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Regulator of RpoS

 RSSB_ECOLI              Reviewed;         337 AA.
P0AEV1; P37055;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 95.
RecName: Full=Regulator of RpoS {ECO:0000255|HAMAP-Rule:MF_00958};
Name=rssB {ECO:0000255|HAMAP-Rule:MF_00958}; Synonyms=hnr, sprE, ychL;
OrderedLocusNames=b1235, JW1223;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Contreras A.;
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8282700; DOI=10.1128/jb.176.1.221-231.1994;
Boesl M., Kersten H.;
"Organization and functions of genes in the upstream region of tyrT of
Escherichia coli: phenotypes of mutants with partial deletion of a new
gene (tgs).";
J. Bacteriol. 176:221-231(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8635466;
Muffler A., Fischer D., Altuvia S., Storz G., Hengge-Aronis R.;
"The response regulator RssB controls stability of the sigma(S)
subunit of RNA polymerase in Escherichia coli.";
EMBO J. 15:1333-1339(1996).
[7]
FUNCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8637901; DOI=10.1073/pnas.93.6.2488;
Pratt L.A., Silhavy T.J.;
"The response regulator SprE controls the stability of RpoS.";
Proc. Natl. Acad. Sci. U.S.A. 93:2488-2492(1996).
[8]
PHOSPHORYLATION AT ASP-58, AND MUTAGENESIS OF ASP-58.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9515704; DOI=10.1046/j.1365-2958.1998.00725.x;
Bouche S., Klauck E., Fischer D., Lucassen M., Jung K.,
Hengge-Aronis R.;
"Regulation of RssB-dependent proteolysis in Escherichia coli: a role
for acetyl phosphate in a response regulator-controlled process.";
Mol. Microbiol. 27:787-795(1998).
[9]
INTERACTION WITH RPOS, AND PHOSPHORYLATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10339606; DOI=10.1073/pnas.96.11.6439;
Becker G., Klauck E., Hengge-Aronis R.;
"Regulation of RpoS proteolysis in Escherichia coli: the response
regulator RssB is a recognition factor that interacts with the
turnover element in RpoS.";
Proc. Natl. Acad. Sci. U.S.A. 96:6439-6444(1999).
[10]
INDUCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10869095; DOI=10.1128/JB.182.14.4117-4120.2000;
Gibson K.E., Silhavy T.J.;
"SprE levels are growth phase regulated in a sigma(S)-dependent manner
at the level of translation.";
J. Bacteriol. 182:4117-4120(2000).
[11]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH RPOS.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10672187; DOI=10.1046/j.1365-2958.2000.01736.x;
Becker G., Klauck E., Hengge-Aronis R.;
"The response regulator RssB, a recognition factor for sigmaS
proteolysis in Escherichia coli, can act like an anti-sigmaS factor.";
Mol. Microbiol. 35:657-666(2000).
[12]
FUNCTION, INTERACTION WITH RPOS, DOMAIN, PHOSPHORYLATION, AND
MUTAGENESIS OF ASP-58.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11442836; DOI=10.1046/j.1365-2958.2001.02482.x;
Klauck E., Lingnau M., Hengge-Aronis R.;
"Role of the response regulator RssB in sigma recognition and
initiation of sigma proteolysis in Escherichia coli.";
Mol. Microbiol. 40:1381-1390(2001).
[13]
ENZYME REGULATION, AND INTERACTION WITH IRAP.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=16600914; DOI=10.1101/gad.1400306;
Bougdour A., Wickner S., Gottesman S.;
"Modulating RssB activity: IraP, a novel regulator of sigma(S)
stability in Escherichia coli.";
Genes Dev. 20:884-897(2006).
[14]
ENZYME REGULATION, AND INTERACTION WITH IRAD AND IRAM.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=18383615; DOI=10.1111/j.1365-2958.2008.06146.x;
Bougdour A., Cunning C., Baptiste P.J., Elliott T., Gottesman S.;
"Multiple pathways for regulation of sigmaS (RpoS) stability in
Escherichia coli via the action of multiple anti-adaptors.";
Mol. Microbiol. 68:298-313(2008).
[15]
FUNCTION IN POLYADENYLATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=19767441; DOI=10.1128/JB.00870-09;
Carabetta V.J., Mohanty B.K., Kushner S.R., Silhavy T.J.;
"The response regulator SprE (RssB) modulates polyadenylation and mRNA
stability in Escherichia coli.";
J. Bacteriol. 191:6812-6821(2009).
[16]
FUNCTION IN POLYADENYLATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20472786; DOI=10.1128/JB.00300-10;
Carabetta V.J., Silhavy T.J., Cristea I.M.;
"The response regulator SprE (RssB) is required for maintaining
poly(A) polymerase I-degradosome association during stationary
phase.";
J. Bacteriol. 192:3713-3721(2010).
[17]
ENZYME REGULATION, INTERACTION WITH IRAP; IRAD AND IRAM, DOMAIN,
PHOSPHORYLATION, AND MUTAGENESIS OF ASP-58; LEU-67; PRO-109; TRP-143;
LEU-214; ALA-216; LEU-218 AND ALA-255.
