RSEB_ECOLI
ID RSEB_ECOLI Reviewed; 318 AA.
AC P0AFX9; P46186; Q2MAF9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sigma-E factor regulatory protein RseB;
DE Flags: Precursor;
GN Name=rseB; OrderedLocusNames=b2571, JW2555;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RSEA,
RP SUBUNIT, SUBCELLULAR LOCATION, OPERON, 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 [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 FUNCTION, INTERACTION WITH RSEA, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND OPERON.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 INTERACTION WITH RSEA, AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION, INTERACTION WITH RSEA, AND SUBUNIT.
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 [10]
RP INTERACTION WITH RSEA, 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 [11]
RP FUNCTION.
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 [12]
RP FUNCTION, BINDING TO RSEA, BINDING TO LIPID-A, AND ACTIVITY REGULATION.
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 [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 23-318, INTERACTION WITH RSEA,
RP SUBUNIT, AND DOMAIN.
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-318, SUBUNIT, AND BINDING TO
RP RSEA.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-318 IN COMPLEX WITH RSEA.
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: Negatively modulates the activity of sigma-E (RpoE) by
CC stabilizing RseA under non-stress conditions. Although not essential
CC for association of sigma-E with Rsea it increases their affinity 2- to
CC 3-fold. When bound to RseA it prevents proteolysis by DegS, which is
CC probably relieved by lipopolysaccharide binding (LPS).
CC {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:17360428,
CC ECO:0000269|PubMed:21245315, ECO:0000269|PubMed:23687042,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
CC -!- ACTIVITY REGULATION: Binding to RseA is inhibited by LPS fragments;
CC phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl chains
CC are minimally necessary to disrupt binding to RseA. Once RseB is no
CC longer bound to RseA the latter is susceptible to DegS degradation.
CC Thus if periplasmic LPS levels increase the sigma-E regulon is induced.
CC {ECO:0000269|PubMed:23687042}.
CC -!- SUBUNIT: Homodimer. Interacts with RseA with 1:1 stoichiometry. Binding
CC to LPS stabilzes a homotetramer that does not bind RseA.
CC {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:17360428,
CC ECO:0000269|PubMed:17496148, ECO:0000269|PubMed:17692869,
CC ECO:0000269|PubMed:18421143, ECO:0000269|PubMed:20512978,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
CC -!- INTERACTION:
CC P0AFX9; P0AFX7: rseA; NbExp=9; IntAct=EBI-1135231, EBI-1117560;
CC P0AFX9; P0AFX9: rseB; NbExp=3; IntAct=EBI-1135231, EBI-1135231;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11777003,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Partially
CC associates with the inner membrane via RseA.
CC -!- DOMAIN: The N-terminal domain (residues 24-203) is responsible for
CC oligomerization, while the C-terminal domain (residues 222-318)
CC interacts with RseA. {ECO:0000269|PubMed:17692869}.
CC -!- DISRUPTION PHENOTYPE: About 2-fold increased sigma-E activity, 2-fold
CC decrease in stability of RseA. {ECO:0000269|PubMed:10500101,
CC ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}.
CC -!- MISCELLANEOUS: Part of the rseD-rpoE-rseA-rseB-rseC operon
CC (PubMed:9159522, PubMed:9159523, PubMed:28924029).
CC {ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- SIMILARITY: Belongs to the RseB family. {ECO:0000305}.
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DR EMBL; U37089; AAC45316.1; -; Genomic_DNA.
DR EMBL; U37455; AAC45319.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10918.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75624.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76747.1; -; Genomic_DNA.
DR PIR; I83298; I83298.
DR RefSeq; NP_417066.1; NC_000913.3.
DR RefSeq; WP_000812053.1; NZ_SSZK01000005.1.
DR PDB; 2P4B; X-ray; 2.40 A; A/B/C=24-318.
DR PDB; 2V42; X-ray; 2.75 A; A/B=23-318.
DR PDB; 2V43; X-ray; 2.37 A; A/B/C=23-318.
DR PDB; 3M4W; X-ray; 2.30 A; A/B/C/D=24-318.
DR PDBsum; 2P4B; -.
DR PDBsum; 2V42; -.
DR PDBsum; 2V43; -.
DR PDBsum; 3M4W; -.
DR AlphaFoldDB; P0AFX9; -.
DR SMR; P0AFX9; -.
DR BioGRID; 4260602; 25.
DR ComplexPortal; CPX-2532; rpoe-rsea-rseb sigma-antisigma complex.
DR DIP; DIP-10802N; -.
DR IntAct; P0AFX9; 2.
DR STRING; 511145.b2571; -.
DR jPOST; P0AFX9; -.
DR PaxDb; P0AFX9; -.
DR PRIDE; P0AFX9; -.
DR EnsemblBacteria; AAC75624; AAC75624; b2571.
DR EnsemblBacteria; BAE76747; BAE76747; BAE76747.
DR GeneID; 66673540; -.
DR GeneID; 947054; -.
DR KEGG; ecj:JW2555; -.
DR KEGG; eco:b2571; -.
DR PATRIC; fig|1411691.4.peg.4163; -.
DR EchoBASE; EB2969; -.
DR eggNOG; COG3026; Bacteria.
DR HOGENOM; CLU_054710_1_0_6; -.
DR InParanoid; P0AFX9; -.
DR OMA; DDFRYQY; -.
DR PhylomeDB; P0AFX9; -.
DR BioCyc; EcoCyc:G7348-MON; -.
DR EvolutionaryTrace; P0AFX9; -.
DR PRO; PR:P0AFX9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:1903865; C:sigma factor antagonist complex; IPI:ComplexPortal.
DR GO; GO:0045152; F:antisigma factor binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0032885; P:regulation of polysaccharide biosynthetic process; IBA:GO_Central.
DR CDD; cd16327; RseB; 1.
DR Gene3D; 3.30.200.100; -; 1.
DR InterPro; IPR033436; MucB/RseB_C.
DR InterPro; IPR038484; MucB/RseB_C_sf.
DR InterPro; IPR033434; MucB/RseB_N.
DR InterPro; IPR005588; MucB_RseB.
DR PANTHER; PTHR38782; PTHR38782; 1.
DR Pfam; PF03888; MucB_RseB; 1.
DR Pfam; PF17188; MucB_RseB_C; 1.
DR PIRSF; PIRSF005427; RseB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid-binding; Periplasm; Reference proteome; Signal;
KW Transcription; Transcription regulation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..318
FT /note="Sigma-E factor regulatory protein RseB"
FT /id="PRO_0000022249"
FT REGION 24..203
FT /note="Responsible for oligomerization"
FT REGION 222..318
FT /note="Interaction with RseA"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 54..64
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2V42"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3M4W"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3M4W"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3M4W"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 179..193
FT /evidence="ECO:0007829|PDB:3M4W"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2V43"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:3M4W"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:3M4W"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2P4B"
SQ 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
