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RSXA_ECOLI
ID   RSXA_ECOLI              Reviewed;         193 AA.
AC   P0A766; P76181; Q2MB70;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit A {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
DE   AltName: Full=Rsx electron transport complex subunit A {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000305};
GN   Name=rsxA {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000303|PubMed:12773378};
GN   Synonyms=rnfA, ydgL; OrderedLocusNames=b1627, JW1619;
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 / 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   [2]
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   [3]
RP   TOPOLOGY.
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   [4]
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   [5]
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_00459, 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_00459,
CC       ECO:0000305|PubMed:12773378}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00459, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00459}.
CC   -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00459}.
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DR   EMBL; U00096; AAC74699.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76486.1; -; Genomic_DNA.
DR   PIR; E64919; E64919.
DR   RefSeq; NP_416144.1; NC_000913.3.
DR   RefSeq; WP_000133193.1; NZ_STEB01000003.1.
DR   AlphaFoldDB; P0A766; -.
DR   SMR; P0A766; -.
DR   BioGRID; 4261327; 41.
DR   STRING; 511145.b1627; -.
DR   TCDB; 3.D.6.1.4; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR   PaxDb; P0A766; -.
DR   PRIDE; P0A766; -.
DR   EnsemblBacteria; AAC74699; AAC74699; b1627.
DR   EnsemblBacteria; BAE76486; BAE76486; BAE76486.
DR   GeneID; 66674481; -.
DR   GeneID; 946148; -.
DR   KEGG; ecj:JW1619; -.
DR   KEGG; eco:b1627; -.
DR   PATRIC; fig|1411691.4.peg.634; -.
DR   EchoBASE; EB3692; -.
DR   eggNOG; COG4657; Bacteria.
DR   HOGENOM; CLU_095255_1_0_6; -.
DR   InParanoid; P0A766; -.
DR   OMA; CPFFGVS; -.
DR   PhylomeDB; P0A766; -.
DR   BioCyc; EcoCyc:G6871-MON; -.
DR   PRO; PR:P0A766; -.
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_00459; RsxA_RnfA; 1.
DR   InterPro; IPR011293; Ion_transpt_RnfA/RsxA.
DR   InterPro; IPR003667; NqrDE/RnfAE.
DR   Pfam; PF02508; Rnf-Nqr; 1.
DR   PIRSF; PIRSF006102; NQR_DE; 1.
DR   TIGRFAMs; TIGR01943; rnfA; 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..193
FT                   /note="Ion-translocating oxidoreductase complex subunit A"
FT                   /id="PRO_0000214289"
FT   TOPO_DOM        1..4
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        26..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        60..62
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        84..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        123..133
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        155..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00459"
FT   TOPO_DOM        192..193
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:10411911,
FT                   ECO:0000269|PubMed:15919996"
SQ   SEQUENCE   193 AA;  20898 MW;  525955B3760398D7 CRC64;
     MTDYLLLFVG TVLVNNFVLV KFLGLCPFMG VSKKLETAMG MGLATTFVMT LASICAWLID
     TWILIPLNLI YLRTLAFILV IAVVVQFTEM VVRKTSPVLY RLLGIFLPLI TTNCAVLGVA
     LLNINLGHNF LQSALYGFSA AVGFSLVMVL FAAIRERLAV ADVPAPFRGN AIALITAGLM
     SLAFMGFSGL VKL
 
 
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