RSEA_ECOLI
ID RSEA_ECOLI Reviewed; 216 AA.
AC P0AFX7; P38106; Q2MAF8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Anti-sigma-E factor RseA;
DE AltName: Full=Regulator of SigE;
DE AltName: Full=Sigma-E anti-sigma factor RseA;
DE AltName: Full=Sigma-E factor negative regulatory protein;
GN Name=rseA; Synonyms=mclA, yfiJ; OrderedLocusNames=b2572, JW2556;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=K12;
RX PubMed=7768826; DOI=10.1128/jb.177.11.3259-3268.1995;
RA Yu H., Schurr M.J., Deretic V.;
RT "Functional equivalence of Escherichia coli sigma E and Pseudomonas
RT aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to
RT reactive oxygen intermediates in algU mutants of P. aeruginosa.";
RL J. Bacteriol. 177:3259-3268(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7889935; DOI=10.1002/j.1460-2075.1995.tb07085.x;
RA Raina S., Missiakas D., Georgopoulos C.;
RT "The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of
RT Escherichia coli.";
RL EMBO J. 14:1043-1055(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
RC STRAIN=K12;
RA Nashimoto H.;
RT "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT coli.";
RL (In) Nierhaus K.H. (eds.);
RL The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN [7]
RP PROTEIN SEQUENCE OF 4-108, INTERACTION WITH RPOE AND SSPB, DOMAIN, CLEAVAGE
RP BY CLPX-CLPP, AND MUTAGENESIS OF 107-ALA-ALA-108.
RX PubMed=15371343; DOI=10.1101/gad.1240104;
RA Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT "Modulating substrate choice: the SspB adaptor delivers a regulator of the
RT extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT degradation.";
RL Genes Dev. 18:2292-2301(2004).
RN [8]
RP PROTEIN SEQUENCE OF 149-153, AND CLEAVAGE BY DEGS.
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 [9]
RP PROTEIN SEQUENCE OF 149-153, CLEAVAGE BY DEGS AND RSEP, AND MUTAGENESIS OF
RP SER-146; PRO-147 AND VAL-148.
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-216, FUNCTION AS AN ANTI-SIGMA
RP FACTOR, INTERACTION WITH RPOE AND RSEB, SUBUNIT, SUBCELLULAR LOCATION,
RP OPERON, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=9159523; DOI=10.1046/j.1365-2958.1997.3611718.x;
RA De Las Penas A., Connolly L., Gross C.A.;
RT "The sigmaE-mediated response to extracytoplasmic stress in Escherichia
RT coli is transduced by RseA and RseB, two negative regulators of sigmaE.";
RL Mol. Microbiol. 24:373-385(1997).
RN [11]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH RPOE AND RSEB, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, DISRUPTION PHENOTYPE, OPERON, AND
RP MUTAGENESIS OF 1-MET--GLU-28; ASP-11; LEU-19 AND TRP-33.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9159522; DOI=10.1046/j.1365-2958.1997.3601713.x;
RA Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.;
RT "Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-
RT factor activity by the RseA, RseB and RseC proteins.";
RL Mol. Microbiol. 24:355-371(1997).
RN [12]
RP INDUCTION, AND PROBABLE CLEAVAGE BY DEGS.
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 [13]
RP INTERACTION WITH RPOE AND RSEB, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11777003; DOI=10.1074/jbc.m006214200;
RA Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.;
RT "RseB binding to the periplasmic domain of RseA modulates the RseA:sigmaE
RT interaction in the cytoplasm and the availability of sigmaE.RNA
RT polymerase.";
RL J. Biol. Chem. 275:33898-33904(2000).
RN [14]
RP CLEAVAGE BY DEGS AND RSEP.
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 [15]
RP CLEAVAGE BY DEGS AND RSEP, AND SUBCELLULAR LOCATION.
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 [16]
RP INTERACTION WITH RPOE, AND SUBUNIT.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12016219; DOI=10.1074/jbc.m202881200;
RA Tam C., Collinet B., Lau G., Raina S., Missiakas D.;
RT "Interaction of the conserved region 4.2 of sigma(E) with the RseA anti-
RT sigma factor.";
RL J. Biol. Chem. 277:27282-27287(2002).
