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Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein)

 RSEA_ECOLI              Reviewed;         216 AA.
P0AFX7; P38106; Q2MAF8;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
30-AUG-2017, entry version 89.
RecName: Full=Anti-sigma-E factor RseA;
AltName: Full=Regulator of SigE;
AltName: Full=Sigma-E anti-sigma factor RseA;
AltName: Full=Sigma-E factor negative regulatory protein;
Name=rseA; Synonyms=mclA, yfiJ; OrderedLocusNames=b2572, JW2556;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
STRAIN=K12;
PubMed=7768826; DOI=10.1128/jb.177.11.3259-3268.1995;
Yu H., Schurr M.J., Deretic V.;
"Functional equivalence of Escherichia coli sigma E and Pseudomonas
aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity
to reactive oxygen intermediates in algU mutants of P. aeruginosa.";
J. Bacteriol. 177:3259-3268(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7889935;
Raina S., Missiakas D., Georgopoulos C.;
"The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor
of Escherichia coli.";
EMBO J. 14:1043-1055(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Nashimoto H., Saito N.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
STRAIN=K12;
Nashimoto H.;
"Non-ribosomal proteins affecting the assembly of ribosomes in
Escherichia coli.";
(In) Nierhaus K.H. (eds.);
The translational apparatus, pp.185-195, Plenum Press, New York
(1993).
[7]
PROTEIN SEQUENCE OF 4-108, INTERACTION WITH RPOE AND SSPB, DOMAIN,
CLEAVAGE BY CLPX-CLPP, AND MUTAGENESIS OF 107-ALA-ALA-108.
PubMed=15371343; DOI=10.1101/gad.1240104;
Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
"Modulating substrate choice: the SspB adaptor delivers a regulator of
the extracytoplasmic-stress response to the AAA+ protease ClpXP for
degradation.";
Genes Dev. 18:2292-2301(2004).
[8]
PROTEIN SEQUENCE OF 149-153, AND CLEAVAGE BY DEGS.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=12679035; DOI=10.1016/S0092-8674(03)00203-4;
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.;
"OMP peptide signals initiate the envelope-stress response by
activating DegS protease via relief of inhibition mediated by its PDZ
domain.";
Cell 113:61-71(2003).
[9]
PROTEIN SEQUENCE OF 149-153, CLEAVAGE BY DEGS AND RSEP, AND
MUTAGENESIS OF SER-146; PRO-147 AND VAL-148.
PubMed=19706448; DOI=10.1073/pnas.0903289106;
Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.;
"Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic
amino acid following DegS cleavage.";
Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-216, FUNCTION AS AN
ANTI-SIGMA FACTOR, INTERACTION WITH RPOE AND RSEB, SUBUNIT,
SUBCELLULAR LOCATION, OPERON, DOMAIN, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=9159523; DOI=10.1046/j.1365-2958.1997.3611718.x;
De Las Penas A., Connolly L., Gross C.A.;
"The sigmaE-mediated response to extracytoplasmic stress in
Escherichia coli is transduced by RseA and RseB, two negative
regulators of sigmaE.";
Mol. Microbiol. 24:373-385(1997).
[11]
FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH RPOE AND RSEB,
SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, DISRUPTION PHENOTYPE,
OPERON, AND MUTAGENESIS OF 1-MET--GLU-28; ASP-11; LEU-19 AND TRP-33.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9159522; DOI=10.1046/j.1365-2958.1997.3601713.x;
Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.;
"Modulation of the Escherichia coli sigmaE (RpoE) heat-shock
transcription-factor activity by the RseA, RseB and RseC proteins.";
Mol. Microbiol. 24:355-371(1997).
[12]
INDUCTION, AND PROBABLE CLEAVAGE BY DEGS.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=10500101; DOI=10.1101/gad.13.18.2449;
Ades S.E., Connolly L.E., Alba B.M., Gross C.A.;
"The Escherichia coli sigma(E)-dependent extracytoplasmic stress
response is controlled by the regulated proteolysis of an anti-sigma
factor.";
Genes Dev. 13:2449-2461(1999).
[13]
INTERACTION WITH RPOE AND RSEB, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11777003; DOI=10.1074/jbc.M006214200;
Collinet B., Yuzawa H., Chen T., Herrera C., Missiakas D.;
"RseB binding to the periplasmic domain of RseA modulates the
RseA:sigmaE interaction in the cytoplasm and the availability of
sigmaE.RNA polymerase.";
J. Biol. Chem. 275:33898-33904(2000).
[14]
CLEAVAGE BY DEGS AND RSEP.
