CHRR_CERS4
ID CHRR_CERS4 Reviewed; 213 AA.
AC P40685; Q3IYV5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Anti-sigma-E factor ChrR;
DE AltName: Full=Sigma-E anti-sigma factor ChrR;
DE AltName: Full=Transcriptional activator ChrR;
GN Name=chrR; OrderedLocusNames=RHOS4_27110; ORFNames=RSP_1093;
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], AND MUTAGENESIS OF CYS-38.
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 SEQUENCE REVISION.
RA Newman J., Donohue T.J.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=10610760; DOI=10.1006/jmbi.1999.3263;
RA Newman J.D., Falkowski M.J., Schilke B.A., Anthony L.C., Donohue T.J.;
RT "The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the target
RT promoters cycA P3 and rpoE P1.";
RL J. Mol. Biol. 294:307-320(1999).
RN [5]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, COFACTOR, INTERACTION WITH SIGME-E
RP (RPOE), SUBUNIT, AND MUTAGENESIS OF CYS-35; CYS-38; CYS-187 AND CYS-189.
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 [6]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-195, FUNCTION AS AN ANTI-SIGMA
RP FACTOR, ZINC-BINDING, INTERACTION WITH RPOE, INDUCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF HIS-5; HIS-6; HIS-31; CYS-35 AND CYS-38.
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: Anti-sigma factor that inhibits the activity of the
CC extracytoplasmic function (ECF) sigma-E factor (RpoE), thereby
CC indirectly regulating the transcription of the cycA and rpoE genes. ECF
CC sigma factors are held in an inactive form by a cognate anti-sigma
CC factor. {ECO:0000269|PubMed:11676534, ECO:0000269|PubMed:15855269,
CC ECO:0000269|PubMed:17803943}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11676534};
CC Note=Binds 2 Zn(2+) ion per subunit. The Zn(2+) bound by the N-terminus
CC is required for anti-sigma function, the function of the Zn(2+) bound
CC by the C-terminus is unknown. {ECO:0000269|PubMed:11676534};
CC -!- SUBUNIT: Forms a 1:1 complex with cognate ECF RNA polymerase sigma
CC factor RpoE; this inhibits the interaction of RpoE with the RNA
CC polymerase catalytic core. {ECO:0000269|PubMed:11676534}.
CC -!- INDUCTION: Induced by singlet oxygen. Autoregulated. Part of the rpoE-
CC chrR operon. {ECO:0000269|PubMed:17803943}.
CC -!- DOMAIN: The N-terminal anti-sigma domain (residues 1-85) is necessary
CC and sufficient to bind sigma-E and inhibit its activity. The C-terminal
CC domain (residues 86-194) is required to respond to singlet oxygen
CC (PubMed:17803943). {ECO:0000269|PubMed:17803943}.
CC -!- DISRUPTION PHENOTYPE: For single chrR mutant about 12-fold increase in
CC rpoE-regulated genes. For double rpoE-chrR deletion mutant no effect on
CC anaerobic photosynthetic growth. In illuminated aerobically growing
CC cells double deletion is bacteriostatic. {ECO:0000269|PubMed:15855269,
CC ECO:0000269|PubMed:17803943}.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
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DR EMBL; U11283; AAB17905.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA80279.1; -; Genomic_DNA.
DR PIR; B58883; B58883.
DR RefSeq; WP_011338712.1; NZ_CP030271.1.
DR RefSeq; YP_354180.1; NC_007493.2.
DR PDB; 2Q1Z; X-ray; 2.40 A; B/D=1-195.
DR PDB; 2Z2S; X-ray; 2.70 A; B/D/F/H=1-203.
DR PDBsum; 2Q1Z; -.
DR PDBsum; 2Z2S; -.
DR AlphaFoldDB; P40685; -.
DR SMR; P40685; -.
DR STRING; 272943.RSP_1093; -.
DR EnsemblBacteria; ABA80279; ABA80279; RSP_1093.
DR KEGG; rsp:RSP_1093; -.
DR PATRIC; fig|272943.9.peg.3072; -.
DR eggNOG; COG3806; Bacteria.
DR OMA; PLHFTSG; -.
DR PhylomeDB; P40685; -.
DR EvolutionaryTrace; P40685; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20301; cupin_ChrR; 1.
DR Gene3D; 1.10.10.1320; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR012807; Anti-sigma_ChrR.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
DR InterPro; IPR025979; ChrR-like_cupin_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF12973; Cupin_7; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR02451; anti_sig_ChrR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; DNA-binding;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10610760"
FT CHAIN 2..213
FT /note="Anti-sigma-E factor ChrR"
FT /id="PRO_0000089658"
FT REGION 2..85
FT /note="Sufficient to bind sigma factor and inhibit its
FT activity"
FT REGION 86..194
FT /note="Required for response to singlet oxygen"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT MUTAGEN 5
FT /note="H->A: No effect on anti-sigma function."
FT /evidence="ECO:0000269|PubMed:17803943"
FT MUTAGEN 6
FT /note="H->A: Loss of anti-sigma function."
FT /evidence="ECO:0000269|PubMed:17803943"
FT MUTAGEN 31
FT /note="H->A: No effect on anti-sigma function."
FT /evidence="ECO:0000269|PubMed:17803943"
FT MUTAGEN 35
FT /note="C->A: Loss of anti-sigma function."
FT /evidence="ECO:0000269|PubMed:11676534,
FT ECO:0000269|PubMed:17803943"
FT MUTAGEN 35
FT /note="C->S: Loss of function; no effect on zinc binding."
FT /evidence="ECO:0000269|PubMed:11676534,
FT ECO:0000269|PubMed:17803943"
FT MUTAGEN 38
FT /note="C->A: Loss of anti-sigma function."
FT /evidence="ECO:0000269|PubMed:11676534,
FT ECO:0000269|PubMed:17803943, ECO:0000269|PubMed:7721683"
FT MUTAGEN 38
FT /note="C->R: In Chr4 mutant; loss of function."
FT /evidence="ECO:0000269|PubMed:11676534,
FT ECO:0000269|PubMed:17803943, ECO:0000269|PubMed:7721683"
FT MUTAGEN 38
FT /note="C->S: Loss of ability to bind zinc."
FT /evidence="ECO:0000269|PubMed:11676534,
FT ECO:0000269|PubMed:17803943, ECO:0000269|PubMed:7721683"
FT MUTAGEN 187
FT /note="C->S: No effect on zinc binding."
FT /evidence="ECO:0000269|PubMed:11676534"
FT MUTAGEN 189
FT /note="C->S: No effect on zinc binding."
FT /evidence="ECO:0000269|PubMed:11676534"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2Z2S"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2Q1Z"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2Q1Z"
SQ 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