RN [17]
RP INTERACTION WITH RSEP, DOMAIN, CLEAVAGE BY RSEP, AND MUTAGENESIS OF
RP 162-GLN--GLN-169 AND 190-GLN--GLN-200.
RC STRAIN=K12 / AD16;
RX PubMed=14633997; DOI=10.1093/emboj/cdg602;
RA Kanehara K., Ito K., Akiyama Y.;
RT "YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a
RT Gln-rich region of RseA.";
RL EMBO J. 22:6389-6398(2003).
RN [18]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [19]
RP CLEAVAGE BY RSEP.
RX PubMed=15496982; DOI=10.1038/sj.emboj.7600449;
RA Akiyama Y., Kanehara K., Ito K.;
RT "RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane
RT sequences.";
RL EMBO J. 23:4434-4442(2004).
RN [20]
RP REGULATION OF DEGRADATION.
RX PubMed=17210793; DOI=10.1101/gad.1496707;
RA Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
RT "Design principles of the proteolytic cascade governing the sigmaE-mediated
RT envelope stress response in Escherichia coli: keys to graded, buffered, and
RT rapid signal transduction.";
RL Genes Dev. 21:124-136(2007).
RN [21]
RP INTERACTION WITH RSEB, AND SUBUNIT.
RX PubMed=17692869; DOI=10.1016/j.jmb.2007.06.039;
RA Wollmann P., Zeth K.;
RT "The structure of RseB: a sensor in periplasmic stress response of E.
RT coli.";
RL J. Mol. Biol. 372:927-941(2007).
RN [22]
RP INTERACTION WITH RSEB, SUBUNIT, 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 [23]
RP BINDING TO RSEB, AND MUTAGENESIS OF ARG-172 AND ARG-185.
RX PubMed=17496148; DOI=10.1073/pnas.0703117104;
RA Kim D.Y., Jin K.S., Kwon E., Ree M., Kim K.K.;
RT "Crystal structure of RseB and a model of its binding mode to RseA.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8779-8784(2007).
RN [24]
RP INTERACTION WITH RSEP, AND CLEAVAGE BY RSEP.
RC STRAIN=K12 / AD16;
RX PubMed=18268014; DOI=10.1074/jbc.m709984200;
RA Koide K., Ito K., Akiyama Y.;
RT "Substrate recognition and binding by RseP, an Escherichia coli
RT intramembrane protease.";
RL J. Biol. Chem. 283:9562-9570(2008).
RN [25]
RP INTERACTION WITH RSEB, AND SUBUNIT.
RX PubMed=18421143; DOI=10.1107/s0909049507066319;
RA Jin K.S., Kim D.Y., Rho Y., Le V.B., Kwon E., Kim K.K., Ree M.;
RT "Solution structures of RseA and its complex with RseB.";
RL J. Synchrotron Radiat. 15:219-222(2008).
RN [26]
RP CLEAVAGE BY DEGS AND RSEP.
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 [27]
RP MUTAGENESIS OF PRO-147 AND VAL-148.
RC STRAIN=K12;
RX PubMed=23016873; DOI=10.1111/mmi.12053;
RA Hizukuri Y., Akiyama Y.;
RT "PDZ domains of RseP are not essential for sequential cleavage of RseA or
RT stress-induced sigma(E) activation in vivo.";
RL Mol. Microbiol. 86:1232-1245(2012).
RN [28]
RP FUNCTION, BINDING TO RSEB, SUBUNIT, AND CLEAVAGE BY DEGS.
RC STRAIN=K12;
RX PubMed=23687042; DOI=10.1126/science.1235358;
RA Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.;
RT "Dual molecular signals mediate the bacterial response to outer-membrane
RT stress.";
RL Science 340:837-841(2013).
RN [29]
RP OPERON.
RC STRAIN=K12 / CF7789;
RX PubMed=28924029; DOI=10.1128/jb.00484-17;
RA Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
RT "Circuitry linking the global Csr and sigma(E)-dependent cell envelope
RT stress response systems.";
RL J. Bacteriol. 0:0-0(2017).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-90 IN COMPLEX WITH RPOE, MODE OF
RP ACTION, AND SUBUNIT.