PubMed=24352426; DOI=10.1101/gad.229617.113;
Battesti A., Hoskins J.R., Tong S., Milanesio P., Mann J.M.,
Kravats A., Tsegaye Y.M., Bougdour A., Wickner S., Gottesman S.;
"Anti-adaptors provide multiple modes for regulation of the RssB
adaptor protein.";
Genes Dev. 27:2722-2735(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-130.
Levchenko I., Grant R.A., Sauer R.T., Baker T.A.;
"The structure of RssB, a ClpX adaptor protein that regulates sigma
S.";
Submitted (SEP-2008) to the PDB data bank.
-!- FUNCTION: Regulates the turnover of the sigma S factor (RpoS) by
promoting its proteolysis in exponentially growing cells. Acts by
binding and delivering RpoS to the ClpXP protease. RssB is not co-
degraded with RpoS, but is released from the complex and can
initiate a new cycle of RpoS recognition and degradation. In
stationary phase, could also act as an anti-sigma factor and
reduce the ability of RpoS to activate gene expression. Is also
involved in the regulation of the mRNA polyadenylation pathway
during stationary phase, probably by maintaining the association
of PcnB with the degradosome. {ECO:0000255|HAMAP-Rule:MF_00958,
ECO:0000269|PubMed:10672187, ECO:0000269|PubMed:11442836,
ECO:0000269|PubMed:19767441, ECO:0000269|PubMed:20472786,
ECO:0000269|PubMed:8635466, ECO:0000269|PubMed:8637901}.
-!- ENZYME REGULATION: Under certain stress conditions, activity is
inhibited by the anti-adapter proteins IraP, IraD and IraM. IraP
is involved in response to phosphate stavation, IraD in response
to DNA damage and IraM in response to magnesium starvation. IraD
and IraM interact with inactive RssB, blocking its ability to
interact with RpoS. IraP may mimic RpoS in its interaction with
RssB and directly competing with RpoS for binding to RssB.
{ECO:0000269|PubMed:16600914, ECO:0000269|PubMed:18383615,
ECO:0000269|PubMed:24352426}.
-!- SUBUNIT: Binds to RpoS with a stoichiometry of 1:1. Interacts with
the anti-adapter proteins IraP, IraD and IraM. {ECO:0000255|HAMAP-
Rule:MF_00958, ECO:0000269|PubMed:10339606,
ECO:0000269|PubMed:10672187, ECO:0000269|PubMed:11442836,
ECO:0000269|PubMed:16600914, ECO:0000269|PubMed:18383615,
ECO:0000269|PubMed:24352426}.
-!- INDUCTION: Expression is induced during stationary phase by RpoS.
{ECO:0000269|PubMed:10869095}.
-!- DOMAIN: Contains an N-terminal receiver domain and a C-terminal
output domain that are both required for binding to RpoS. IraP and
IraD interact with the N-terminal domain. IraM interacts with the
C-terminal domain and, more weakly, the N-terminal domain.
{ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426}.
-!- PTM: Phosphorylated. Phosphorylation stimulates the interaction
with RpoS and, therefore, the proteolysis of RpoS.
{ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:10339606,
ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426,
ECO:0000269|PubMed:9515704}.
-!- DISRUPTION PHENOTYPE: Mutants exhibit nearly constitutively high
levels of RpoS and are impaired in the post-transcriptional growth
phase-related and osmotic regulation of RpoS. In exponentially
growing cells, mutants exhibit significantly reduced levels of
polyadenylation and increased stability of specific mRNAs.
{ECO:0000269|PubMed:19767441, ECO:0000269|PubMed:8635466}.
-!- SIMILARITY: Belongs to the RssB family. {ECO:0000255|HAMAP-
Rule:MF_00958}.
-----------------------------------------------------------------------
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EMBL; X66003; CAA46802.1; -; Genomic_DNA.
EMBL; M64675; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
EMBL; U00096; AAC74317.1; -; Genomic_DNA.
EMBL; AP009048; BAA36103.1; -; Genomic_DNA.
PIR; A36871; A36871.
RefSeq; NP_415751.1; NC_000913.3.
