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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)DescriptionActionsGraphical viewLength
Metal bindingi6Zinc 1; via pros nitrogen1
Metal bindingi31Zinc 1; via tele nitrogen1
Metal bindingi35Zinc 11
Metal bindingi38Zinc 11
Metal bindingi141Zinc 2; via pros nitrogen1
Metal bindingi143Zinc 2; via tele nitrogen1
Metal bindingi147Zinc 21
Metal bindingi177Zinc 2; via tele nitrogen1

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi5H → A: No effect on anti-sigma function. 1 Publication1
Mutagenesisi6H → A: Loss of anti-sigma function. 1 Publication1
Mutagenesisi31H → A: No effect on anti-sigma function. 1 Publication1
Mutagenesisi35C → A: Loss of anti-sigma function. 2 Publications1
Mutagenesisi35C → S: Loss of function; no effect on zinc binding. 2 Publications1
Mutagenesisi38C → A: Loss of anti-sigma function. 3 Publications1
Mutagenesisi38C → R in Chr4 mutant; loss of function. 3 Publications1
Mutagenesisi38C → S: Loss of ability to bind zinc. 3 Publications1
Mutagenesisi187C → S: No effect on zinc binding. 1 Publication1
Mutagenesisi189C → S: No effect on zinc binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000896582 – 213Anti-sigma-E factor ChrRAdd BLAST212

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

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 17Combined sources9
Helixi22 – 34Combined sources13
Helixi36 – 54Combined sources19
Helixi65 – 71Combined sources7
Helixi94 – 98Combined sources5
Helixi102 – 104Combined sources3
Beta strandi111 – 113Combined sources3
Beta strandi115 – 119Combined sources5
Beta strandi122 – 132Combined sources11
Beta strandi147 – 157Combined sources11
Beta strandi159 – 164Combined sources6
Beta strandi168 – 171Combined sources4
Beta strandi183 – 185Combined sources3
Beta strandi187 – 193Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP40685.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 85Sufficient to bind sigma factor and inhibit its activityAdd BLAST84
Regioni86 – 194Required for response to singlet oxygenAdd BLAST109

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.
OMAiGDFIWLD.
OrthoDBiPOG091H03V3.
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.
IPR027383. Znf_put.
[Graphical view]
PfamiPF12973. Cupin_7. 1 hit.
PF13490. zf-HC2. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q1ZX-ray2.40B/D1-195[»]
2Z2SX-ray2.70B/D/F/H1-203[»]
ProteinModelPortaliP40685.
SMRiP40685.
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.
OMAiGDFIWLD.
OrthoDBiPOG091H03V3.
PhylomeDBiP40685.

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.
IPR027383. Znf_put.
[Graphical view]
PfamiPF12973. Cupin_7. 1 hit.
PF13490. zf-HC2. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR02451. anti_sig_ChrR. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 96 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.