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Protein

Anti-sigma-E factor ChrR

Gene

chrR

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ion per subunit. The Zn2+ bound by the N-terminus is required for anti-sigma function, the function of the Zn2+ bound by the C-terminus is unknown.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61Zinc 1; via pros nitrogen
Metal bindingi31 – 311Zinc 1; via tele nitrogen
Metal bindingi35 – 351Zinc 1
Metal bindingi38 – 381Zinc 1
Metal bindingi141 – 1411Zinc 2; via pros nitrogen
Metal bindingi143 – 1431Zinc 2; via tele nitrogen
Metal bindingi147 – 1471Zinc 2
Metal bindingi177 – 1771Zinc 2; via tele nitrogen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciRSPH272943:GJAS-2775-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Anti-sigma-E factor ChrR
Alternative name(s):
Sigma-E anti-sigma factor ChrR
Transcriptional activator ChrR
Gene namesi
Name:chrR
Ordered Locus Names:RHOS4_27110
ORF Names:RSP_1093
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Chromosome 1

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51H → A: No effect on anti-sigma function. 1 Publication
Mutagenesisi6 – 61H → A: Loss of anti-sigma function. 1 Publication
Mutagenesisi31 – 311H → A: No effect on anti-sigma function. 1 Publication
Mutagenesisi35 – 351C → A: Loss of anti-sigma function. 2 Publications
Mutagenesisi35 – 351C → S: Loss of function; no effect on zinc binding. 2 Publications
Mutagenesisi38 – 381C → A: Loss of anti-sigma function. 3 Publications
Mutagenesisi38 – 381C → R in Chr4 mutant; loss of function. 3 Publications
Mutagenesisi38 – 381C → S: Loss of ability to bind zinc. 3 Publications
Mutagenesisi187 – 1871C → S: No effect on zinc binding. 1 Publication
Mutagenesisi189 – 1891C → S: No effect on zinc binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 213212Anti-sigma-E factor ChrRPRO_0000089658Add
BLAST

Expressioni

Inductioni

Induced by singlet oxygen. Autoregulated. Part of the rpoE-chrR operon.1 Publication

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

STRINGi272943.RSP_1093.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179Combined sources
Helixi22 – 3413Combined sources
Helixi36 – 5419Combined sources
Helixi65 – 717Combined sources
Helixi94 – 985Combined sources
Helixi102 – 1043Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi122 – 13211Combined sources
Beta strandi147 – 15711Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi187 – 1937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q1ZX-ray2.40B/D1-195[»]
2Z2SX-ray2.70B/D/F/H1-203[»]
ProteinModelPortaliP40685.
SMRiP40685. Positions 2-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40685.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8584Sufficient to bind sigma factor and inhibit its activityAdd
BLAST
Regioni86 – 194109Required for response to singlet oxygenAdd
BLAST

Domaini

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).1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108NIX. Bacteria.
COG3806. LUCA.
HOGENOMiHOG000284569.
KOiK07167.
OMAiCICLAAT.
OrthoDBiEOG67Q99D.
PhylomeDBiP40685.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012807. Anti-sigma_ChrR.
IPR025979. ChrR-like_cupin_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF12973. Cupin_7. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR02451. anti_sig_ChrR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIRHHVSDA LLTAYAAGTL SEAFSLVVAT HLSLCDECRA RAGALDAVGG
60 70 80 90 100
SLMEETAPVA LSEGSLASVM AQLDRQIQRP APARRADPRA PAPLADYVGR
110 120 130 140 150
RLEDVRWRTL GGGVRQAILP TGGEAIARLL WIPGGQAVPD HGHRGLELTL
160 170 180 190 200
VLQGAFRDET DRFGAGDIEI ADQELEHTPV AERGLDCICL AATDAPLRFN
210
SFLPKLVQPF FRI
Length:213
Mass (Da):22,865
Last modified:January 23, 2007 - v4
Checksum:i46152BC5858C845F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11283 Genomic DNA. Translation: AAB17905.1.
CP000143 Genomic DNA. Translation: ABA80279.1.
PIRiB58883.
RefSeqiWP_011338712.1. NZ_AKVW01000001.1.
YP_354180.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA80279; ABA80279; RSP_1093.
GeneIDi3720852.
KEGGirsp:RSP_1093.
PATRICi23155413. VBIRhoSph57909_3072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11283 Genomic DNA. Translation: AAB17905.1.
CP000143 Genomic DNA. Translation: ABA80279.1.
PIRiB58883.
RefSeqiWP_011338712.1. NZ_AKVW01000001.1.
YP_354180.1. NC_007493.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q1ZX-ray2.40B/D1-195[»]
2Z2SX-ray2.70B/D/F/H1-203[»]
ProteinModelPortaliP40685.
SMRiP40685. Positions 2-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_1093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA80279; ABA80279; RSP_1093.
GeneIDi3720852.
KEGGirsp:RSP_1093.
PATRICi23155413. VBIRhoSph57909_3072.

Phylogenomic databases

eggNOGiENOG4108NIX. Bacteria.
COG3806. LUCA.
HOGENOMiHOG000284569.
KOiK07167.
OMAiCICLAAT.
OrthoDBiEOG67Q99D.
PhylomeDBiP40685.

Enzyme and pathway databases

BioCyciRSPH272943:GJAS-2775-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40685.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR012807. Anti-sigma_ChrR.
IPR025979. ChrR-like_cupin_dom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF12973. Cupin_7. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR02451. anti_sig_ChrR. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ChrR positively regulates transcription of the Rhodobacter sphaeroides cytochrome c2 gene."
    Schilke B.A., Donohue T.J.
    J. Bacteriol. 177:1929-1937(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF CYS-38.
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
  2. Newman J., Donohue T.J.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
    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.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
  4. "The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the target promoters cycA P3 and rpoE P1."
    Newman J.D., Falkowski M.J., Schilke B.A., Anthony L.C., Donohue T.J.
    J. Mol. Biol. 294:307-320(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
  5. "The importance of zinc-binding to the function of Rhodobacter sphaeroides ChrR as an anti-sigma factor."
    Newman J.D., Anthony J.R., Donohue T.J.
    J. Mol. Biol. 313:485-499(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTI-SIGMA FACTOR, COFACTOR, INTERACTION WITH SIGME-E (RPOE), SUBUNIT, MUTAGENESIS OF CYS-35; CYS-38; CYS-187 AND CYS-189.
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
  6. "A transcriptional response to singlet oxygen, a toxic byproduct of photosynthesis."
    Anthony J.R., Warczak K.L., Donohue T.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:6502-6507(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTI-SIGMA FACTOR, DISRUPTION PHENOTYPE.
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
  7. "A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria."
    Campbell E.A., Greenwell R., Anthony J.R., Wang S., Lim L., Das K., Sofia H.J., Donohue T.J., Darst S.A.
    Mol. Cell 27:793-805(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-195, FUNCTION AS AN ANTI-SIGMA FACTOR, ZINC-BINDING, INTERACTION WITH RPOE, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-5; HIS-6; HIS-31; CYS-35 AND CYS-38.
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Entry informationi

Entry nameiCHRR_RHOS4
AccessioniPrimary (citable) accession number: P40685
Secondary accession number(s): Q3IYV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 11, 2015
This is version 93 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.