RX PubMed=12718891; DOI=10.1016/s1097-2765(03)00148-5;
RA Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M., Gross C.A.,
RA Darst S.A.;
RT "Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain
RT of its anti-sigma RseA.";
RL Mol. Cell 11:1067-1078(2003).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-108 IN COMPLEX WITH SSPB,
RP SUBUNIT, AND MUTAGENESIS OF GLN-79; TRP-85 AND MET-88.
RX PubMed=15880122; DOI=10.1038/nsmb934;
RA Levchenko I., Grant R.A., Flynn J.M., Sauer R.T., Baker T.A.;
RT "Versatile modes of peptide recognition by the AAA+ adaptor protein SspB.";
RL Nat. Struct. Mol. Biol. 12:520-525(2005).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 121-216 IN COMPLEX WITH RSEB.
RX PubMed=20512978; DOI=10.1002/pro.393;
RA Kim D.Y., Kwon E., Choi J., Hwang H.Y., Kim K.K.;
RT "Structural basis for the negative regulation of bacterial stress response
RT by RseB.";
RL Protein Sci. 19:1258-1263(2010).
CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive
CC form by an anti-sigma factor until released by regulated intramembrane
CC proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers
CC a concerted proteolytic cascade to transmit information and elicit
CC cellular responses. The membrane-spanning regulatory substrate protein
CC is first cut periplasmically (site-1 protease, S1P, DegS), then within
CC the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic
CC proteases finish degrading the anti-sigma factor, liberating sigma-E.
CC Overexpression of RseA blocks sigma-E from acting, results in cell
CC lysis in stationary phase and temperature-sensitivity above 37 degrees
CC Celsius. {ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- SUBUNIT: Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this
CC inhibits the interaction of sigma-E with the RNA polymerase catalytic
CC core and leads to a decreased expression of sigma-E-regulated genes.
CC Interacts with RseB with 1:1 stoichiometry. The liberated N-terminus
CC (residues 1-108) forms a complex with SspB and RpoE; binding to SspB is
CC competitively inhibited by ssrA-tags, although the 2 proteins bind in
CC opposite directions in SspB's peptide-binding groove.
CC {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12016219,
CC ECO:0000269|PubMed:12718891, ECO:0000269|PubMed:14633997,
CC ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:15880122,
CC ECO:0000269|PubMed:17360428, ECO:0000269|PubMed:17692869,
CC ECO:0000269|PubMed:18268014, ECO:0000269|PubMed:18421143,
CC ECO:0000269|PubMed:20512978, ECO:0000269|PubMed:23687042,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
CC -!- INTERACTION:
CC P0AFX7; P0AEE3: degS; NbExp=7; IntAct=EBI-1117560, EBI-1132101;
CC P0AFX7; P0AFX9: rseB; NbExp=9; IntAct=EBI-1117560, EBI-1135231;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11777003,
CC ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Following
CC cleavage by DegS the large fragment of the protein is still in the
CC inner membrane and retains its anti-sigma-E activity.
CC -!- INDUCTION: Transiently induced by cold shock in a PNPase-dependent
CC fashion. Upon stress induction (OMPs or heat shock) decreases in under
CC 3 minutes (at protein level). Part of the rseD-rpoE-rseA-rseB-rseC
CC operon (PubMed:9159522, PubMed:9159523, PubMed:28924029).
CC {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:14527658,
CC ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- DOMAIN: The N-terminal cytosolic domain interacts with sigma-E, and
CC upon overexpression leads to temperature sensitivity above 37 degrees
CC Celsius and cell lysis in stationary phase. After degradation by RseP
CC residues 77-108 bind to SspB, targeting RseA for degradation by the
CC ClpX-ClpP protease.
CC -!- DOMAIN: The C-terminal periplasmic domain (residues 169-186) interacts
CC with RseB and is also the target for DegS; RseB and DegS binding sites
CC do not appreciably overlap. Gln-rich regions (residues 162-169, Q1, and
CC 190-200, Q2) contribute to preventing RseP from acting before DegS.
CC Insertion of 8 consecutive Gln residues into a protein lacking Q1 and
CC Q2 restores DegS-dependence of RseP cleavage.
CC -!- PTM: Sequentially cleaved by DegS (a site-1 protease) in its
CC periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2
CC protease) between positions Ala-108 and Cys-109. The N-terminal
CC fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent
CC fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE
CC from RseA. {ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369,
CC ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:14633997,
CC ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:15496982,
CC ECO:0000269|PubMed:18268014, ECO:0000269|PubMed:18945679,
CC ECO:0000269|PubMed:19706448, ECO:0000269|PubMed:23687042}.
