RCSB_ECOLI
ID RCSB_ECOLI Reviewed; 216 AA.
AC P0DMC7; P14374; P69407;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Transcriptional regulatory protein RcsB {ECO:0000255|HAMAP-Rule:MF_00981};
DE AltName: Full=Capsular synthesis regulator component B;
GN Name=rcsB {ECO:0000255|HAMAP-Rule:MF_00981};
GN OrderedLocusNames=b2217, JW2205;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=2404948; DOI=10.1128/jb.172.2.659-669.1990;
RA Stout V., Gottesman S.;
RT "RcsB and RcsC: a two-component regulator of capsule synthesis in
RT Escherichia coli.";
RL J. Bacteriol. 172:659-669(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-9, AND FUNCTION IN COLANIC ACID
RP SYNTHESIS AND CELL DIVISION.
RC STRAIN=K12;
RX PubMed=1597415; DOI=10.1128/jb.174.12.3964-3971.1992;
RA Gervais F.G., Phoenix P., Drapeau G.R.;
RT "The rcsB gene, a positive regulator of colanic acid biosynthesis in
RT Escherichia coli, is also an activator of ftsZ expression.";
RL J. Bacteriol. 174:3964-3971(1992).
RN [6]
RP INTERACTION WITH RCSA.
RX PubMed=1999391; DOI=10.1128/jb.173.5.1738-1747.1991;
RA Stout V., Torres-Cabassa A., Maurizi M.R., Gutnick D., Gottesman S.;
RT "RcsA, an unstable positive regulator of capsular polysaccharide
RT synthesis.";
RL J. Bacteriol. 173:1738-1747(1991).
RN [7]
RP FUNCTION, INTERACTION WITH RCSA, AND BINDING TO RCSAB BOX.
RX PubMed=10702265; DOI=10.1074/jbc.275.10.7013;
RA Wehland M., Bernhard F.;
RT "The RcsAB box. Characterization of a new operator essential for the
RT regulation of exopolysaccharide biosynthesis in enteric bacteria.";
RL J. Biol. Chem. 275:7013-7020(2000).
RN [8]
RP PHOSPHORELAY.
RX PubMed=11758943; DOI=10.1271/bbb.65.2364;
RA Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
RT "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway
RT involved in capsular synthesis in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11566985; DOI=10.1128/jb.183.20.5870-5876.2001;
RA Davalos-Garcia M., Conter A., Toesca I., Gutierrez C., Cam K.;
RT "Regulation of osmC gene expression by the two-component system rcsB-rcsC
RT in Escherichia coli.";
RL J. Bacteriol. 183:5870-5876(2001).
RN [10]
RP FUNCTION, PHOSPHORYLATION, AND PHOSPHORELAY.
RX PubMed=11309126; DOI=10.1046/j.1365-2958.2001.02393.x;
RA Takeda S.-H., Fujisawa Y., Matsubara M., Aiba H., Mizuno T.;
RT "A novel feature of the multistep phosphorelay in Escherichia coli: a
RT revised model of the RcsC->YojN->RcsB signalling pathway implicated in
RT capsular synthesis and swarming behaviour.";
RL Mol. Microbiol. 40:440-450(2001).
RN [11]
RP FUNCTION, AND PHOSPHORELAY.
RC STRAIN=K12 / ST001;
RX PubMed=13129944; DOI=10.1128/jb.185.19.5735-5746.2003;
RA Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
RA Mizuno T.;
RT "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB
RT phosphorelay system in Escherichia coli.";
RL J. Bacteriol. 185:5735-5746(2003).
RN [12]
RP INTERACTION WITH RCSD.
RX PubMed=15476819; DOI=10.1016/j.jmb.2004.08.096;
RA Rogov V.V., Bernhard F., Loehr F., Doetsch V.;
RT "Solution structure of the Escherichia coli YojN histidine-
RT phosphotransferase domain and its interaction with cognate phosphoryl
RT receiver domains.";
RL J. Mol. Biol. 343:1035-1048(2004).
RN [13]
RP ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100;
RX PubMed=19240136; DOI=10.1101/gad.499409;
RA Tschowri N., Busse S., Hengge R.;
RT "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light
RT response of Escherichia coli.";
RL Genes Dev. 23:522-534(2009).
