RSD_ECOLI
ID RSD_ECOLI Reviewed; 158 AA.
AC P0AFX4; P31690; Q2M8T2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Regulator of sigma D {ECO:0000255|HAMAP-Rule:MF_01181};
GN Name=rsd {ECO:0000255|HAMAP-Rule:MF_01181};
GN OrderedLocusNames=b3995, JW3959;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nishimura K., Inokuchi H.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (JUN-1993).
RN [6]
RP FUNCTION, AND INTERACTION WITH RPOD.
RX PubMed=9560209; DOI=10.1073/pnas.95.9.4953;
RA Jishage M., Ishihama A.;
RT "A stationary phase protein in Escherichia coli with binding activity to
RT the major sigma subunit of RNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4953-4958(1998).
RN [7]
RP FUNCTION.
RX PubMed=10368152; DOI=10.1128/jb.181.12.3768-3776.1999;
RA Jishage M., Ishihama A.;
RT "Transcriptional organization and in vivo role of the Escherichia coli rsd
RT gene, encoding the regulator of RNA polymerase sigma D.";
RL J. Bacteriol. 181:3768-3776(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH RPOD, AND SUBUNIT.
RX PubMed=17681541; DOI=10.1016/j.jmb.2007.06.081;
RA Patikoglou G.A., Westblade L.F., Campbell E.A., Lamour V., Lane W.J.,
RA Darst S.A.;
RT "Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in
RT complex with sigma70 domain 4.";
RL J. Mol. Biol. 372:649-659(2007).
CC -!- FUNCTION: Binds RpoD and negatively regulates RpoD-mediated
CC transcription activation by preventing the interaction between the
CC primary sigma factor RpoD with the catalytic core of the RNA polymerase
CC and with promoter DNA. May be involved in replacement of the RNA
CC polymerase sigma subunit from RpoD to RpoS during the transition from
CC exponential growth to the stationary phase. {ECO:0000255|HAMAP-
CC Rule:MF_01181, ECO:0000269|PubMed:10368152,
CC ECO:0000269|PubMed:9560209}.
CC -!- SUBUNIT: Interacts with RpoD. {ECO:0000255|HAMAP-Rule:MF_01181,
CC ECO:0000269|PubMed:17681541, ECO:0000269|PubMed:9560209}.
CC -!- INTERACTION:
CC P0AFX4; P00579: rpoD; NbExp=11; IntAct=EBI-1134364, EBI-545104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01181}.
CC -!- SIMILARITY: Belongs to the Rsd/AlgQ family. {ECO:0000255|HAMAP-
CC Rule:MF_01181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=D12624; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D12624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00006; AAC43093.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76969.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77324.1; -; Genomic_DNA.
DR PIR; F65206; F65206.
DR RefSeq; NP_418423.1; NC_000913.3.
DR RefSeq; WP_000934302.1; NZ_STEB01000045.1.
DR PDB; 2P7V; X-ray; 2.60 A; A=1-158.
DR PDB; 4XWJ; X-ray; 2.10 A; A=1-151.
DR PDBsum; 2P7V; -.
DR PDBsum; 4XWJ; -.
DR AlphaFoldDB; P0AFX4; -.
DR SMR; P0AFX4; -.
DR BioGRID; 4259334; 1.
DR BioGRID; 852790; 3.
DR ComplexPortal; CPX-4901; rpod-rsd sigma-antisigma complex.
DR DIP; DIP-10800N; -.
DR IntAct; P0AFX4; 8.
DR STRING; 511145.b3995; -.
DR jPOST; P0AFX4; -.
DR PaxDb; P0AFX4; -.
DR PRIDE; P0AFX4; -.
DR EnsemblBacteria; AAC76969; AAC76969; b3995.
DR EnsemblBacteria; BAE77324; BAE77324; BAE77324.
DR GeneID; 66672093; -.
DR GeneID; 948496; -.
DR KEGG; ecj:JW3959; -.
DR KEGG; eco:b3995; -.
DR PATRIC; fig|1411691.4.peg.2716; -.
DR EchoBASE; EB1689; -.
DR eggNOG; COG3160; Bacteria.
DR HOGENOM; CLU_142729_0_0_6; -.
DR InParanoid; P0AFX4; -.
DR OMA; DVIDHWL; -.
DR PhylomeDB; P0AFX4; -.
DR BioCyc; EcoCyc:EG11738-MON; -.
DR BioCyc; MetaCyc:EG11738-MON; -.
DR EvolutionaryTrace; P0AFX4; -.
DR PRO; PR:P0AFX4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1903865; C:sigma factor antagonist complex; IPI:ComplexPortal.
DR GO; GO:0001000; F:bacterial-type RNA polymerase core enzyme binding; IDA:EcoCyc.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IMP:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030813; P:positive regulation of nucleotide catabolic process; IDA:EcoCyc.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:EcoCyc.
DR Gene3D; 1.20.120.1370; -; 1.
DR HAMAP; MF_01181; Rsd; 1.
DR InterPro; IPR038309; Rsd/AlgQ_sf.
DR InterPro; IPR023785; Sigma70_reg_Rsd.
DR InterPro; IPR007448; Sigma70_reg_Rsd_AlgQ.
DR Pfam; PF04353; Rsd_AlgQ; 1.
DR PIRSF; PIRSF016548; Rsd_AlgQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..158
FT /note="Regulator of sigma D"
FT /id="PRO_0000097476"
FT REGION 59..71
FT /note="Interaction with RpoD"
FT REGION 101..108
FT /note="Interaction with RpoD"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 17..37
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 51..70
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 83..108
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:4XWJ"
FT HELIX 120..150
FT /evidence="ECO:0007829|PDB:4XWJ"
SQ SEQUENCE 158 AA; 18243 MW; BDB699DAC440A808 CRC64;
MLNQLDNLTE RVRGSNKLVD RWLHVRKHLL VAYYNLVGIK PGKESYMRLN EKALDDFCQS
LVDYLSAGHF SIYERILHKL EGNGQLARAA KIWPQLEANT QQIMDYYDSS LETAIDHDNY
LEFQQVLSDI GEALEARFVL EDKLILLVLD AARVKHPA
