RSSB_ECOLI
ID RSSB_ECOLI Reviewed; 337 AA.
AC P0AEV1; P37055;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Regulator of RpoS {ECO:0000255|HAMAP-Rule:MF_00958};
GN Name=rssB {ECO:0000255|HAMAP-Rule:MF_00958}; Synonyms=hnr, sprE, ychL;
GN OrderedLocusNames=b1235, JW1223;
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 Contreras A.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8282700; DOI=10.1128/jb.176.1.221-231.1994;
RA Boesl M., Kersten H.;
RT "Organization and functions of genes in the upstream region of tyrT of
RT Escherichia coli: phenotypes of mutants with partial deletion of a new gene
RT (tgs).";
RL J. Bacteriol. 176:221-231(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8635466; DOI=10.1002/j.1460-2075.1996.tb00475.x;
RA Muffler A., Fischer D., Altuvia S., Storz G., Hengge-Aronis R.;
RT "The response regulator RssB controls stability of the sigma(S) subunit of
RT RNA polymerase in Escherichia coli.";
RL EMBO J. 15:1333-1339(1996).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8637901; DOI=10.1073/pnas.93.6.2488;
RA Pratt L.A., Silhavy T.J.;
RT "The response regulator SprE controls the stability of RpoS.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2488-2492(1996).
RN [8]
RP PHOSPHORYLATION AT ASP-58, AND MUTAGENESIS OF ASP-58.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9515704; DOI=10.1046/j.1365-2958.1998.00725.x;
RA Bouche S., Klauck E., Fischer D., Lucassen M., Jung K., Hengge-Aronis R.;
RT "Regulation of RssB-dependent proteolysis in Escherichia coli: a role for
RT acetyl phosphate in a response regulator-controlled process.";
RL Mol. Microbiol. 27:787-795(1998).
RN [9]
RP INTERACTION WITH RPOS, AND PHOSPHORYLATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10339606; DOI=10.1073/pnas.96.11.6439;
RA Becker G., Klauck E., Hengge-Aronis R.;
RT "Regulation of RpoS proteolysis in Escherichia coli: the response regulator
RT RssB is a recognition factor that interacts with the turnover element in
RT RpoS.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6439-6444(1999).
RN [10]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10869095; DOI=10.1128/jb.182.14.4117-4120.2000;
RA Gibson K.E., Silhavy T.J.;
RT "SprE levels are growth phase regulated in a sigma(S)-dependent manner at
RT the level of translation.";
RL J. Bacteriol. 182:4117-4120(2000).
RN [11]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH RPOS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10672187; DOI=10.1046/j.1365-2958.2000.01736.x;
RA Becker G., Klauck E., Hengge-Aronis R.;
RT "The response regulator RssB, a recognition factor for sigmaS proteolysis
RT in Escherichia coli, can act like an anti-sigmaS factor.";
RL Mol. Microbiol. 35:657-666(2000).
RN [12]
RP FUNCTION, INTERACTION WITH RPOS, DOMAIN, PHOSPHORYLATION, AND MUTAGENESIS
RP OF ASP-58.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11442836; DOI=10.1046/j.1365-2958.2001.02482.x;
RA Klauck E., Lingnau M., Hengge-Aronis R.;
RT "Role of the response regulator RssB in sigma recognition and initiation of
RT sigma proteolysis in Escherichia coli.";
RL Mol. Microbiol. 40:1381-1390(2001).
RN [13]
RP ACTIVITY REGULATION, AND INTERACTION WITH IRAP.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16600914; DOI=10.1101/gad.1400306;
RA Bougdour A., Wickner S., Gottesman S.;
RT "Modulating RssB activity: IraP, a novel regulator of sigma(S) stability in
RT Escherichia coli.";
RL Genes Dev. 20:884-897(2006).
RN [14]
RP ACTIVITY REGULATION, AND INTERACTION WITH IRAD AND IRAM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18383615; DOI=10.1111/j.1365-2958.2008.06146.x;
RA Bougdour A., Cunning C., Baptiste P.J., Elliott T., Gottesman S.;
RT "Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia
RT coli via the action of multiple anti-adaptors.";
RL Mol. Microbiol. 68:298-313(2008).
RN [15]
RP FUNCTION IN POLYADENYLATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19767441; DOI=10.1128/jb.00870-09;
RA Carabetta V.J., Mohanty B.K., Kushner S.R., Silhavy T.J.;
RT "The response regulator SprE (RssB) modulates polyadenylation and mRNA
RT stability in Escherichia coli.";
RL J. Bacteriol. 191:6812-6821(2009).
