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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.
07-JUN-2017, entry version 99.
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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EMBL; U11283; AAB17905.1; -; Genomic_DNA.
EMBL; CP000143; ABA80279.1; -; Genomic_DNA.
PIR; B58883; B58883.
RefSeq; WP_011338712.1; NZ_AKVW01000001.1.
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; CICLAVT; -.
OrthoDB; POG091H03V3; -.
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.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; 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.
InterPro; IPR027383; Znf_put.
Pfam; PF12973; Cupin_7; 1.
Pfam; PF13490; zf-HC2; 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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