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Sigma-E factor regulatory protein RseB

 RSEB_ECOLI              Reviewed;         318 AA.
P0AFX9; P46186; Q2MAF9;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
20-JUN-2018, entry version 88.
RecName: Full=Sigma-E factor regulatory protein RseB;
Flags: Precursor;
Name=rseB; OrderedLocusNames=b2571, JW2555;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RSEA,
SUBUNIT, SUBCELLULAR LOCATION, OPERON, 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).
[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]
FUNCTION, INTERACTION WITH RSEA, SUBUNIT, SUBCELLULAR LOCATION,
DISRUPTION PHENOTYPE, AND OPERON.
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).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
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).
[8]
INTERACTION WITH RSEA, AND SUBCELLULAR LOCATION.
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).
[9]
FUNCTION, INTERACTION WITH RSEA, AND SUBUNIT.
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).
[10]
INTERACTION WITH RSEA, 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).
[11]
FUNCTION.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=21245315; DOI=10.1073/pnas.1019277108;
Chaba R., Alba B.M., Guo M.S., Sohn J., Ahuja N., Sauer R.T.,
Gross C.A.;
"Signal integration by DegS and RseB governs the sigma-E-mediated
envelope stress response in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 108:2106-2111(2011).
[12]
FUNCTION, BINDING TO RSEA, BINDING TO LIPID-A, AND ENZYME REGULATION.
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).
[13]
OPERON.
STRAIN=K12 / CF7789;
PubMed=28924029; DOI=10.1128/JB.00484-17;
Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
"Circuitry linking the global Csr and sigma(E)-dependent cell envelope
stress response systems.";
J. Bacteriol. 0:0-0(2017).
[14]
X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 23-318, INTERACTION WITH
RSEA, SUBUNIT, AND DOMAIN.
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).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-318, SUBUNIT, AND BINDING
TO RSEA.
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-318 IN COMPLEX WITH RSEA.
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: Negatively modulates the activity of sigma-E (RpoE) by
stabilizing RseA under non-stress conditions. Although not
essential for association of sigma-E with Rsea it increases their
affinity 2- to 3-fold. When bound to RseA it prevents proteolysis
by DegS, which is probably relieved by lipopolysaccharide binding
(LPS). {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:17360428,
ECO:0000269|PubMed:21245315, ECO:0000269|PubMed:23687042,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
-!- ENZYME REGULATION: Binding to RseA is inhibited by LPS fragments;
phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl
chains are minimally necessary to disrupt binding to RseA. Once
RseB is no longer bound to RseA the latter is susceptible to DegS
degradation. Thus if periplasmic LPS levels increase the sigma-E
regulon is induced. {ECO:0000269|PubMed:23687042}.
-!- SUBUNIT: Homodimer. Interacts with RseA with 1:1 stoichiometry.
Binding to LPS stabilzes a homotetramer that does not bind RseA.
{ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:17360428,
ECO:0000269|PubMed:17496148, ECO:0000269|PubMed:17692869,
ECO:0000269|PubMed:18421143, ECO:0000269|PubMed:20512978,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1135231, EBI-1135231;
P0AFX7:rseA; NbExp=8; IntAct=EBI-1135231, EBI-1117560;
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11777003,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
Note=Partially associates with the inner membrane via RseA.
-!- DOMAIN: The N-terminal domain (residues 24-203) is responsible for
oligomerization, while the C-terminal domain (residues 222-318)
interacts with RseA. {ECO:0000269|PubMed:17692869}.
-!- DISRUPTION PHENOTYPE: About 2-fold increased sigma-E activity, 2-
fold decrease in stability of RseA. {ECO:0000269|PubMed:10500101,
ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
-!- MISCELLANEOUS: Part of the rseD-rpoE-rseA-rseB-rseC operon
(PubMed:9159522, PubMed:9159523, PubMed:28924029).
{ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:9159522,
ECO:0000269|PubMed:9159523}.
-!- SIMILARITY: Belongs to the RseB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U37089; AAC45316.1; -; Genomic_DNA.
EMBL; U37455; AAC45319.1; -; Genomic_DNA.
EMBL; D64044; BAA10918.1; -; Genomic_DNA.
EMBL; U00096; AAC75624.1; -; Genomic_DNA.
EMBL; AP009048; BAE76747.1; -; Genomic_DNA.
PIR; I83298; I83298.
RefSeq; NP_417066.1; NC_000913.3.
RefSeq; WP_000812053.1; NZ_LN832404.1.
PDB; 2P4B; X-ray; 2.40 A; A/B/C=24-318.
PDB; 2V42; X-ray; 2.75 A; A/B=23-318.
PDB; 2V43; X-ray; 2.37 A; A/B/C=23-318.
PDB; 3M4W; X-ray; 2.30 A; A/B/C/D=24-318.
PDBsum; 2P4B; -.
PDBsum; 2V42; -.
PDBsum; 2V43; -.
PDBsum; 3M4W; -.
ProteinModelPortal; P0AFX9; -.
