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Anti-sigma-E factor ChrR (Sigma-E anti-sigma factor ChrR) (Transcriptional activator ChrR)

 CHRR_RHOS4              Reviewed;         213 AA.
P40685; Q3IYV5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
16-JAN-2019, entry version 103.
RecName: Full=Anti-sigma-E factor ChrR;
AltName: Full=Sigma-E anti-sigma factor ChrR;
AltName: Full=Transcriptional activator ChrR;
Name=chrR; OrderedLocusNames=RHOS4_27110; ORFNames=RSP_1093;
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
158).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Rhodobacter.
NCBI_TaxID=272943;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-38.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
PubMed=7721683; DOI=10.1128/jb.177.8.1929-1937.1995;
Schilke B.A., Donohue T.J.;
"ChrR positively regulates transcription of the Rhodobacter
sphaeroides cytochrome c2 gene.";
J. Bacteriol. 177:1929-1937(1995).
[2]
SEQUENCE REVISION.
Newman J., Donohue T.J.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
Kaplan S.;
"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-13.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
PubMed=10610760; DOI=10.1006/jmbi.1999.3263;
Newman J.D., Falkowski M.J., Schilke B.A., Anthony L.C., Donohue T.J.;
"The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the
target promoters cycA P3 and rpoE P1.";
J. Mol. Biol. 294:307-320(1999).
[5]
FUNCTION AS AN ANTI-SIGMA FACTOR, COFACTOR, INTERACTION WITH SIGME-E
(RPOE), SUBUNIT, AND MUTAGENESIS OF CYS-35; CYS-38; CYS-187 AND
CYS-189.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
PubMed=11676534; DOI=10.1006/jmbi.2001.5069;
Newman J.D., Anthony J.R., Donohue T.J.;
"The importance of zinc-binding to the function of Rhodobacter
sphaeroides ChrR as an anti-sigma factor.";
J. Mol. Biol. 313:485-499(2001).
[6]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
PubMed=15855269; DOI=10.1073/pnas.0502225102;
Anthony J.R., Warczak K.L., Donohue T.J.;
"A transcriptional response to singlet oxygen, a toxic byproduct of
photosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 102:6502-6507(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-195, FUNCTION AS AN
ANTI-SIGMA FACTOR, ZINC-BINDING, INTERACTION WITH RPOE, INDUCTION,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-5; HIS-6; HIS-31; CYS-35
AND CYS-38.
STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
PubMed=17803943; DOI=10.1016/j.molcel.2007.07.009;
Campbell E.A., Greenwell R., Anthony J.R., Wang S., Lim L., Das K.,
Sofia H.J., Donohue T.J., Darst S.A.;
"A conserved structural module regulates transcriptional responses to
diverse stress signals in bacteria.";
Mol. Cell 27:793-805(2007).
-!- FUNCTION: Anti-sigma factor that inhibits the activity of the
extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby
indirectly regulating the transcription of the cycA and rpoE
genes. ECF sigma factors are held in an inactive form by a cognate
anti-sigma factor. {ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:15855269, ECO:0000269|PubMed:17803943}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11676534};
Note=Binds 2 Zn(2+) ion per subunit. The Zn(2+) bound by the N-
terminus is required for anti-sigma function, the function of the
Zn(2+) bound by the C-terminus is unknown.
{ECO:0000269|PubMed:11676534};
-!- SUBUNIT: Forms a 1:1 complex with cognate ECF RNA polymerase sigma
factor RpoE; this inhibits the interaction of RpoE with the RNA
polymerase catalytic core. {ECO:0000269|PubMed:11676534}.
-!- INDUCTION: Induced by singlet oxygen. Autoregulated. Part of the
rpoE-chrR operon. {ECO:0000269|PubMed:17803943}.
-!- DOMAIN: The N-terminal anti-sigma domain (residues 1-85) is
necessary and sufficient to bind sigma-E and inhibit its activity.
The C-terminal domain (residues 86-194) is required to respond to
singlet oxygen (PubMed:17803943). {ECO:0000269|PubMed:17803943}.
-!- DISRUPTION PHENOTYPE: For single chrR mutant about 12-fold
increase in rpoE-regulated genes. For double rpoE-chrR deletion
mutant no effect on anaerobic photosynthetic growth. In
illuminated aerobically growing cells double deletion is
bacteriostatic. {ECO:0000269|PubMed:15855269,
ECO:0000269|PubMed:17803943}.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U11283; AAB17905.1; -; Genomic_DNA.
EMBL; CP000143; ABA80279.1; -; Genomic_DNA.
PIR; B58883; B58883.
RefSeq; WP_011338712.1; NZ_CP030271.1.
RefSeq; YP_354180.1; NC_007493.2.
PDB; 2Q1Z; X-ray; 2.40 A; B/D=1-195.
