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NEPI_SHIFL
ID   NEPI_SHIFL              Reviewed;         396 AA.
AC   P0ADL2; P31438; P76725;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN   Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN   OrderedLocusNames=SF3799, S3969;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN45239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP18957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN45239.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP18957.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_709532.3; NC_004337.2.
DR   RefSeq; WP_001288549.1; NZ_WPGW01000019.1.
DR   AlphaFoldDB; P0ADL2; -.
DR   SMR; P0ADL2; -.
DR   STRING; 198214.SF3799; -.
DR   EnsemblBacteria; AAN45239; AAN45239; SF3799.
DR   EnsemblBacteria; AAP18957; AAP18957; S3969.
DR   GeneID; 1026064; -.
DR   GeneID; 66672441; -.
DR   KEGG; sfl:SF3799; -.
DR   KEGG; sfx:S3969; -.
DR   PATRIC; fig|198214.7.peg.4484; -.
DR   HOGENOM; CLU_001265_61_1_6; -.
DR   OrthoDB; 1384345at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..396
FT                   /note="Purine ribonucleoside efflux pump NepI"
FT                   /id="PRO_0000169617"
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..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01189"
SQ   SEQUENCE   396 AA;  41842 MW;  DB240A4A8C1B9D1B CRC64;
     MSEFIAENRG ADAITRPNWS AVFSVAFCVA CLIIVEFLPV SLLTPMAQDL GISEGVAGQS
     VTVTAFVAMF ASLFITQTIQ ATDRRYVVIL FAVLLTLSCL LVSFANSFSL LLIGRACLGL
     ALGGFWAMSA SLTMRLVPPR TVPKALSVIF GAVSIALVIA APLGSFLGEL IGWRNVFNAA
     AVMGVLCIFW IIKSLPSLPG EPSHQKQNTF RLLQRPGVMA GMIAIFMSFA GQFAFFTYIR
     PVYMNLAGFG VDGLTLVLLS FGIASFIGTS LSSFILKRSV KLALAGAPLI LAVSALVLTL
     WGSDKIVATG VAIIWGLTFA LVPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAIG
     GYALDNIGLT SPLMLSGTLM LLTALLVTAK VKMKKS
 
 
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