RSXE_SALCH
ID RSXE_SALCH Reviewed; 230 AA.
AC Q57PI3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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}; OrderedLocusNames=SCH_1472;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX65378.1; -; Genomic_DNA.
DR RefSeq; WP_001289628.1; NC_006905.1.
DR AlphaFoldDB; Q57PI3; -.
DR SMR; Q57PI3; -.
DR EnsemblBacteria; AAX65378; AAX65378; SCH_1472.
DR KEGG; sec:SCH_1472; -.
DR HOGENOM; CLU_046659_1_0_6; -.
DR OMA; DGFMMGL; -.
DR Proteomes; UP000000538; 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..230
FT /note="Ion-translocating oxidoreductase complex subunit E"
FT /id="PRO_0000214277"
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 230 AA; 24318 MW; E198B4CEA13F249E CRC64;
MSEIKDIVVQ GLWKNNSALV QLLGLCPLLA VTSTATNALG LGLATTLVLT LTNLTVSALR
RWTPAEIRIP IYVMIIASVV SAVQMLINAY AFGLYQSLGI FIPLIVTNCI VVGRAEAFAA
KKGPWLSALD GFSIGMGATG AMFVLGSLRE ILGNGTLFDG ADSLLGGWAK VLRVEIFHTD
SPFLLAMLPP GAFIGLGLML AVKYLIDEKM KKRRAETAPS AVPAGETGKV