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NEPI_SALTY
ID   NEPI_SALTY              Reviewed;         397 AA.
AC   Q7CPG0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN   Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; OrderedLocusNames=STM3776;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Involved in the efflux of purine ribonucleosides, such as
CC       inosine and guanosine. {ECO:0000255|HAMAP-Rule:MF_01189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + inosine(in) = H(+)(in) + inosine(out);
CC         Xref=Rhea:RHEA:29211, ChEBI:CHEBI:15378, ChEBI:CHEBI:17596;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01189};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29212;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01189};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(in) + H(+)(out) = guanosine(out) + H(+)(in);
CC         Xref=Rhea:RHEA:29583, ChEBI:CHEBI:15378, ChEBI:CHEBI:16750;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01189};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29584;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01189};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01189}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01189}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC       NepI (TC 2.A.1.2.26) subfamily. {ECO:0000255|HAMAP-Rule:MF_01189}.
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DR   EMBL; AE006468; AAL22634.1; -; Genomic_DNA.
DR   RefSeq; NP_462675.1; NC_003197.2.
DR   RefSeq; WP_001004798.1; NC_003197.2.
DR   AlphaFoldDB; Q7CPG0; -.
DR   SMR; Q7CPG0; -.
DR   STRING; 99287.STM3776; -.
DR   PaxDb; Q7CPG0; -.
DR   EnsemblBacteria; AAL22634; AAL22634; STM3776.
DR   GeneID; 1255300; -.
DR   KEGG; stm:STM3776; -.
DR   PATRIC; fig|99287.12.peg.3996; -.
DR   HOGENOM; CLU_001265_61_1_6; -.
DR   OMA; LLMTGHF; -.
DR   PhylomeDB; Q7CPG0; -.
DR   BioCyc; SENT99287:STM3776-MON; -.
DR   Proteomes; UP000001014; 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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   HAMAP; MF_01189; MFS_NepI; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR023680; MFS_NepI.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Antiport; Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="Purine ribonucleoside efflux pump NepI"
FT                   /id="PRO_0000294116"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        43..54
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        76..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        107
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        129..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        169..175
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        197..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        237..255
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        277..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        303..305
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        327..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        365..366
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
FT   TOPO_DOM        388..397
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
SQ   SEQUENCE   397 AA;  41690 MW;  23D04CCE7975C66B CRC64;
     MNENIAEKFR ADGVARPNWS AVFAVAFCVA CLITVEFLPV SLLTPMAQDL GISEGVAGQS
     VTVTAFVAMF SSLFITQIIQ ATDRRYIVIL FAVLLTASCL MVSFANSFTL LLLGRACLGL
     ALGGFWAMSA SLTMRLVPAR TVPKALSVIF GAVSIALVIA APLGSFLGGI IGWRNVFNAA
     AVMGVLCVIW VVKSLPSLPG EPSHQKQNMF SLLQRPGVMA GMIAIFMSFA GQFAFFTYIR
     PVYMNLAGFD VDGLTLVLLS FGIASFVGTS FSSYVLKRSV KLALAGAPLL LALSALTLIV
     WGSDKTVAAA IAIIWGLAFA LVPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAVG
     GYALDNFGLL SPLALSGGLM LLTALVVAAK VRITPMS
 
 
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