RN [16]
RP FUNCTION IN POLYADENYLATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20472786; DOI=10.1128/jb.00300-10;
RA Carabetta V.J., Silhavy T.J., Cristea I.M.;
RT "The response regulator SprE (RssB) is required for maintaining poly(A)
RT polymerase I-degradosome association during stationary phase.";
RL J. Bacteriol. 192:3713-3721(2010).
RN [17]
RP ACTIVITY REGULATION, INTERACTION WITH IRAP; IRAD AND IRAM, DOMAIN,
RP PHOSPHORYLATION, AND MUTAGENESIS OF ASP-58; LEU-67; PRO-109; TRP-143;
RP LEU-214; ALA-216; LEU-218 AND ALA-255.
RX PubMed=24352426; DOI=10.1101/gad.229617.113;
RA Battesti A., Hoskins J.R., Tong S., Milanesio P., Mann J.M., Kravats A.,
RA Tsegaye Y.M., Bougdour A., Wickner S., Gottesman S.;
RT "Anti-adaptors provide multiple modes for regulation of the RssB adaptor
RT protein.";
RL Genes Dev. 27:2722-2735(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-130.
RA Levchenko I., Grant R.A., Sauer R.T., Baker T.A.;
RT "The structure of RssB, a ClpX adaptor protein that regulates sigma S.";
RL Submitted (SEP-2008) to the PDB data bank.
CC -!- FUNCTION: Regulates the turnover of the sigma S factor (RpoS) by
CC promoting its proteolysis in exponentially growing cells. Acts by
CC binding and delivering RpoS to the ClpXP protease. RssB is not co-
CC degraded with RpoS, but is released from the complex and can initiate a
CC new cycle of RpoS recognition and degradation. In stationary phase,
CC could also act as an anti-sigma factor and reduce the ability of RpoS
CC to activate gene expression. Is also involved in the regulation of the
CC mRNA polyadenylation pathway during stationary phase, probably by
CC maintaining the association of PcnB with the degradosome.
CC {ECO:0000255|HAMAP-Rule:MF_00958, ECO:0000269|PubMed:10672187,
CC ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:19767441,
CC ECO:0000269|PubMed:20472786, ECO:0000269|PubMed:8635466,
CC ECO:0000269|PubMed:8637901}.
CC -!- ACTIVITY REGULATION: Under certain stress conditions, activity is
CC inhibited by the anti-adapter proteins IraP, IraD and IraM. IraP is
CC involved in response to phosphate stavation, IraD in response to DNA
CC damage and IraM in response to magnesium starvation. IraD and IraM
CC interact with inactive RssB, blocking its ability to interact with
CC RpoS. IraP may mimic RpoS in its interaction with RssB and directly
CC competing with RpoS for binding to RssB. {ECO:0000269|PubMed:16600914,
CC ECO:0000269|PubMed:18383615, ECO:0000269|PubMed:24352426}.
CC -!- SUBUNIT: Binds to RpoS with a stoichiometry of 1:1. Interacts with the
CC anti-adapter proteins IraP, IraD and IraM. {ECO:0000255|HAMAP-
CC Rule:MF_00958, ECO:0000269|PubMed:10339606,
CC ECO:0000269|PubMed:10672187, ECO:0000269|PubMed:11442836,
CC ECO:0000269|PubMed:16600914, ECO:0000269|PubMed:18383615,
CC ECO:0000269|PubMed:24352426}.
CC -!- INTERACTION:
CC P0AEV1; P39375: iraD; NbExp=4; IntAct=EBI-1122979, EBI-6479779;
CC P0AEV1; P75987: iraM; NbExp=2; IntAct=EBI-1122979, EBI-6479798;
CC P0AEV1; P0AAN9: iraP; NbExp=3; IntAct=EBI-1122979, EBI-1116300;
CC -!- INDUCTION: Expression is induced during stationary phase by RpoS.
CC {ECO:0000269|PubMed:10869095}.
CC -!- DOMAIN: Contains an N-terminal receiver domain and a C-terminal output
CC domain that are both required for binding to RpoS. IraP and IraD
CC interact with the N-terminal domain. IraM interacts with the C-terminal
CC domain and, more weakly, the N-terminal domain.
CC {ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426}.
CC -!- PTM: Phosphorylated. Phosphorylation stimulates the interaction with
CC RpoS and, therefore, the proteolysis of RpoS. {ECO:0000255|HAMAP-
CC Rule:MF_00958, ECO:0000269|PubMed:10339606,
CC ECO:0000269|PubMed:11442836, ECO:0000269|PubMed:24352426,
CC ECO:0000269|PubMed:9515704}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit nearly constitutively high levels
CC of RpoS and are impaired in the post-transcriptional growth phase-
CC related and osmotic regulation of RpoS. In exponentially growing cells,
CC mutants exhibit significantly reduced levels of polyadenylation and
CC increased stability of specific mRNAs. {ECO:0000269|PubMed:19767441,
CC ECO:0000269|PubMed:8635466}.