STRAIN=K12;
PubMed=12183368; DOI=10.1101/gad.1002302;
Kanehara K., Ito K., Akiyama Y.;
"YaeL (EcfE) activates the sigma(E) pathway of stress response through
a site-2 cleavage of anti-sigma(E), RseA.";
Genes Dev. 16:2147-2155(2002).
[15]
CLEAVAGE BY DEGS AND RSEP, AND SUBCELLULAR LOCATION.
STRAIN=K12;
PubMed=12183369; DOI=10.1101/gad.1008902;
Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.;
"DegS and YaeL participate sequentially in the cleavage of RseA to
activate the sigma(E)-dependent extracytoplasmic stress response.";
Genes Dev. 16:2156-2168(2002).
[16]
INTERACTION WITH RPOE, AND SUBUNIT.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=12016219; DOI=10.1074/jbc.M202881200;
Tam C., Collinet B., Lau G., Raina S., Missiakas D.;
"Interaction of the conserved region 4.2 of sigma(E) with the RseA
anti-sigma factor.";
J. Biol. Chem. 277:27282-27287(2002).
[17]
INTERACTION WITH RSEP, DOMAIN, CLEAVAGE BY RSEP, AND MUTAGENESIS OF
162-GLN--GLN-169 AND 190-GLN--GLN-200.
STRAIN=K12 / AD16;
PubMed=14633997; DOI=10.1093/emboj/cdg602;
Kanehara K., Ito K., Akiyama Y.;
"YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and
a Gln-rich region of RseA.";
EMBO J. 22:6389-6398(2003).
[18]
INDUCTION BY COLD SHOCK.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14527658; DOI=10.1016/S0923-2508(03)00167-0;
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V.,
Pesole G., Deho G.;
"Changes in Escherichia coli transcriptome during acclimatization at
low temperature.";
Res. Microbiol. 154:573-580(2003).
[19]
CLEAVAGE BY RSEP.
PubMed=15496982; DOI=10.1038/sj.emboj.7600449;
Akiyama Y., Kanehara K., Ito K.;
"RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane
sequences.";
EMBO J. 23:4434-4442(2004).
[20]
REGULATION OF DEGRADATION.
PubMed=17210793; DOI=10.1101/gad.1496707;
Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
"Design principles of the proteolytic cascade governing the sigmaE-
mediated envelope stress response in Escherichia coli: keys to graded,
buffered, and rapid signal transduction.";
Genes Dev. 21:124-136(2007).
[21]
INTERACTION WITH RSEB, AND SUBUNIT.
PubMed=17692869; DOI=10.1016/j.jmb.2007.06.039;
Wollmann P., Zeth K.;
"The structure of RseB: a sensor in periplasmic stress response of E.
coli.";
J. Mol. Biol. 372:927-941(2007).
[22]
INTERACTION WITH RSEB, SUBUNIT, AND DOMAIN.
PubMed=17360428; DOI=10.1073/pnas.0611567104;
Cezairliyan B.O., Sauer R.T.;
"Inhibition of regulated proteolysis by RseB.";
Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007).
[23]
BINDING TO RSEB, AND MUTAGENESIS OF ARG-172 AND ARG-185.
PubMed=17496148; DOI=10.1073/pnas.0703117104;
Kim D.Y., Jin K.S., Kwon E., Ree M., Kim K.K.;
"Crystal structure of RseB and a model of its binding mode to RseA.";
Proc. Natl. Acad. Sci. U.S.A. 104:8779-8784(2007).
[24]
INTERACTION WITH RSEP, AND CLEAVAGE BY RSEP.
STRAIN=K12 / AD16;
PubMed=18268014; DOI=10.1074/jbc.M709984200;
Koide K., Ito K., Akiyama Y.;
"Substrate recognition and binding by RseP, an Escherichia coli
intramembrane protease.";
J. Biol. Chem. 283:9562-9570(2008).
[25]
INTERACTION WITH RSEB, AND SUBUNIT.
PubMed=18421143; DOI=10.1107/S0909049507066319;
Jin K.S., Kim D.Y., Rho Y., Le V.B., Kwon E., Kim K.K., Ree M.;
"Solution structures of RseA and its complex with RseB.";
J. Synchrotron Radiat. 15:219-222(2008).
[26]
CLEAVAGE BY DEGS AND RSEP.
STRAIN=K12;
PubMed=18945679; DOI=10.1074/jbc.M806603200;
Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.;
"A pair of circularly permutated PDZ domains control RseP, the S2P
family intramembrane protease of Escherichia coli.";
J. Biol. Chem. 283:35042-35052(2008).
[27]
MUTAGENESIS OF PRO-147 AND VAL-148.