PDB; 2Z2S; X-ray; 2.70 A; B/D/F/H=1-203.
PDBsum; 2Q1Z; -.
PDBsum; 2Z2S; -.
ProteinModelPortal; P40685; -.
SMR; P40685; -.
STRING; 272943.RSP_1093; -.
EnsemblBacteria; ABA80279; ABA80279; RSP_1093.
GeneID; 3720852; -.
KEGG; rsp:RSP_1093; -.
PATRIC; fig|272943.9.peg.3072; -.
eggNOG; ENOG4108NIX; Bacteria.
eggNOG; COG3806; LUCA.
HOGENOM; HOG000284569; -.
KO; K07167; -.
OMA; PLHFTSG; -.
PhylomeDB; P40685; -.
EvolutionaryTrace; P40685; -.
Proteomes; UP000002703; Chromosome 1.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR012807; Anti-sigma_ChrR.
InterPro; IPR025979; ChrR-like_cupin_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR011051; RmlC_Cupin_sf.
Pfam; PF12973; Cupin_7; 1.
SUPFAM; SSF51182; SSF51182; 1.
TIGRFAMs; TIGR02451; anti_sig_ChrR; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Direct protein sequencing;
DNA-binding; Metal-binding; Reference proteome; Transcription;
Transcription regulation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10610760}.
CHAIN 2 213 Anti-sigma-E factor ChrR.
/FTId=PRO_0000089658.
REGION 2 85 Sufficient to bind sigma factor and
inhibit its activity.
REGION 86 194 Required for response to singlet oxygen.
METAL 6 6 Zinc 1; via pros nitrogen.
METAL 31 31 Zinc 1; via tele nitrogen.
METAL 35 35 Zinc 1.
METAL 38 38 Zinc 1.
METAL 141 141 Zinc 2; via pros nitrogen.
METAL 143 143 Zinc 2; via tele nitrogen.
METAL 147 147 Zinc 2.
METAL 177 177 Zinc 2; via tele nitrogen.
MUTAGEN 5 5 H->A: No effect on anti-sigma function.
{ECO:0000269|PubMed:17803943}.
MUTAGEN 6 6 H->A: Loss of anti-sigma function.
{ECO:0000269|PubMed:17803943}.
MUTAGEN 31 31 H->A: No effect on anti-sigma function.
{ECO:0000269|PubMed:17803943}.
MUTAGEN 35 35 C->A: Loss of anti-sigma function.
{ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:17803943}.
MUTAGEN 35 35 C->S: Loss of function; no effect on zinc
binding. {ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:17803943}.
MUTAGEN 38 38 C->A: Loss of anti-sigma function.
{ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:17803943,
ECO:0000269|PubMed:7721683}.
MUTAGEN 38 38 C->R: In Chr4 mutant; loss of function.
{ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:17803943,
ECO:0000269|PubMed:7721683}.
MUTAGEN 38 38 C->S: Loss of ability to bind zinc.
{ECO:0000269|PubMed:11676534,
ECO:0000269|PubMed:17803943,
ECO:0000269|PubMed:7721683}.
MUTAGEN 187 187 C->S: No effect on zinc binding.
{ECO:0000269|PubMed:11676534}.
MUTAGEN 189 189 C->S: No effect on zinc binding.
{ECO:0000269|PubMed:11676534}.
HELIX 9 17 {ECO:0000244|PDB:2Q1Z}.
HELIX 22 34 {ECO:0000244|PDB:2Q1Z}.
HELIX 36 54 {ECO:0000244|PDB:2Q1Z}.
HELIX 65 71 {ECO:0000244|PDB:2Q1Z}.
HELIX 94 98 {ECO:0000244|PDB:2Q1Z}.
HELIX 102 104 {ECO:0000244|PDB:2Z2S}.
STRAND 111 113 {ECO:0000244|PDB:2Q1Z}.
STRAND 115 119 {ECO:0000244|PDB:2Q1Z}.
STRAND 122 132 {ECO:0000244|PDB:2Q1Z}.
STRAND 147 157 {ECO:0000244|PDB:2Q1Z}.
STRAND 159 164 {ECO:0000244|PDB:2Q1Z}.
STRAND 168 171 {ECO:0000244|PDB:2Q1Z}.
STRAND 183 185 {ECO:0000244|PDB:2Q1Z}.
STRAND 187 193 {ECO:0000244|PDB:2Q1Z}.