CC -!- DISRUPTION PHENOTYPE: About 10-fold increased sigma-E activity. Neither
CC sigma-E nor RseB associate with the inner membrane.
CC {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
CC -!- CAUTION: PubMed:9159522 mis-identifies Trp-33 as residue 32.
CC {ECO:0000305}.
CC -!- CAUTION: In vitro (PubMed:19706448) and in vivo (PubMed:23016873)
CC results on the importance of the identity of residue 148 for cleavage
CC by RseP differ. {ECO:0000305|PubMed:19706448,
CC ECO:0000305|PubMed:23016873}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D13169; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U10148; AAA83999.1; -; Genomic_DNA.
DR EMBL; U37089; AAC45315.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10919.1; -; Genomic_DNA.
DR EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75625.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76748.1; -; Genomic_DNA.
DR EMBL; U37455; AAC45318.1; -; Genomic_DNA.
DR PIR; B57255; B57255.
DR RefSeq; NP_417067.1; NC_000913.3.
DR RefSeq; WP_001168459.1; NZ_STEB01000011.1.
DR PDB; 1OR7; X-ray; 2.00 A; C/F=1-90.
DR PDB; 1YFN; X-ray; 1.80 A; E/F/G/H=77-108.
DR PDB; 3M4W; X-ray; 2.30 A; E/F/G/H=121-216.
DR PDBsum; 1OR7; -.
DR PDBsum; 1YFN; -.
DR PDBsum; 3M4W; -.
DR AlphaFoldDB; P0AFX7; -.
DR SMR; P0AFX7; -.
DR BioGRID; 4261964; 1.
DR BioGRID; 851391; 1.
DR ComplexPortal; CPX-2532; rpoe-rsea-rseb sigma-antisigma complex.
DR DIP; DIP-39581N; -.
DR IntAct; P0AFX7; 6.
DR STRING; 511145.b2572; -.
DR jPOST; P0AFX7; -.
DR PaxDb; P0AFX7; -.
DR PRIDE; P0AFX7; -.
DR EnsemblBacteria; AAC75625; AAC75625; b2572.
DR EnsemblBacteria; BAE76748; BAE76748; BAE76748.
DR GeneID; 66673539; -.
DR GeneID; 947053; -.
DR KEGG; ecj:JW2556; -.
DR KEGG; eco:b2572; -.
DR PATRIC; fig|1411691.4.peg.4162; -.
DR EchoBASE; EB2245; -.
DR eggNOG; COG3073; Bacteria.
DR HOGENOM; CLU_108851_1_0_6; -.
DR InParanoid; P0AFX7; -.
DR OMA; PEWNIAE; -.
DR PhylomeDB; P0AFX7; -.
DR BioCyc; EcoCyc:EG12341-MON; -.
DR EvolutionaryTrace; P0AFX7; -.
DR PRO; PR:P0AFX7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:1903865; C:sigma factor antagonist complex; IPI:ComplexPortal.
DR GO; GO:0016989; F:sigma factor antagonist activity; IMP:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR CDD; cd16328; RseA_N; 1.
DR DisProt; DP00552; -.
DR Gene3D; 1.10.10.880; -; 1.
DR InterPro; IPR005573; Anti-sigma_E_RseA_C.
DR InterPro; IPR005572; Anti-sigma_E_RseA_N.
DR InterPro; IPR036147; Anti-sigma_E_RseA_N_sf.
DR InterPro; IPR026279; RseA.
DR Pfam; PF03873; RseA_C; 1.
DR Pfam; PF03872; RseA_N; 1.
DR PIRSF; PIRSF016938; RseA; 1.
DR SUPFAM; SSF89069; SSF89069; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Coiled coil;
KW Direct protein sequencing; Membrane; Reference proteome; Signal-anchor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..216
FT /note="Anti-sigma-E factor RseA"
FT /id="PRO_0000097480"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9159522"
FT TRANSMEM 101..118
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 119..216
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9159522"
FT REGION 1..97
FT /note="Sufficient to repress sigma-E"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..186
FT /note="Primary binding site for RseB"
FT REGION 190..200
FT /note="Poly-Gln (Q2)"
FT COILED 158..202
FT /evidence="ECO:0000255"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108..109
FT /note="Cleavage; by RseP"
FT SITE 148..149
FT /note="Cleavage; by DegS"
FT MUTAGEN 1..28
FT /note="Missing: Loss of anti-sigma factor activity."
