NEPI_SALTI
ID NEPI_SALTI Reviewed; 397 AA.
AC Q8XGS2; O70010; Q7ALZ4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; Synonyms=gaiA;
GN OrderedLocusNames=STY4008, t3742;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-397, INDUCTION, AND ROLE IN
RP VIRULENCE.
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12228264; DOI=10.1128/iai.70.10.5404-5411.2002;
RA Basso H., Rharbaoui F., Staendner L.H., Medina E., Garcia-Del Portillo F.,
RA Guzman C.A.;
RT "Characterization of a novel intracellularly activated gene from Salmonella
RT enterica serovar typhi.";
RL Infect. Immun. 70:5404-5411(2002).
CC -!- FUNCTION: Involved in the efflux of purine ribonucleosides, such as
CC inosine and guanosine (By similarity). Required for triggering
CC apoptosis and bacterial survival inside macrophages (PubMed:12228264).
CC {ECO:0000255|HAMAP-Rule:MF_01189, ECO:0000269|PubMed:12228264}.
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 -!- INDUCTION: Induced upon invasion of the host cell.
CC {ECO:0000269|PubMed:12228264}.
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 ECO:0000305}.
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DR EMBL; AE014613; AAO71233.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD03218.1; -; Genomic_DNA.
DR EMBL; AJ006101; CAA06861.1; -; Genomic_DNA.
DR PIR; S70825; S70825.
DR RefSeq; NP_458159.1; NC_003198.1.
DR RefSeq; WP_001004798.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8XGS2; -.
DR SMR; Q8XGS2; -.
DR STRING; 220341.16504847; -.
DR EnsemblBacteria; AAO71233; AAO71233; t3742.
DR KEGG; stt:t3742; -.
DR KEGG; sty:STY4008; -.
DR PATRIC; fig|220341.7.peg.4092; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_61_1_6; -.
DR OMA; LLMTGHF; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 2: Evidence at transcript level;
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_0000294115"
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"
FT CONFLICT 309..310
FT /note="AA -> GG (in Ref. 3; CAA06861)"
FT /evidence="ECO:0000305"
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
