05 A; A/B/C=43-355.
DR PDB; 4RR1; X-ray; 2.30 A; A/B/C=43-355.
DR PDB; 6EW9; X-ray; 2.20 A; A/B/C=43-355.
DR PDBsum; 1SOT; -.
DR PDBsum; 1SOZ; -.
DR PDBsum; 1TE0; -.
DR PDBsum; 1VCW; -.
DR PDBsum; 2QF0; -.
DR PDBsum; 2QF3; -.
DR PDBsum; 2QGR; -.
DR PDBsum; 2R3U; -.
DR PDBsum; 2R3Y; -.
DR PDBsum; 2RCE; -.
DR PDBsum; 3B8J; -.
DR PDBsum; 3GCN; -.
DR PDBsum; 3GCO; -.
DR PDBsum; 3GDS; -.
DR PDBsum; 3GDU; -.
DR PDBsum; 3GDV; -.
DR PDBsum; 3LGI; -.
DR PDBsum; 3LGT; -.
DR PDBsum; 3LGU; -.
DR PDBsum; 3LGV; -.
DR PDBsum; 3LGW; -.
DR PDBsum; 3LGY; -.
DR PDBsum; 3LH1; -.
DR PDBsum; 3LH3; -.
DR PDBsum; 4RQY; -.
DR PDBsum; 4RQZ; -.
DR PDBsum; 4RR0; -.
DR PDBsum; 4RR1; -.
DR PDBsum; 6EW9; -.
DR AlphaFoldDB; P0AEE3; -.
DR SMR; P0AEE3; -.
DR BioGRID; 4261915; 7.
DR DIP; DIP-39580N; -.
DR IntAct; P0AEE3; 3.
DR STRING; 511145.b3235; -.
DR MEROPS; S01.275; -.
DR jPOST; P0AEE3; -.
DR PaxDb; P0AEE3; -.
DR PRIDE; P0AEE3; -.
DR EnsemblBacteria; AAC76267; AAC76267; b3235.
DR EnsemblBacteria; BAE77278; BAE77278; BAE77278.
DR GeneID; 947865; -.
DR KEGG; ecj:JW3204; -.
DR KEGG; eco:b3235; -.
DR PATRIC; fig|1411691.4.peg.3493; -.
DR EchoBASE; EB1605; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_2_2_6; -.
DR InParanoid; P0AEE3; -.
DR OMA; THGWVLE; -.
DR PhylomeDB; P0AEE3; -.
DR BioCyc; EcoCyc:EG11652-MON; -.
DR BioCyc; MetaCyc:EG11652-MON; -.
DR BRENDA; 3.4.21.107; 2026.
DR EvolutionaryTrace; P0AEE3; -.
DR PRO; PR:P0AEE3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IMP:EcoliWiki.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008233; F:peptidase activity; IMP:EcoliWiki.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:EcoCyc.
DR GO; GO:0008236; F:serine-type peptidase activity; IMP:EcoliWiki.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="Serine endoprotease DegS"
FT /id="PRO_0000026938"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11442831"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..355
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:11442831"
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:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286"
FT BINDING 184
FT /ligand="substrate"
FT BINDING 259..264
FT /ligand="substrate"
FT BINDING 351
FT /ligand="substrate"
FT MUTAGEN 122
FT /note="D->A: Causes substantial reduction of peptidase
FT activity. Binds activator peptides."
FT /evidence="ECO:0000269|PubMed:17938245,
FT ECO:0000269|PubMed:17981123"
FT MUTAGEN 162
FT /note="Y->A: Loss of peptidase activity. Binds activator
FT peptides."
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:17981123,
FT ECO:0000269|PubMed:20739286"
FT MUTAGEN 162
FT /note="Y->F: Loss of 60% of peptidase activity."
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:17938245, ECO:0000269|PubMed:17981123,
FT ECO:0000269|PubMed:20739286"
FT MUTAGEN 178
FT /note="R->A: Causes substantial reduction of peptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:17981123,
FT ECO:0000269|PubMed:20739286"
FT MUTAGEN 183
FT /note="P->A: Loss of peptidase activity. Also affects an
FT interface contact between the PDZ and protease domains."
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:17981123"
FT MUTAGEN 191
FT /note="Q->A: Loss of peptidase activity."
FT /evidence="ECO:0000269|PubMed:20739286"
FT MUTAGEN 198
FT /note="H->A: Behaves like wild-type."
FT /evidence="ECO:0000269|PubMed:19836340,
FT ECO:0000269|PubMed:20739286, ECO:0000269|PubMed:21245315"
FT MUTAGEN 198
FT /note="H->P: Partially bypasses the requirement for peptide
FT activation, acts synergistically with mutations that
FT disrupt contacts between the protease and PDZ domains and
FT with an rseB disruption."
FT /evidence="ECO:0000269|PubMed:19836340,
FT ECO:0000269|PubMed:20739286, ECO:0000269|PubMed:21245315"
FT MUTAGEN 201
FT /note="S->A: Does not restore RseA degradation in a degS
FT disruption. Loss of RseA degradation."
FT /evidence="ECO:0000269|PubMed:10500101"
FT MUTAGEN 227
FT /note="E->A: Loss of peptidase activity."
FT /evidence="ECO:0000269|PubMed:15137941,
FT ECO:0000269|PubMed:17981123"
FT MUTAGEN 243
FT /note="K->D: Increases the basal rate of RseA cleavage 3-
FT fold, acts synergistically with an rseB disruption."
FT /evidence="ECO:0000269|PubMed:17981123,
FT ECO:0000269|PubMed:21245315"
FT MUTAGEN 256
FT /note="R->A: Dramatically increases the basal rate of RseA
FT cleavage."
FT /evidence="ECO:0000269|PubMed:17981123"
FT MUTAGEN 256
FT /note="R->D: Dramatically increases the basal rate of RseA
FT cleavage."
FT /evidence="ECO:0000269|PubMed:17981123"
FT MUTAGEN 320
FT /note="D->A: Dramatically increases the basal rate of RseA
FT cleavage."
FT /evidence="ECO:0000269|PubMed:17981123"
FT CONFLICT 253
FT /note="R -> A (in Ref. 5; M24777)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="V -> E (in Ref. 5; M24777)"
FT /evidence="ECO:0000305"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1TE0"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:3LGI"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3LGI"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:3LGI"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3LGI"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:3LGI"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3LGI"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1SOT"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4RQZ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1SOT"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3LGI"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3LGI"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:3LGI"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1SOT"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1TE0"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:1TE0"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:1TE0"
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