CC -!- SIMILARITY: Belongs to the RssB family. {ECO:0000255|HAMAP-
CC Rule:MF_00958}.
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DR EMBL; X66003; CAA46802.1; -; Genomic_DNA.
DR EMBL; M64675; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U00096; AAC74317.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36103.1; -; Genomic_DNA.
DR PIR; A36871; A36871.
DR RefSeq; NP_415751.1; NC_000913.3.
DR RefSeq; WP_000193447.1; NZ_STEB01000005.1.
DR PDB; 3EOD; X-ray; 1.75 A; A=1-130.
DR PDB; 6Z4C; X-ray; 2.00 A; A/B=1-337.
DR PDB; 6Z4E; X-ray; 2.00 A; A=1-337.
DR PDB; 7L9C; X-ray; 1.85 A; A=1-129.
DR PDB; 7LCM; X-ray; 1.91 A; A=1-129.
DR PDBsum; 3EOD; -.
DR PDBsum; 6Z4C; -.
DR PDBsum; 6Z4E; -.
DR PDBsum; 7L9C; -.
DR PDBsum; 7LCM; -.
DR AlphaFoldDB; P0AEV1; -.
DR SMR; P0AEV1; -.
DR BioGRID; 4261926; 3.
DR BioGRID; 850222; 1.
DR ComplexPortal; CPX-5024; rpoS-rssB sigma-antisigma complex.
DR IntAct; P0AEV1; 5.
DR STRING; 511145.b1235; -.
DR jPOST; P0AEV1; -.
DR PaxDb; P0AEV1; -.
DR PRIDE; P0AEV1; -.
DR EnsemblBacteria; AAC74317; AAC74317; b1235.
DR EnsemblBacteria; BAA36103; BAA36103; BAA36103.
DR GeneID; 58390554; -.
DR GeneID; 945855; -.
DR KEGG; ecj:JW1223; -.
DR KEGG; eco:b1235; -.
DR PATRIC; fig|1411691.4.peg.1050; -.
DR EchoBASE; EB2042; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_055989_1_0_6; -.
DR InParanoid; P0AEV1; -.
DR OMA; HWHLEYL; -.
DR PhylomeDB; P0AEV1; -.
DR BioCyc; EcoCyc:EG12121-MON; -.
DR EvolutionaryTrace; P0AEV1; -.
DR PRO; PR:P0AEV1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:1903865; C:sigma factor antagonist complex; IPI:ComplexPortal.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:EcoCyc.
DR GO; GO:0031648; P:protein destabilization; IMP:EcoCyc.
DR Gene3D; 3.60.40.10; -; 1.
DR HAMAP; MF_00958; RssB; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR028616; RssB.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..337
FT /note="Regulator of RpoS"
FT /id="PRO_0000081388"
FT DOMAIN 9..123
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 58
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00958,
FT ECO:0000269|PubMed:9515704"
FT MUTAGEN 58
FT /note="D->P,Q,R: Lack of phosphorylation. Cannot bind
FT RpoS."
FT /evidence="ECO:0000269|PubMed:11442836,
FT ECO:0000269|PubMed:24352426, ECO:0000269|PubMed:9515704"
FT MUTAGEN 67
FT /note="L->A: Lack of phosphorylation."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 109
FT /note="P->S: Resistant to IraP but not to IraD. Increases
FT stabilization by IraM. Decreases phosphorylation."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 143
FT /note="W->R: Resistant to both IraP and IraD. Increases
FT stabilization by IraM."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 214
FT /note="L->H: Resistant to IraP and IraD."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 216
FT /note="A->T: Resistant to IraP, IraD and IraM."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 218
FT /note="L->V: Resistant to IraP, IraD and IraM."
FT /evidence="ECO:0000269|PubMed:24352426"
FT MUTAGEN 255
FT /note="A->V: Resistant to IraM."
FT /evidence="ECO:0000269|PubMed:24352426"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3EOD"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3EOD"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7L9C"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3EOD"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:3EOD"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3EOD"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3EOD"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:6Z4E"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:6Z4E"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 185..204
FT /evidence="ECO:0007829|PDB:6Z4E"
FT HELIX 210..233
FT /evidence="ECO:0007829|PDB:6Z4E"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:6Z4E"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:6Z4E"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:6Z4E"
SQ 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