RN [14]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [15]
RP FUNCTION IN BGL DEREPRESSION, ACTIVITY REGULATION, INTERACTION WITH RCSA
RP AND BGLJ, AND MUTAGENESIS OF ASP-56.
RC STRAIN=CSH50;
RX PubMed=20952573; DOI=10.1128/jb.00807-10;
RA Venkatesh G.R., Kembou Koungni F.C., Paukner A., Stratmann T.,
RA Blissenbach B., Schnetz K.;
RT "BglJ-RcsB heterodimers relieve repression of the Escherichia coli bgl
RT operon by H-NS.";
RL J. Bacteriol. 192:6456-6464(2010).
RN [16]
RP FUNCTION, INTERACTION WITH GADE, AND BINDING TO THE GAD BOX.
RX PubMed=20189963; DOI=10.1093/nar/gkq097;
RA Castanie-Cornet M.P., Cam K., Bastiat B., Cros A., Bordes P., Gutierrez C.;
RT "Acid stress response in Escherichia coli: mechanism of regulation of gadA
RT transcription by RcsB and GadE.";
RL Nucleic Acids Res. 38:3546-3554(2010).
CC -!- FUNCTION: Component of the Rcs signaling system, which controls
CC transcription of numerous genes. RcsB is the response regulator that
CC binds to regulatory DNA regions. Can function both in an RcsA-dependent
CC or RcsA-independent manner. The system regulates expression of numerous
CC genes, including genes involved in colanic acid capsule synthesis,
CC biofilm formation, cell division and outer membrane proteins synthesis.
CC Also involved, with GadE, in control of glutamate-dependent acid
CC resistance, and, with BglJ, in derepression of the cryptic bgl operon.
CC The RcsB-BglJ activity is probably independent of RcsB phosphorylation.
CC {ECO:0000255|HAMAP-Rule:MF_00981, ECO:0000269|PubMed:10702265,
CC ECO:0000269|PubMed:11309126, ECO:0000269|PubMed:11566985,
CC ECO:0000269|PubMed:13129944, ECO:0000269|PubMed:1597415,
CC ECO:0000269|PubMed:20189963, ECO:0000269|PubMed:20952573}.
CC -!- ACTIVITY REGULATION: Activity is modulated by phosphorylation and
CC interaction with other transcriptional regulators. Probably up-
CC regulated by YmgA/AriR, and possibly down-regulated by YcgZ, all 3 are
CC connector proteins providing additional signal input into the signaling
CC system. {ECO:0000269|PubMed:19240136, ECO:0000269|PubMed:20952573}.
CC -!- SUBUNIT: Interacts with RcsD and RcsA. Homodimer. Can form an
CC heterodimer with the coactivator RcsA, which binds to the RcsAB boxes
CC to promote transcription of RcsA-dependent genes. Can also form a
CC heterodimer with GadE to bind to the GAD box, and with BglJ to bind to
CC the bgl promoter. {ECO:0000255|HAMAP-Rule:MF_00981,
CC ECO:0000269|PubMed:10702265, ECO:0000269|PubMed:11566985,
CC ECO:0000269|PubMed:15476819, ECO:0000269|PubMed:1999391,
CC ECO:0000269|PubMed:20189963, ECO:0000269|PubMed:20952573}.
CC -!- INTERACTION:
CC P0DMC7; P39404: bglJ; NbExp=4; IntAct=EBI-369670, EBI-551429;
CC P0DMC7; P37195: dctR; NbExp=3; IntAct=EBI-369670, EBI-562540;
CC P0DMC7; P0DMC7: rcsB; NbExp=3; IntAct=EBI-369670, EBI-369670;
CC P0DMC7; P39838: rcsD; NbExp=5; IntAct=EBI-369670, EBI-556803;
CC -!- INDUCTION: Expression is dependent on the alternate sigma factor, RpoN
CC (PubMed:2404948). Repressed by hydroxyurea.
CC {ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:2404948}.
CC -!- PTM: Phosphorylated and activated by RcsD.
CC {ECO:0000305|PubMed:11309126}.
CC -!- MISCELLANEOUS: There is a close linkage between the Rcs and PhoQ/P
CC signaling systems, and both signaling systems respond to certain
CC external divalent cations (zinc and magnesium).
