NEPI_SHISS
ID NEPI_SHISS Reviewed; 396 AA.
AC Q3YWE6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; OrderedLocusNames=SSON_3615;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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=AAZ90166.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000038; AAZ90166.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q3YWE6; -.
DR SMR; Q3YWE6; -.
DR EnsemblBacteria; AAZ90166; AAZ90166; SSON_3615.
DR KEGG; ssn:SSON_3615; -.
DR HOGENOM; CLU_001265_61_1_6; -.
DR Proteomes; UP000002529; 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..396
FT /note="Purine ribonucleoside efflux pump NepI"
FT /id="PRO_0000294120"
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; 41857 MW; 2560D74212C42E59 CRC64;
MSEFIAENRG ADAITRPNWS AVFSVAFCVA CLIIVEFLPV SLLTPMAQDL GISEGVAGQS
VTVTAFVAMF ASLFITQTIQ ATDRRNVVIL FAVLLTLSCL LVSFANSFSL LLIGRACLGL
ALGGFWAMSA SLTMRLVPPR TVPKALSVIF GAVSIALVIA APLGSFLGEL IGWRNVFNAA
AVMGVLCIFW IIKSLPSLPG EPSHQKQNTF RLLQRPGVMA GMIAIFMSFA GQFAFFTYIR
PVYMNLAGFS VDGLTLVLLS FGIASFIGTS LSSFILKRSV KLALAGAPLI LAVSALVLTL
WGSDKIVATG VAIIWGLTFA LVPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAIG
GYALDNIGLT SPLMFSGTLM LLTALLVTAK VKMKKS