SEQUENCE 213 AA; 22865 MW; 46152BC5858C845F CRC64;
MTIRHHVSDA LLTAYAAGTL SEAFSLVVAT HLSLCDECRA RAGALDAVGG SLMEETAPVA
LSEGSLASVM AQLDRQIQRP APARRADPRA PAPLADYVGR RLEDVRWRTL GGGVRQAILP
TGGEAIARLL WIPGGQAVPD HGHRGLELTL VLQGAFRDET DRFGAGDIEI ADQELEHTPV
AERGLDCICL AATDAPLRFN SFLPKLVQPF FRI


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Pathways :
WP654: ATM
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
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WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1963: The effect of Glucocorticoids on target gene expression
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2148: Brain derived neurotrophic factor
WP272: Blood Clotting Cascade
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor

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[rslA Rv0736] Anti-sigma-L factor RslA (Regulator of SigL) (Sigma-L anti-sigma factor RslA)
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[sigF Rv3286c] RNA polymerase sigma factor SigF (Sigma factor SigF) (Alternative RNA polymerase sigma factor SigF) (RNA polymerase sigma-F factor) (Sigma-F factor) (Stress response/stationary phase sigma factor SigF)
[rseA STM14_3233] Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA) (Sigma-E factor negative regulatory protein)
[rpoE RHOS4_27100 RSP_1092] ECF RNA polymerase sigma factor RpoE (Alternative RNA polymerase sigma factor RpoE) (RNA polymerase sigma-E factor) (Sigma-24)
[rshA Rv3221A] Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)
[SIGF SIG6 SOLDAT8 At2g36990 T1J8] RNA polymerase sigma factor sigF, chloroplastic (Sigma factor F) (Sigma-F) (Protein SINGLET OXYGEN-LINKED DEATH ACTIVATOR 8) (RNA polymerase sigma factor sig6) (Atsig6) (Sigma factor 6)
[rsbW usfX Rv3287c] Anti-sigma-F factor RsbW (Anti-sigma-F factor UsfX) (Regulator of SigF) (Sigma-F anti-sigma factor RsbW)
[sigR SCO5216] ECF RNA polymerase sigma factor SigR (ECF sigma factor SigR) (Alternative RNA polymerase sigma factor SigR) (RNA polymerase sigma-R factor) (Sigma-R factor)
[chrR yieF b3713 JW3691] Quinone reductase (EC 1.6.5.2) (Chromate reductase) (CHRR) (EC 1.6.-.-) (NAD(P)H dehydrogenase (quinone))
[sigC Rv2069 MTCY49.08] ECF RNA polymerase sigma factor SigC (ECF sigma factor SigC) (Alternative RNA polymerase sigma factor SigC) (RNA polymerase sigma-C factor) (Sigma-C factor)
[chrR PP_4138] Quinone reductase (EC 1.6.5.2) (Chromate reductase) (CHRR) (EC 1.6.-.-) (NAD(P)H dehydrogenase (quinone))
[GCN4 AAS3 ARG9 YEL009C] General control protein GCN4 (Amino acid biosynthesis regulatory protein)
[MPR1] N-acetyltransferase MPR1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Sigma1278b gene for proline-analog resistance 1)
[csfB gin yaaM BSU00240] Anti-sigma-G factor Gin (Protein CsfB)
[rpoE sigE STM14_3234] ECF RNA polymerase sigma-E factor (RNA polymerase sigma-E factor)
[FLO11 MAL5 MUC1 S1 S2 YIR019C] Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1)
[rpoS appR katF nur otsX sigS b2741 JW5437] RNA polymerase sigma factor RpoS (Sigma S) (Sigma-38)
[sigL Rv0735] ECF RNA polymerase sigma factor SigL (ECF sigma factor SigL) (Alternative RNA polymerase sigma factor SigL) (RNA polymerase sigma-L factor) (Sigma-L factor)
[rpoH fam hin htpR b3461 JW3426] RNA polymerase sigma factor RpoH (Heat shock regulatory protein F33.4) (RNA polymerase sigma-32 factor)
[sigM Rv3911] ECF RNA polymerase sigma factor SigM (ECF sigma factor SigM) (Alternative RNA polymerase sigma factor SigM) (RNA polymerase sigma-M factor) (Sigma-M factor)
[RSP5 MDP1 NPI1 YER125W SYGP-ORF41] E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase RSP5) (Reverses SPT-phenotype protein 5)
[sigW ybbL BSU01730] ECF RNA polymerase sigma factor SigW (ECF sigma factor SigW) (Alternative RNA polymerase sigma factor SigW) (RNA polymerase sigma-W factor) (Sigma-W factor)
[rshA MSMEG_1915 MSMEI_1875] Anti-sigma factor RshA (Regulator of SigH) (Sigma-H anti-sigma factor RshA)
[rseA MSMEG_5071 MSMEI_4944] Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA)
[sigH rpoE MSMEG_1914 MSMEI_1874] ECF RNA polymerase sigma factor SigH (ECF sigma factor SigH) (Alternative RNA polymerase sigma factor SigH) (RNA polymerase sigma-H factor) (Sigma-H factor)
[sigA mysA rpoD rpoV Rv2703 MTCY05A6.24] RNA polymerase sigma factor SigA (Sigma-A)
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