FT /evidence="ECO:0000269|PubMed:9159522"
FT MUTAGEN 11
FT /note="D->H: Loss of anti-sigma factor activity."
FT /evidence="ECO:0000269|PubMed:9159522"
FT MUTAGEN 19
FT /note="L->P: Loss of anti-sigma factor activity."
FT /evidence="ECO:0000269|PubMed:9159522"
FT MUTAGEN 33
FT /note="W->C: Loss of anti-sigma factor activity."
FT /evidence="ECO:0000269|PubMed:9159522"
FT MUTAGEN 79
FT /note="Q->A: No binding of N-terminal fragment to SspB."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 85
FT /note="W->A: No binding of N-terminal fragment to SspB."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 88
FT /note="M->A: Reduced binding of N-terminal fragment to
FT SspB."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 107..108
FT /note="AA->DD: Significantly less degradation by ClpX-ClpP
FT when present as a 1-108 peptide fragment."
FT /evidence="ECO:0000269|PubMed:15371343"
FT MUTAGEN 146
FT /note="S->X: No effect on protein cleavage."
FT /evidence="ECO:0000269|PubMed:19706448"
FT MUTAGEN 147
FT /note="P->X: No effect on protein cleavage in vitro and in
FT vivo."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 148
FT /note="V->A,C,I,L,M,N,T: Normal cleavage by DegS and RseP
FT in vitro (PubMed:19706448), for A-148 decreased cleavage by
FT DegS in vivo (PubMed:23016873)."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 148
FT /note="V->D,E,G,F,P: Not cleaved by DegS nor RseP in vitro
FT (PubMed:19706448)."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 148
FT /note="V->H,K,Q,R,S,Y: Cleaved by DegS but not by RseP in
FT vitro (PubMed:19706448), for R-148 and S-148 decreased
FT cleavage by DegS in vivo (PubMed:23016873)."
FT /evidence="ECO:0000269|PubMed:19706448,
FT ECO:0000269|PubMed:23016873"
FT MUTAGEN 162..169
FT /note="QQQQVQEQ->AAAAVAEA: RseA is degraded by RseP in the
FT absence of DegS."
FT /evidence="ECO:0000269|PubMed:14633997"
FT MUTAGEN 172
FT /note="R->A: Still binds RseB. No binding to RseB; when
FT associated with A-185."
FT /evidence="ECO:0000269|PubMed:17496148"
FT MUTAGEN 172
FT /note="R->D: No binding to RseB."
FT /evidence="ECO:0000269|PubMed:17496148"
FT MUTAGEN 185
FT /note="R->A: Still binds RseB. No binding to RseB; when
FT associated with A-172."
FT /evidence="ECO:0000269|PubMed:17496148"
FT MUTAGEN 185
FT /note="R->E: No binding to RseB."
FT /evidence="ECO:0000269|PubMed:17496148"
FT MUTAGEN 190..200
FT /note="QLQFEQAQTQQ->ALAFFAAATAA: RseA is degraded by RseP
FT in the absence of DegS."
FT /evidence="ECO:0000269|PubMed:14633997"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 27..44
FT /evidence="ECO:0007829|PDB:1OR7"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1OR7"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1YFN"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:1YFN"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3M4W"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:3M4W"
SQ SEQUENCE 216 AA; 24321 MW; 63BD12131C611C32 CRC64;
MQKEQLSALM DGETLDSELL NELAHNPEMQ KTWESYHLIR DSMRGDTPEV LHFDISSRVM
AAIEEEPVRQ PATLIPEAQP APHQWQKMPF WQKVRPWAAQ LTQMGVAACV SLAVIVGVQH
YNGQSETSQQ PETPVFNTLP MMGKASPVSL GVPSEATANN GQQQQVQEQR RRINAMLQDY
ELQRRLHSEQ LQFEQAQTQQ AAVQVPGIQT LGTQSQ
