RPOE_CERS4
ID RPOE_CERS4 Reviewed; 181 AA.
AC Q3IYV6; O33546;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=ECF RNA polymerase sigma factor RpoE;
DE AltName: Full=Alternative RNA polymerase sigma factor RpoE;
DE AltName: Full=RNA polymerase sigma-E factor;
DE AltName: Full=Sigma-24;
GN Name=rpoE; OrderedLocusNames=RHOS4_27100; ORFNames=RSP_1092;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=7721683; DOI=10.1128/jb.177.8.1929-1937.1995;
RA Schilke B.A., Donohue T.J.;
RT "ChrR positively regulates transcription of the Rhodobacter sphaeroides
RT cytochrome c2 gene.";
RL J. Bacteriol. 177:1929-1937(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION AS A SIGMA FACTOR, INTERACTION WITH CHRR, AND SUBUNIT.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=11676534; DOI=10.1006/jmbi.2001.5069;
RA Newman J.D., Anthony J.R., Donohue T.J.;
RT "The importance of zinc-binding to the function of Rhodobacter sphaeroides
RT ChrR as an anti-sigma factor.";
RL J. Mol. Biol. 313:485-499(2001).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=15855269; DOI=10.1073/pnas.0502225102;
RA Anthony J.R., Warczak K.L., Donohue T.J.;
RT "A transcriptional response to singlet oxygen, a toxic byproduct of
RT photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6502-6507(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), FUNCTION AS A SIGMA FACTOR,
RP INTERACTION WITH CHRR, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=17803943; DOI=10.1016/j.molcel.2007.07.009;
RA Campbell E.A., Greenwell R., Anthony J.R., Wang S., Lim L., Das K.,
RA Sofia H.J., Donohue T.J., Darst S.A.;
RT "A conserved structural module regulates transcriptional responses to
RT diverse stress signals in bacteria.";
RL Mol. Cell 27:793-805(2007).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. Extracytoplasmic function (ECF) sigma factors are held in an
CC inactive form by a cognate anti-sigma factor until released. Sigma-E
CC controls a transcriptional response to singlet oxygen, a by-product of
CC photosynthesis; its continuous activity requires constant exposure to
CC singlet oxygen. The regulon has about 180 genes that protect against or
CC repair damage induced by singlet oxygen, including itself and rpoH2, a
CC heat shock-responsive sigma factor. {ECO:0000269|PubMed:11676534,
CC ECO:0000269|PubMed:15855269, ECO:0000269|PubMed:17803943}.
CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core
CC formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1
CC omega subunit) to form the RNA polymerase holoenzyme that can initiate
CC transcription. Forms a 1:1 complex (via sigma-70 factor domain 4) with
CC anti-sigma factor ChrR; this inhibits the interaction of RpoE with the
CC RNA polymerase catalytic core. {ECO:0000269|PubMed:11676534,
CC ECO:0000269|PubMed:17803943}.
CC -!- INDUCTION: Induced under conditions that produce singlet oxygen (shift
CC from anaerobic photosynthetic to aerobic growth in light). Not induced
CC by H(2)O(2), paraquat (stimulates superoxide formation) or diamide
CC (alters the thiol redox state). Autoregulated. Part of the rpoE-chrR
CC operon. {ECO:0000269|PubMed:15855269, ECO:0000269|PubMed:17803943}.
CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC interaction with the -10 element in promoter DNA, and plays an
CC important role in melting the double-stranded DNA and the formation of
CC the transcription bubble. The sigma-70 factor domain-2 mediates
CC interaction with the RNA polymerase subunits RpoB and RpoC (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC H) motif that mediates interaction with the -35 element in promoter
CC DNA. The domain also mediates interaction with the RNA polymerase
CC subunit RpoA (By similarity). Interactions between Sigma-70 factor
CC domain-4 and anti-sigma factors prevents interaction of sigma factors
CC with the RNA polymerase catalytic core (PubMed:17803943) (Probable).
CC {ECO:0000250, ECO:0000269|PubMed:17803943, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: For single rpoE mutant increased sensitivity to
CC singlet oxygen when carotenoid levels are low. For double rpoE-chrR
CC deletion mutant no effect on anaerobic photosynthetic growth. In
CC illuminated aerobically growing cells single and double deletion is
CC bacteriostatic. {ECO:0000269|PubMed:15855269,
CC ECO:0000269|PubMed:17803943}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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DR EMBL; U11283; AAB17906.2; -; Genomic_DNA.
DR EMBL; CP000143; ABA80278.1; -; Genomic_DNA.
DR PIR; A58883; A58883.
DR RefSeq; WP_011338711.1; NZ_AKVW01000001.1.
DR RefSeq; YP_354179.1; NC_007493.2.
DR PDB; 2Q1Z; X-ray; 2.40 A; A/C=1-181.
DR PDB; 2Z2S; X-ray; 2.70 A; A/C/E/G=1-181.
DR PDBsum; 2Q1Z; -.
DR PDBsum; 2Z2S; -.
DR AlphaFoldDB; Q3IYV6; -.
DR SMR; Q3IYV6; -.
DR STRING; 272943.RSP_1092; -.
DR EnsemblBacteria; ABA80278; ABA80278; RSP_1092.
DR KEGG; rsp:RSP_1092; -.
DR PATRIC; fig|272943.9.peg.3071; -.
DR eggNOG; COG1595; Bacteria.
DR OMA; AWRHPEV; -.
DR PhylomeDB; Q3IYV6; -.
DR EvolutionaryTrace; Q3IYV6; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..181
FT /note="ECF RNA polymerase sigma factor RpoE"
FT /id="PRO_0000422739"
FT DNA_BIND 151..170
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 29..96
FT /note="Sigma-70 factor domain-2"
FT REGION 129..178
FT /note="Sigma-70 factor domain-4"
FT MOTIF 53..56
FT /note="Interaction with polymerase core subunit RpoC"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 23..43
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 113..131
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:2Q1Z"
SQ SEQUENCE 181 AA; 20703 MW; E00259EB530A7008 CRC64;
MTDKSDRTDW VALMRAIRDH RDEAAFAELF QHFAPKVKGF LMKSGSVASQ AEECAQDVMA
TVWQKAHLFD PSRASVATWI FTIARNRRID GLRKDRQPEP EDLFWGPDSE PDQADVYEMQ
QENARLGRAI ARLPEAQRAL IERAFFGDLT HRELAAETGL PLGTIKSRIR LALDRLRQHM
S
