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GDX_ECOLI
ID   GDX_ECOLI               Reviewed;         105 AA.
AC   P69937; P30743; Q2M6F4;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Guanidinium exporter {ECO:0000303|PubMed:29507227};
DE   AltName: Full=Quaternary ammonium compound-resistance protein SugE {ECO:0000305};
GN   Name=gdx {ECO:0000303|PubMed:29507227};
GN   Synonyms=sugE {ECO:0000303|PubMed:8096175};
GN   OrderedLocusNames=b4148, JW5738;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8096175; DOI=10.1002/j.1460-2075.1993.tb05729.x;
RA   Greener T., Govezensky D., Zamir A.;
RT   "A novel multicopy suppressor of a groEL mutation includes two nested open
RT   reading frames transcribed from different promoters.";
RL   EMBO J. 12:889-896(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / CS520;
RX   PubMed=9677290; DOI=10.1006/jmbi.1998.1894;
RA   Bishop R.E., Leskiw B.K., Hodges R.S., Kay C.M., Weiner J.H.;
RT   "The entericidin locus of Escherichia coli and its implications for
RT   programmed bacterial cell death.";
RL   J. Mol. Biol. 280:583-596(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, AND OVEREXPRESSION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=11948170; DOI=10.1128/jb.184.9.2543-2545.2002;
RA   Chung Y.J., Saier M.H. Jr.;
RT   "Overexpression of the Escherichia coli sugE gene confers resistance to a
RT   narrow range of quaternary ammonium compounds.";
RL   J. Bacteriol. 184:2543-2545(2002).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14728684; DOI=10.1111/j.1432-1033.2003.03959.x;
RA   Klammt C., Loehr F., Schaefer B., Haase W., Doetsch V., Rueterjans H.,
RA   Glaubitz C., Bernhard F.;
RT   "High level cell-free expression and specific labeling of integral membrane
RT   proteins.";
RL   Eur. J. Biochem. 271:568-580(2004).
RN   [8]
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).
RN   [9]
RP   INDUCTION.
RX   PubMed=28001368; DOI=10.1021/acs.biochem.6b01270;
RA   Sherlock M.E., Malkowski S.N., Breaker R.R.;
RT   "Biochemical validation of a second guanidine riboswitch class in
RT   bacteria.";
RL   Biochemistry 56:352-358(2017).
RN   [10]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=29507227; DOI=10.1073/pnas.1719187115;
RA   Kermani A.A., Macdonald C.B., Gundepudi R., Stockbridge R.B.;
RT   "Guanidinium export is the primal function of SMR family transporters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:3060-3065(2018).
CC   -!- FUNCTION: Guanidinium ion exporter. Couples guanidinium export to the
CC       proton motive force, exchanging one guanidinium ion for two protons
CC       (PubMed:29507227). Overexpression leads to resistance to a subset of
CC       toxic quaternary ammonium compounds such as cetylpyridinium,
CC       cetyldimethylethyl ammonium and cetrimide cations (PubMed:11948170).
CC       {ECO:0000269|PubMed:11948170, ECO:0000269|PubMed:29507227}.
CC   -!- SUBUNIT: Homodimer. The subunits assemble with antiparallel topology.
CC       {ECO:0000269|PubMed:29507227}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:14728684,
CC       ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14728684}.
CC   -!- INDUCTION: Transcriptionally regulated by guanidine, via a guanidine-
CC       sensing riboswitch. {ECO:0000269|PubMed:28001368}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.
CC       Gdx/SugE subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:8096175) thought to suppress a groEL
CC       mutation and mimic the effect of groE overexpression. This was later
CC       shown (PubMed:11948170) to be probably due to an artifact.
CC       {ECO:0000305|PubMed:11948170, ECO:0000305|PubMed:8096175}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97047.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA49570.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X69949; CAA49570.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X69949; CAA49571.1; -; Genomic_DNA.
DR   EMBL; U21726; AAC46453.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97047.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77108.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78152.1; -; Genomic_DNA.
DR   PIR; S56376; S56376.
DR   RefSeq; NP_418572.4; NC_000913.3.
DR   RefSeq; WP_000118482.1; NZ_STEB01000014.1.
DR   AlphaFoldDB; P69937; -.
DR   SMR; P69937; -.
DR   BioGRID; 4262698; 178.
DR   STRING; 511145.b4148; -.
DR   TCDB; 2.A.7.1.4; the drug/metabolite transporter (dmt) superfamily.
DR   PaxDb; P69937; -.
DR   EnsemblBacteria; AAC77108; AAC77108; b4148.
DR   EnsemblBacteria; BAE78152; BAE78152; BAE78152.
DR   GeneID; 66671938; -.
DR   GeneID; 948671; -.
DR   KEGG; ecj:JW5738; -.
DR   KEGG; eco:b4148; -.
DR   PATRIC; fig|1411691.4.peg.2550; -.
DR   EchoBASE; EB1573; -.
DR   eggNOG; COG2076; Bacteria.
DR   HOGENOM; CLU_133067_1_2_6; -.
DR   InParanoid; P69937; -.
DR   OMA; FEIAWAI; -.
DR   PhylomeDB; P69937; -.
DR   BioCyc; EcoCyc:SUGE-MON; -.
DR   BioCyc; MetaCyc:SUGE-MON; -.
DR   PRO; PR:P69937; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0015299; F:solute:proton antiporter activity; IDA:EcoCyc.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
DR   InterPro; IPR000390; Small_drug/metabolite_transptr.
DR   InterPro; IPR045324; Small_multidrug_res.
DR   PANTHER; PTHR30561; PTHR30561; 1.
DR   Pfam; PF00893; Multi_Drug_Res; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..105
FT                   /note="Guanidinium exporter"
FT                   /id="PRO_0000108095"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..57
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:15919996"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..105
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:15919996"
SQ   SEQUENCE   105 AA;  10900 MW;  C4686D9EDC1B7D08 CRC64;
     MSWIILVIAG LLEVVWAVGL KYTHGFSRLT PSVITVTAMI VSMALLAWAM KSLPVGTAYA
     VWTGIGAVGA AITGIVLLGE SANPMRLASL ALIVLGIIGL KLSTH
 
 
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