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RSXE_SHIBS
ID   RSXE_SHIBS              Reviewed;         231 AA.
AC   Q320Y9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=SBO_1502;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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; CP000036; ABB66119.1; -; Genomic_DNA.
DR   RefSeq; WP_001289657.1; NC_007613.1.
DR   AlphaFoldDB; Q320Y9; -.
DR   SMR; Q320Y9; -.
DR   EnsemblBacteria; ABB66119; ABB66119; SBO_1502.
DR   KEGG; sbo:SBO_1502; -.
DR   HOGENOM; CLU_046659_1_0_6; -.
DR   OMA; DGFMMGL; -.
DR   Proteomes; UP000007067; 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_1000014109"
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
 
 
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