RSXE_ECOLI
ID RSXE_ECOLI Reviewed; 231 AA.
AC P77179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000305};
DE AltName: Full=Rsx electron transport complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000305};
GN Name=rsxE {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000303|PubMed:12773378};
GN Synonyms=rnfE, ydgQ; OrderedLocusNames=b1632, JW1624;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=10411911; DOI=10.1073/pnas.96.15.8540;
RA Saeaef A., Johansson M., Wallin E., von Heijne G.;
RT "Divergent evolution of membrane protein topology: the Escherichia coli
RT RnfA and RnfE homologues.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8540-8544(1999).
RN [5]
RP FUNCTION, SUBUNIT, AND GENE NAME.
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 [6]
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).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane (By
CC similarity). Required to maintain the reduced state of SoxR. Probably
CC transfers electron from NAD(P)H to SoxR (PubMed:12773378).
CC {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000269|PubMed:12773378}.
CC -!- SUBUNIT: The complex is composed of six subunits: RsxA, RsxB, RsxC,
CC RsxD, RsxE and RsxG. {ECO:0000255|HAMAP-Rule:MF_00478,
CC ECO:0000305|PubMed:12773378}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00478, ECO:0000269|PubMed:10411911,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00478, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00478}.
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DR EMBL; U00096; AAC74704.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15386.1; -; Genomic_DNA.
DR PIR; B64920; B64920.
DR RefSeq; NP_416149.1; NC_000913.3.
DR RefSeq; WP_001289652.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P77179; -.
DR SMR; P77179; -.
DR BioGRID; 4260257; 117.
DR STRING; 511145.b1632; -.
DR TCDB; 3.D.6.1.4; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR PaxDb; P77179; -.
DR PRIDE; P77179; -.
DR EnsemblBacteria; AAC74704; AAC74704; b1632.
DR EnsemblBacteria; BAA15386; BAA15386; BAA15386.
DR GeneID; 947509; -.
DR KEGG; ecj:JW1624; -.
DR KEGG; eco:b1632; -.
DR PATRIC; fig|1411691.4.peg.629; -.
DR EchoBASE; EB3697; -.
DR eggNOG; COG4660; Bacteria.
DR HOGENOM; CLU_046659_1_0_6; -.
DR InParanoid; P77179; -.
DR OMA; DGFMMGL; -.
DR PhylomeDB; P77179; -.
DR BioCyc; EcoCyc:G6876-MON; -.
DR PRO; PR:P77179; -.
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:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00478; RsxE_RnfE; 1.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR InterPro; IPR010968; RnfE.
DR PANTHER; PTHR30586:SF0; PTHR30586:SF0; 1.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01948; rnfE; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Membrane;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..231
FT /note="Ion-translocating oxidoreductase complex subunit E"
FT /id="PRO_0000214269"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10411911"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TOPO_DOM 60..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10411911"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TOPO_DOM 84..85
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10411911"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TOPO_DOM 107..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10411911"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TOPO_DOM 146..181
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10411911"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT TOPO_DOM 203..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10411911,
FT ECO:0000269|PubMed:15919996"
SQ SEQUENCE 231 AA; 24459 MW; CFA37A2D292604C3 CRC64;
MSEIKDVIVQ GLWKNNSALV QLLGLCPLLA VTSTATNALG LGLATTLVLT LTNLTISTLR
HWTPAEIRIP IYVMIIASVV SAVQMLINAY AFGLYQSLGI FIPLIVTNCI VVGRAEAFAA
KKGPALSALD GFSIGMGATC AMFVLGSLRE IIGNGTLFDG ADALLGSWAK VLRVEIFHTD
SPFLLAMLPP GAFIGLGLML AGKYLIDERM KKRRAEAAAE RALPNGETGN V
