ID   RSXE_ECO24              Reviewed;         231 AA.
AC   A7ZM92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00478};
DE   AltName: Full=Rsx electron transport complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478};
GN   Name=rsxE {ECO:0000255|HAMAP-Rule:MF_00478}; Synonyms=rnfE;
GN   OrderedLocusNames=EcE24377A_1841;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane. Required to
CC       maintain the reduced state of SoxR. {ECO:0000255|HAMAP-Rule:MF_00478}.
CC   -!- SUBUNIT: The complex is composed of six subunits: RsxA, RsxB, RsxC,
CC       RsxD, RsxE and RsxG. {ECO:0000255|HAMAP-Rule:MF_00478}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00478}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00478}.
CC   -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00478}.
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DR   EMBL; CP000800; ABV18183.1; -; Genomic_DNA.
DR   RefSeq; WP_001289657.1; NC_009801.1.
DR   AlphaFoldDB; A7ZM92; -.
DR   SMR; A7ZM92; -.
DR   EnsemblBacteria; ABV18183; ABV18183; EcE24377A_1841.
DR   KEGG; ecw:EcE24377A_1841; -.
DR   HOGENOM; CLU_046659_1_0_6; -.
DR   OMA; DGFMMGL; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Membrane;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..231
FT                   /note="Ion-translocating oxidoreductase complex subunit E"
FT                   /id="PRO_1000060407"
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   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00478"
SQ   SEQUENCE   231 AA;  24489 MW;  D4A2CA2D292604C3 CRC64;
     MSEIKDVIVQ GLWKNNSALV QLLGLCPLLA VTSTATNALG LGLATTLVLT LTNLTISTLR
     HWTPAEIRIP IYVMIIASVV SAVQMLINAY AFGLYQSLGI FIPLIVTNCI VVGRAEAFAA
     KKGPALSALD GFSIGMGATC AMFVLGSLRE IIGNGTLFDG ADALLGSWAK VLRVEIFHTD
     SPFLLAMLPP GAFIGLGLML AGKYLIDERM KKRRTEAAAE RALPNGETGN V