SMR; P0AFX9; -.
BioGrid; 4260602; 25.
ComplexPortal; CPX-2532; Sigma-E factor negative regulation complex.
DIP; DIP-10802N; -.
IntAct; P0AFX9; 2.
STRING; 316385.ECDH10B_2739; -.
EPD; P0AFX9; -.
PaxDb; P0AFX9; -.
PRIDE; P0AFX9; -.
EnsemblBacteria; AAC75624; AAC75624; b2571.
EnsemblBacteria; BAE76747; BAE76747; BAE76747.
GeneID; 947054; -.
KEGG; ecj:JW2555; -.
KEGG; eco:b2571; -.
PATRIC; fig|1411691.4.peg.4163; -.
EchoBASE; EB2969; -.
EcoGene; EG13177; rseB.
eggNOG; ENOG4105VQK; Bacteria.
eggNOG; COG3026; LUCA.
HOGENOM; HOG000272273; -.
InParanoid; P0AFX9; -.
KO; K03598; -.
OMA; VYERNGS; -.
BioCyc; EcoCyc:G7348-MONOMER; -.
EvolutionaryTrace; P0AFX9; -.
PRO; PR:P0AFX9; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0045152; F:antisigma factor binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd16327; RseB; 1.
Gene3D; 3.30.200.100; -; 1.
InterPro; IPR033436; MucB/RseB_C.
InterPro; IPR038484; MucB/RseB_C_sf.
InterPro; IPR033434; MucB/RseB_N.
InterPro; IPR005588; MucB_RseB.
PANTHER; PTHR38782; PTHR38782; 1.
Pfam; PF03888; MucB_RseB; 1.
Pfam; PF17188; MucB_RseB_C; 1.
PIRSF; PIRSF005427; RseB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Lipid-binding; Periplasm;
Reference proteome; Signal; Transcription; Transcription regulation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 318 Sigma-E factor regulatory protein RseB.
/FTId=PRO_0000022249.
REGION 24 203 Responsible for oligomerization.
REGION 222 318 Interaction with RseA.
HELIX 26 40 {ECO:0000244|PDB:3M4W}.
STRAND 41 51 {ECO:0000244|PDB:3M4W}.
STRAND 54 64 {ECO:0000244|PDB:3M4W}.
STRAND 66 75 {ECO:0000244|PDB:3M4W}.
STRAND 77 79 {ECO:0000244|PDB:3M4W}.
STRAND 82 86 {ECO:0000244|PDB:3M4W}.
STRAND 89 93 {ECO:0000244|PDB:3M4W}.
STRAND 100 103 {ECO:0000244|PDB:3M4W}.
STRAND 108 111 {ECO:0000244|PDB:2V42}.
HELIX 113 116 {ECO:0000244|PDB:3M4W}.
HELIX 119 122 {ECO:0000244|PDB:3M4W}.
TURN 123 125 {ECO:0000244|PDB:3M4W}.
STRAND 126 136 {ECO:0000244|PDB:3M4W}.
STRAND 139 148 {ECO:0000244|PDB:3M4W}.
STRAND 155 161 {ECO:0000244|PDB:3M4W}.
TURN 162 164 {ECO:0000244|PDB:3M4W}.
STRAND 167 173 {ECO:0000244|PDB:3M4W}.
STRAND 179 193 {ECO:0000244|PDB:3M4W}.
HELIX 196 203 {ECO:0000244|PDB:3M4W}.
STRAND 223 225 {ECO:0000244|PDB:3M4W}.
STRAND 232 237 {ECO:0000244|PDB:3M4W}.
STRAND 242 245 {ECO:0000244|PDB:2V43}.
STRAND 250 255 {ECO:0000244|PDB:3M4W}.
STRAND 260 267 {ECO:0000244|PDB:3M4W}.
STRAND 275 279 {ECO:0000244|PDB:3M4W}.
STRAND 282 289 {ECO:0000244|PDB:3M4W}.
STRAND 292 300 {ECO:0000244|PDB:3M4W}.
HELIX 302 309 {ECO:0000244|PDB:3M4W}.
STRAND 312 314 {ECO:0000244|PDB:2P4B}.
SEQUENCE 318 AA; 35750 MW; 3F8C34DD85600B54 CRC64;
MKQLWFAMSL VTGSLLFSAN ASATPASGAL LQQMNLASQS LNYELSFISI NKQGVESLRY
RHARLDNRPL AQLLQMDGPR REVVQRGNEI SYFEPGLEPF TLNGDYIVDS LPSLIYTDFK
RLSPYYDFIS VGRTRIADRL CEVIRVVARD GTRYSYIVWM DTESKLPMRV DLLDRDGETL
EQFRVIAFNV NQDISSSMQT LAKANLPPLL SVPVGEKAKF SWTPTWLPQG FSEVSSSRRP
LPTMDNMPIE SRLYSDGLFS FSVNVNRATP SSTDQMLRTG RRTVSTSVRD NAEITIVGEL
PPQTAKRIAE NIKFGAAQ


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