NEPI_ECO27
ID NEPI_ECO27 Reviewed; 396 AA.
AC B7UMD5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; OrderedLocusNames=E2348C_3977;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS11525.1; -; Genomic_DNA.
DR RefSeq; WP_001339875.1; NC_011601.1.
DR AlphaFoldDB; B7UMD5; -.
DR SMR; B7UMD5; -.
DR EnsemblBacteria; CAS11525; CAS11525; E2348C_3977.
DR KEGG; ecg:E2348C_3977; -.
DR HOGENOM; CLU_001265_61_1_6; -.
DR OMA; LLMTGHF; -.
DR Proteomes; UP000008205; 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_1000164496"
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; 41800 MW; CC212117ADCCA2B6 CRC64;
MSEFIAENRG ADAITRPNWS AVFSVAFCVA CLIIVEFLPV SLLTPMAQDL GISEGVAGQS
VTVTAFVAMF ASLFITQTIQ ATDRRYVVIL FAVLLTLSCL LVSFANSFSL LLIGRACLGL
ALGGFWAISA SLTMRLVPPR TVPKALSVIF GAVSIALVIA APLGGFLGEL IGWRNVFNAA
AAMGVLCIFW IIKSLPSLPG EPSHQKQNTF RLLQRPGVMA GMIAIFMSFA GQFAFFTYIR
PVYMNLAGFG VDGLTLVLLS FGIASFVGTS LSSFILKRSV KLALAGAPFV LALSALVLTL
WGSDKIVATG VAIIWGLTFA LIPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAIG
GYALDNIGLT SPLMLSGTLM LLTALLVTAK VKMKKS