CC {ECO:0000305|PubMed:13129944}.
CC -!- SIMILARITY: Belongs to the RcsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00981}.
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DR EMBL; M28242; AAA24504.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75277.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16000.1; -; Genomic_DNA.
DR EMBL; S37760; AAB22290.1; -; Genomic_DNA.
DR PIR; JV0068; BVECCB.
DR RefSeq; NP_416721.1; NC_000913.3.
DR RefSeq; WP_001061917.1; NZ_STEB01000002.1.
DR PDB; 5I4C; X-ray; 2.00 A; A=1-147.
DR PDB; 5VXN; X-ray; 3.38 A; A/B/C/D=1-216.
DR PDB; 5W43; X-ray; 3.15 A; A/B=1-216.
DR PDBsum; 5I4C; -.
DR PDBsum; 5VXN; -.
DR PDBsum; 5W43; -.
DR AlphaFoldDB; P0DMC7; -.
DR SMR; P0DMC7; -.
DR BioGRID; 4260879; 5.
DR BioGRID; 851761; 4.
DR ComplexPortal; CPX-5762; rcsAB DNA-binding transcription factor complex.
DR ComplexPortal; CPX-5763; bglJ-rcsB DNA-binding transcription factor complex.
DR ComplexPortal; CPX-5764; matA-rcsB DNA-binding transcription factor complex.
DR ComplexPortal; CPX-5765; rcsB DNA-binding transcription factor homodimer.
DR ComplexPortal; CPX-5781; gadE-rcsB DNA-binding transcription factor complex.
DR IntAct; P0DMC7; 43.
DR STRING; 511145.b2217; -.
DR jPOST; P0DMC7; -.
DR PaxDb; P0DMC7; -.
DR PRIDE; P0DMC7; -.
DR EnsemblBacteria; AAC75277; AAC75277; b2217.
DR EnsemblBacteria; BAA16000; BAA16000; BAA16000.
DR GeneID; 67373623; -.
DR GeneID; 947441; -.
DR KEGG; ecj:JW2205; -.
DR KEGG; eco:b2217; -.
DR PATRIC; fig|1411691.4.peg.18; -.
DR EchoBASE; EB0814; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_1_6; -.
DR OMA; TITMIDN; -.
DR PhylomeDB; P0DMC7; -.
DR BioCyc; EcoCyc:RCSB-MON; -.
DR PRO; PR:P0DMC7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:EcoCyc.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990451; P:cellular stress response to acidic pH; IDA:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IMP:CACAO.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:1901913; P:regulation of capsule organization; IDA:ComplexPortal.
DR GO; GO:0043470; P:regulation of carbohydrate catabolic process; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IMP:CACAO.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CACAO.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00981; RcsB; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR030864; RcsB.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Capsule biogenesis/degradation; DNA-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..216
FT /note="Transcriptional regulatory protein RcsB"
FT /id="PRO_0000081209"
FT DOMAIN 5..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 144..209
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
FT DNA_BIND 168..187
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00981"
FT MUTAGEN 56
FT /note="D->E: Increases heterodimer formation with RcsA.
FT Does not affect heterodimer formation with BglJ."
FT /evidence="ECO:0000269|PubMed:20952573"
FT MUTAGEN 56
FT /note="D->N: Decreases heterodimer formation with RcsA.
FT Does not affect heterodimer formation with BglJ."
FT /evidence="ECO:0000269|PubMed:20952573"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:5I4C"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5I4C"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5I4C"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:5I4C"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5I4C"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5I4C"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5I4C"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:5W43"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:5W43"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5W43"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:5W43"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:5W43"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5W43"
SQ SEQUENCE 216 AA; 23671 MW; A78D1BD3004E0680 CRC64;
MNNMNVIIAD DHPIVLFGIR KSLEQIEWVN VVGEFEDSTA LINNLPKLDA HVLITDLSMP
GDKYGDGITL IKYIKRHFPS LSIIVLTMNN NPAILSAVLD LDIEGIVLKQ GAPTDLPKAL
AALQKGKKFT PESVSRLLEK ISAGGYGDKR LSPKESEVLR LFAEGFLVTE IAKKLNRSIK
TISSQKKSAM MKLGVENDIA LLNYLSSVTL SPADKD
