RSEC_ECOLI
ID RSEC_ECOLI Reviewed; 159 AA.
AC P46187; Q2MAG0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein RseC {ECO:0000305};
GN Name=rseC {ECO:0000303|PubMed:9159522, ECO:0000303|PubMed:9159523};
GN OrderedLocusNames=b2570, JW2554;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7889935; DOI=10.1002/j.1460-2075.1995.tb07085.x;
RA Raina S., Missiakas D., Georgopoulos C.;
RT "The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of
RT Escherichia coli.";
RL EMBO J. 14:1043-1055(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=9159523; DOI=10.1046/j.1365-2958.1997.3611718.x;
RA De Las Penas A., Connolly L., Gross C.A.;
RT "The sigmaE-mediated response to extracytoplasmic stress in Escherichia
RT coli is transduced by RseA and RseB, two negative regulators of sigmaE.";
RL Mol. Microbiol. 24:373-385(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE, AND OPERON.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9159522; DOI=10.1046/j.1365-2958.1997.3601713.x;
RA Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S.;
RT "Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-
RT factor activity by the RseA, RseB and RseC proteins.";
RL Mol. Microbiol. 24:355-371(1997).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12773378; DOI=10.1093/emboj/cdg252;
RA Koo M.S., Lee J.H., Rah S.Y., Yeo W.S., Lee J.W., Lee K.L., Koh Y.S.,
RA Kang S.O., Roe J.H.;
RT "A reducing system of the superoxide sensor SoxR in Escherichia coli.";
RL EMBO J. 22:2614-2622(2003).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=18344336; DOI=10.1128/aem.02809-07;
RA Yang X., Ma Q., Wood T.K.;
RT "The R1 conjugative plasmid increases Escherichia coli biofilm formation
RT through an envelope stress response.";
RL Appl. Environ. Microbiol. 74:2690-2699(2008).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=24580753; DOI=10.1186/gb-2014-15-3-r44;
RA Krisko A., Copic T., Gabaldon T., Lehner B., Supek F.;
RT "Inferring gene function from evolutionary change in signatures of
RT translation efficiency.";
RL Genome Biol. 15:R44.1-R44.17(2014).
RN [11]
RP OPERON.
RC STRAIN=K12 / CF7789;
RX PubMed=28924029; DOI=10.1128/jb.00484-17;
RA Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
RT "Circuitry linking the global Csr and sigma(E)-dependent cell envelope
RT stress response systems.";
RL J. Bacteriol. 0:0-0(2017).
CC -!- FUNCTION: May play a role in reduction of the SoxR iron-sulfur cluster.
CC May work together with the RsxABCDGE complex.
CC {ECO:0000269|PubMed:12773378}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: According to PubMed:9159522, insertion mutant
CC shows a modest reduction in sigma-E (rpoE) activity. However,
CC PubMed:9159523 shows that deletion of the gene has no effect on sigma-E
CC activity (PubMed:9159522, PubMed:9159523). Deletion of the gene
CC enhances soxS expression (PubMed:12773378). Mutant shows increased
CC motility and biofilm formation (PubMed:18344336). Deletion mutant is
CC more sensitive than wild-type specifically to hydrogen peroxide
CC exposure, but not other stresses (PubMed:24580753).
CC {ECO:0000269|PubMed:12773378, ECO:0000269|PubMed:18344336,
CC ECO:0000269|PubMed:24580753, ECO:0000269|PubMed:9159522,
CC ECO:0000269|PubMed:9159523}.
CC -!- MISCELLANEOUS: Part of the rseD-rpoE-rseA-rseB-rseC operon
CC (PubMed:9159522, PubMed:9159523, PubMed:28924029).
CC {ECO:0000305|PubMed:28924029, ECO:0000305|PubMed:9159522,
CC ECO:0000305|PubMed:9159523}.
CC -!- SIMILARITY: Belongs to the RseC family. {ECO:0000305}.
CC -!- CAUTION: Was originally suggested to positively regulate sigma-E
CC activity in vitro. {ECO:0000305|PubMed:9159522}.
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DR EMBL; U37089; AAC45317.1; -; Genomic_DNA.
DR EMBL; U37455; AAC45320.1; -; Genomic_DNA.
DR EMBL; D64044; BAA10917.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75623.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76746.1; -; Genomic_DNA.
DR PIR; I83299; I83299.
DR RefSeq; NP_417065.1; NC_000913.3.
DR RefSeq; WP_000589068.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P46187; -.
DR BioGRID; 4260599; 11.
DR STRING; 511145.b2570; -.
DR PaxDb; P46187; -.
DR PRIDE; P46187; -.
DR EnsemblBacteria; AAC75623; AAC75623; b2570.
DR EnsemblBacteria; BAE76746; BAE76746; BAE76746.
DR GeneID; 947052; -.
DR KEGG; ecj:JW2554; -.
DR KEGG; eco:b2570; -.
DR PATRIC; fig|1411691.4.peg.4164; -.
DR EchoBASE; EB2970; -.
DR eggNOG; COG3086; Bacteria.
DR HOGENOM; CLU_124911_0_0_6; -.
DR InParanoid; P46187; -.
DR OMA; MVKEWAT; -.
DR PhylomeDB; P46187; -.
DR BioCyc; EcoCyc:G7347-MON; -.
DR PRO; PR:P46187; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR InterPro; IPR026268; RseC.
DR InterPro; IPR007359; SigmaE_reg_RseC_MucC.
DR PANTHER; PTHR35867; PTHR35867; 1.
DR PIRSF; PIRSF004923; RseC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..159
FT /note="Protein RseC"
FT /id="PRO_0000097483"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..98
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 159 AA; 16639 MW; BCFD8970DF6277C0 CRC64;
MIKEWATVVS WQNGQALVSC DVKASCSSCA SRAGCGSRVL NKLGPQTTHT IVVPCDEPLV
PGQKVELGIA EGSLLSSALL VYMSPLVGLF LIASLFQLLF ASDVAALCGA ILGGIGGFLI
ARGYSRKFAA RAEWQPIILS VALPPGLVRF ETSSEDASQ