STRAIN=K12;
PubMed=23016873; DOI=10.1111/mmi.12053;
Hizukuri Y., Akiyama Y.;
"PDZ domains of RseP are not essential for sequential cleavage of RseA
or stress-induced sigma(E) activation in vivo.";
Mol. Microbiol. 86:1232-1245(2012).
[28]
FUNCTION, BINDING TO RSEB, SUBUNIT, AND CLEAVAGE BY DEGS.
STRAIN=K12;
PubMed=23687042; DOI=10.1126/science.1235358;
Lima S., Guo M.S., Chaba R., Gross C.A., Sauer R.T.;
"Dual molecular signals mediate the bacterial response to outer-
membrane stress.";
Science 340:837-841(2013).
[29]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-90 IN COMPLEX WITH RPOE,
MODE OF ACTION, AND SUBUNIT.
PubMed=12718891; DOI=10.1016/S1097-2765(03)00148-5;
Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M.,
Gross C.A., Darst S.A.;
"Crystal structure of Escherichia coli sigmaE with the cytoplasmic
domain of its anti-sigma RseA.";
Mol. Cell 11:1067-1078(2003).
[30]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 77-108 IN COMPLEX WITH SSPB,
SUBUNIT, AND MUTAGENESIS OF GLN-79; TRP-85 AND MET-88.
PubMed=15880122; DOI=10.1038/nsmb934;
Levchenko I., Grant R.A., Flynn J.M., Sauer R.T., Baker T.A.;
"Versatile modes of peptide recognition by the AAA+ adaptor protein
SspB.";
Nat. Struct. Mol. Biol. 12:520-525(2005).
[31]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 121-216 IN COMPLEX WITH
RSEB.
PubMed=20512978; DOI=10.1002/pro.393;
Kim D.Y., Kwon E., Choi J., Hwang H.Y., Kim K.K.;
"Structural basis for the negative regulation of bacterial stress
response by RseB.";
Protein Sci. 19:1258-1263(2010).
-!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
sigma factor sigma-E (RpoE). ECF sigma factors are held in an
inactive form by an anti-sigma factor until released by regulated
intramembrane proteolysis (RIP). RIP occurs when an
extracytoplasmic signal triggers a concerted proteolytic cascade
to transmit information and elicit cellular responses. The
membrane-spanning regulatory substrate protein is first cut
periplasmically (site-1 protease, S1P, DegS), then within the
membrane itself (site-2 protease, S2P, RseP), while cytoplasmic
proteases finish degrading the anti-sigma factor, liberating
sigma-E. Overexpression of RseA blocks sigma-E from acting,
results in cell lysis in stationary phase and temperature-
sensitivity above 37 degrees Celsius.
{ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}.
-!- SUBUNIT: Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE);
this inhibits the interaction of sigma-E with the RNA polymerase
catalytic core and leads to a decreased expression of sigma-E-
regulated genes. Interacts with RseB with 1:1 stoichiometry. The
liberated N-terminus (residues 1-108) forms a complex with SspB
and RpoE; binding to SspB is competitively inhibited by ssrA-tags,
although the 2 proteins bind in opposite directions in SspB's
peptide-binding groove. {ECO:0000269|PubMed:11777003,
ECO:0000269|PubMed:12016219, ECO:0000269|PubMed:12718891,
ECO:0000269|PubMed:14633997, ECO:0000269|PubMed:15371343,
ECO:0000269|PubMed:15880122, ECO:0000269|PubMed:17360428,
ECO:0000269|PubMed:17692869, ECO:0000269|PubMed:18268014,
ECO:0000269|PubMed:18421143, ECO:0000269|PubMed:20512978,
ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}.
-!- INTERACTION:
P0AEE3:degS; NbExp=4; IntAct=EBI-1117560, EBI-1132101;
P0AFX9:rseB; NbExp=6; IntAct=EBI-1117560, EBI-1135231;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}; Single-
pass type II membrane protein {ECO:0000269|PubMed:11777003,
ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}. Note=Following cleavage by DegS the
large fragment of the protein is still in the inner membrane and
retains its anti-sigma-E activity.
-!- INDUCTION: Transiently induced by cold shock in a PNPase-dependent
fashion. Upon stress induction (OMPs or heat shock) decreases in
under 3 minutes (at protein level). Part of the rpoE-rseA-rseB-
rseC operon. {ECO:0000269|PubMed:10500101,
ECO:0000269|PubMed:14527658}.