RefSeq; WP_000193447.1; NZ_LN832404.1.
PDB; 3EOD; X-ray; 1.75 A; A=1-130.
PDBsum; 3EOD; -.
ProteinModelPortal; P0AEV1; -.
SMR; P0AEV1; -.
BioGrid; 4261926; 3.
IntAct; P0AEV1; 4.
STRING; 316385.ECDH10B_1295; -.
PaxDb; P0AEV1; -.
PRIDE; P0AEV1; -.
EnsemblBacteria; AAC74317; AAC74317; b1235.
EnsemblBacteria; BAA36103; BAA36103; BAA36103.
GeneID; 945855; -.
KEGG; ecj:JW1223; -.
KEGG; eco:b1235; -.
PATRIC; fig|1411691.4.peg.1050; -.
EchoBASE; EB2042; -.
EcoGene; EG12121; rssB.
eggNOG; ENOG4105I93; Bacteria.
eggNOG; COG0784; LUCA.
HOGENOM; HOG000119811; -.
InParanoid; P0AEV1; -.
KO; K02485; -.
OMA; HWHLEYL; -.
PhylomeDB; P0AEV1; -.
BioCyc; EcoCyc:EG12121-MONOMER; -.
EvolutionaryTrace; P0AEV1; -.
PRO; PR:P0AEV1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:EcoCyc.
GO; GO:0031648; P:protein destabilization; IMP:EcoCyc.
CDD; cd00156; REC; 1.
Gene3D; 3.60.40.10; -; 1.
HAMAP; MF_00958; RssB; 1.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR028616; RssB.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
Pfam; PF00072; Response_reg; 1.
SMART; SM00448; REC; 1.
SUPFAM; SSF52172; SSF52172; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
Stress response.
CHAIN 1 337 Regulator of RpoS.
/FTId=PRO_0000081388.
DOMAIN 9 123 Response regulatory.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
MOD_RES 58 58 4-aspartylphosphate. {ECO:0000255|HAMAP-
Rule:MF_00958,
ECO:0000269|PubMed:9515704}.
MUTAGEN 58 58 D->P,Q,R: Lack of phosphorylation. Cannot
bind RpoS. {ECO:0000269|PubMed:11442836,
ECO:0000269|PubMed:24352426,
ECO:0000269|PubMed:9515704}.
MUTAGEN 67 67 L->A: Lack of phosphorylation.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 109 109 P->S: Resistant to IraP but not to IraD.
Increases stabilization by IraM.
Decreases phosphorylation.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 143 143 W->R: Resistant to both IraP and IraD.
Increases stabilization by IraM.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 214 214 L->H: Resistant to IraP and IraD.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 216 216 A->T: Resistant to IraP, IraD and IraM.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 218 218 L->V: Resistant to IraP, IraD and IraM.
{ECO:0000269|PubMed:24352426}.
MUTAGEN 255 255 A->V: Resistant to IraM.
{ECO:0000269|PubMed:24352426}.
TURN 4 7 {ECO:0000244|PDB:3EOD}.
STRAND 9 13 {ECO:0000244|PDB:3EOD}.
HELIX 17 29 {ECO:0000244|PDB:3EOD}.
STRAND 33 38 {ECO:0000244|PDB:3EOD}.
HELIX 40 47 {ECO:0000244|PDB:3EOD}.
STRAND 53 57 {ECO:0000244|PDB:3EOD}.
HELIX 67 75 {ECO:0000244|PDB:3EOD}.
STRAND 82 86 {ECO:0000244|PDB:3EOD}.
HELIX 91 100 {ECO:0000244|PDB:3EOD}.
STRAND 103 108 {ECO:0000244|PDB:3EOD}.
HELIX 115 124 {ECO:0000244|PDB:3EOD}.
SEQUENCE 337 AA; 37302 MW; AB962EF94BC7B470 CRC64;
MTQPLVGKQI LIVEDEQVFR SLLDSWFSSL GATTVLAADG VDALELLGGF TPDLMICDIA
MPRMNGLKLL EHIRNRGDQT PVLVISATEN MADIAKALRL GVEDVLLKPV KDLNRLREMV
FACLYPSMFN SRVEEEERLF RDWDAMVDNP AAAAKLLQEL QPPVQQVISH CRVNYRQLVA
ADKPGLVLDI AALSENDLAF YCLDVTRAGH NGVLAALLLR ALFNGLLQEQ LAHQNQRLPE
LGALLKQVNH LLRQANLPGQ FPLLVGYYHR ELKNLILVSA GLNATLNTGE HQVQISNGVP
LGTLGNAYLN QLSQRCDAWQ CQIWGTGGRL RLMLSAE


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