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NEPI_SALG2
ID   NEPI_SALG2              Reviewed;         397 AA.
AC   B5RG43;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN   Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; OrderedLocusNames=SG3652;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR39437.1; -; Genomic_DNA.
DR   RefSeq; WP_001004790.1; NC_011274.1.
DR   AlphaFoldDB; B5RG43; -.
DR   SMR; B5RG43; -.
DR   EnsemblBacteria; CAR39437; CAR39437; SG3652.
DR   KEGG; seg:SG3652; -.
DR   HOGENOM; CLU_001265_61_1_6; -.
DR   OMA; LLMTGHF; -.
DR   Proteomes; UP000008321; 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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="Purine ribonucleoside efflux pump NepI"
FT                   /id="PRO_1000138357"
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;  41778 MW;  4E86EDEDD8038A08 CRC64;
     MNENIAEKFR ADGVARPNWS AVFAVAFCVA CLITVEFLPV SLLTPMAQDL GISEGIAGQS
     VTVTAFVAMF SSLFITQIIQ ATDRRYIVIL FAVLLTASCL MVSFANSFTL LLLGRACLGL
     ALGGFWAMSA SLTMRLVPAR TVPKALSVIF GAVSIALVIA APLGSFLGGI IGWRNVFNAA
     AVMGVLCVIW VVKSLPSLPG EPSHQKQNMF SLLQRPGVMA GMIAIFMSFA GQFAFFTYIR
     PVYMNLAGFD VDGLTLVLLS FGIASFVGTS FSSYVLKRSV KLALAGAPLL LALSALTLIV
     WGSDKTVAAV IAIIWGLAFA LVPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAVG
     GYALDNFGLL SPLALSGCLM LLTALVVAAK VRITPMS
 
 
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