-!- DOMAIN: The N-terminal cytosolic domain interacts with sigma-E,
and upon overexpression leads to temperature sensitivity above 37
degrees Celsius and cell lysis in stationary phase. After
degradation by RseP residues 77-108 bind to SspB, targeting RseA
for degradation by the ClpX-ClpP protease.
-!- DOMAIN: The C-terminal periplasmic domain (residues 169-186)
interacts with RseB and is also the target for DegS; RseB and DegS
binding sites do not appreciably overlap. Gln-rich regions
(residues 162-169, Q1, and 190-200, Q2) contribute to preventing
RseP from acting before DegS. Insertion of 8 consecutive Gln
residues into a protein lacking Q1 and Q2 restores DegS-
depenedence of RseP cleavage.
-!- PTM: Sequentially cleaved by DegS (a site-1 protease) in its
periplasmic domain between Val-148 and Ser-149, then by RseP (a
site-2 protease) between positions Ala-108 and Cys-109. The N-
terminal fragment is then degraded by primarily ClpX-ClpP in an
ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-
ClpP frees RpoE from RseA. {ECO:0000269|PubMed:12183368,
ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:12679035,
ECO:0000269|PubMed:14633997, ECO:0000269|PubMed:15371343,
ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014,
ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:19706448,
ECO:0000269|PubMed:23687042}.
-!- DISRUPTION PHENOTYPE: About 10-fold increased sigma-E activity.
Neither sigma-E nor RseB associate with the inner membrane.
{ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}.
-!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
-!- CAUTION: PubMed:9159522 mis-identifies Trp-33 as residue 32.
{ECO:0000305}.
-!- CAUTION: In vitro (PubMed:19706448) and in vivo (PubMed:23016873)
results on the importance of the identity of residue 148 for
cleavage by RseP differ. {ECO:0000305|PubMed:19706448,
ECO:0000305|PubMed:23016873}.
-!- SEQUENCE CAUTION:
Sequence=D13169; Type=Frameshift; Positions=75; Evidence={ECO:0000305};
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EMBL; U10148; AAA83999.1; -; Genomic_DNA.
EMBL; U37089; AAC45315.1; -; Genomic_DNA.
EMBL; D64044; BAA10919.1; -; Genomic_DNA.
EMBL; D13169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U00096; AAC75625.1; -; Genomic_DNA.
EMBL; AP009048; BAE76748.1; -; Genomic_DNA.
EMBL; U37455; AAC45318.1; -; Genomic_DNA.
PIR; B57255; B57255.
RefSeq; NP_417067.1; NC_000913.3.
RefSeq; WP_001168459.1; NZ_LN832404.1.
PDB; 1OR7; X-ray; 2.00 A; C/F=1-90.
PDB; 1YFN; X-ray; 1.80 A; E/F/G/H=77-108.
PDB; 3M4W; X-ray; 2.30 A; E/F/G/H=121-216.
PDBsum; 1OR7; -.
PDBsum; 1YFN; -.
PDBsum; 3M4W; -.
DisProt; DP00552; -.
ProteinModelPortal; P0AFX7; -.
SMR; P0AFX7; -.
DIP; DIP-39581N; -.
IntAct; P0AFX7; 5.
STRING; 316385.ECDH10B_2740; -.
PaxDb; P0AFX7; -.
PRIDE; P0AFX7; -.
EnsemblBacteria; AAC75625; AAC75625; b2572.
EnsemblBacteria; BAE76748; BAE76748; BAE76748.
GeneID; 947053; -.
KEGG; ecj:JW2556; -.
KEGG; eco:b2572; -.
PATRIC; fig|1411691.4.peg.4162; -.
EchoBASE; EB2245; -.
EcoGene; EG12341; rseA.
eggNOG; ENOG41069PW; Bacteria.
eggNOG; COG3073; LUCA.
HOGENOM; HOG000272262; -.
InParanoid; P0AFX7; -.
KO; K03597; -.
BioCyc; EcoCyc:EG12341-MONOMER; -.
EvolutionaryTrace; P0AFX7; -.
PRO; PR:P0AFX7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016989; F:sigma factor antagonist activity; IMP:EcoCyc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006950; P:response to stress; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd16328; RseA_N; 1.
InterPro; IPR005573; Anti-sigma_E_RseA_C.
InterPro; IPR005572; Anti-sigma_E_RseA_N.
InterPro; IPR026279; RseA.
Pfam; PF03873; RseA_C; 1.
Pfam; PF03872; RseA_N; 1.
PIRSF; PIRSF016938; RseA; 1.
SUPFAM; SSF89069; SSF89069; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Coiled coil;
Complete proteome; Direct protein sequencing; Membrane;
Reference proteome; Signal-anchor; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix.
CHAIN 1 216 Anti-sigma-E factor RseA.
/FTId=PRO_0000097480.
TOPO_DOM 1 100 Cytoplasmic.
{ECO:0000305|PubMed:9159522}.
TRANSMEM 101 118 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 119 216 Periplasmic.
{ECO:0000305|PubMed:9159522}.
REGION 1 97 Sufficient to repress sigma-E.
REGION 169 186 Primary binding site for RseB.
REGION 190 200 Poly-Gln (Q2).
COILED 158 202 {ECO:0000255}.
COMPBIAS 162 169 Poly-Gln (Q1).
SITE 108 109 Cleavage; by RseP.
SITE 148 149 Cleavage; by DegS.
MUTAGEN 1 28 Missing: Loss of anti-sigma factor
activity. {ECO:0000269|PubMed:9159522}.
MUTAGEN 11 11 D->H: Loss of anti-sigma factor activity.
{ECO:0000269|PubMed:9159522}.
MUTAGEN 19 19 L->P: Loss of anti-sigma factor activity.
{ECO:0000269|PubMed:9159522}.
MUTAGEN 33 33 W->C: Loss of anti-sigma factor activity.
{ECO:0000269|PubMed:9159522}.
MUTAGEN 79 79 Q->A: No binding of N-terminal fragment
to SspB. {ECO:0000269|PubMed:15880122}.
MUTAGEN 85 85 W->A: No binding of N-terminal fragment
to SspB. {ECO:0000269|PubMed:15880122}.
MUTAGEN 88 88 M->A: Reduced binding of N-terminal
fragment to SspB.
{ECO:0000269|PubMed:15880122}.
MUTAGEN 107 108 AA->DD: Significantly less degradation by
ClpX-ClpP when present as a 1-108 peptide
fragment. {ECO:0000269|PubMed:15371343}.
MUTAGEN 146 146 S->X: No effect on protein cleavage.
{ECO:0000269|PubMed:19706448}.
MUTAGEN 147 147 P->X: No effect on protein cleavage in
vitro and in vivo.
{ECO:0000269|PubMed:19706448,
ECO:0000269|PubMed:23016873}.
MUTAGEN 148 148 V->A,C,I,L,M,N,T: Normal cleavage by DegS
and RseP in vitro (PubMed:19706448), for
A-148 decreased cleavage by DegS in vivo
(PubMed:23016873).
{ECO:0000269|PubMed:19706448,
ECO:0000269|PubMed:23016873}.
MUTAGEN 148 148 V->D,E,G,F,P: Not cleaved by DegS nor
RseP in vitro (PubMed:19706448).
{ECO:0000269|PubMed:19706448,
ECO:0000269|PubMed:23016873}.
MUTAGEN 148 148 V->H,K,Q,R,S,Y: Cleaved by DegS but not
by RseP in vitro (PubMed:19706448), for
R-148 and S-148 decreased cleavage by
DegS in vivo (PubMed:23016873).
{ECO:0000269|PubMed:19706448,
ECO:0000269|PubMed:23016873}.
MUTAGEN 162 169 QQQQVQEQ->AAAAVAEA: RseA is degraded by
RseP in the absence of DegS.
{ECO:0000269|PubMed:14633997}.
MUTAGEN 172 172 R->A: Still binds RseB. No binding to
RseB; when associated with A-185.
{ECO:0000269|PubMed:17496148}.
MUTAGEN 172 172 R->D: No binding to RseB.
{ECO:0000269|PubMed:17496148}.
MUTAGEN 185 185 R->A: Still binds RseB. No binding to
RseB; when associated with A-172.
{ECO:0000269|PubMed:17496148}.
MUTAGEN 185 185 R->E: No binding to RseB.
{ECO:0000269|PubMed:17496148}.
MUTAGEN 190 200 QLQFEQAQTQQ->ALAFFAAATAA: RseA is
degraded by RseP in the absence of DegS.
{ECO:0000269|PubMed:14633997}.
HELIX 3 10 {ECO:0000244|PDB:1OR7}.
HELIX 17 24 {ECO:0000244|PDB:1OR7}.
HELIX 27 44 {ECO:0000244|PDB:1OR7}.
STRAND 49 53 {ECO:0000244|PDB:1OR7}.
HELIX 55 64 {ECO:0000244|PDB:1OR7}.
HELIX 82 85 {ECO:0000244|PDB:1YFN}.
HELIX 89 93 {ECO:0000244|PDB:1YFN}.
HELIX 134 136 {ECO:0000244|PDB:3M4W}.
HELIX 170 186 {ECO:0000244|PDB:3M4W}.
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


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