NEPI_SALPB
ID NEPI_SALPB Reviewed; 397 AA.
AC A9MWE8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189};
GN Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189}; OrderedLocusNames=SPAB_04694;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX70005.1; -; Genomic_DNA.
DR RefSeq; WP_001004800.1; NC_010102.1.
DR AlphaFoldDB; A9MWE8; -.
DR SMR; A9MWE8; -.
DR KEGG; spq:SPAB_04694; -.
DR PATRIC; fig|1016998.12.peg.4417; -.
DR HOGENOM; CLU_001265_61_1_6; -.
DR OMA; LLMTGHF; -.
DR BioCyc; SENT1016998:SPAB_RS19070-MON; -.
DR Proteomes; UP000008556; 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_1000085470"
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; 41718 MW; C4C63DA96F12C673 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
WGSDKTVAAV IAIIWGLAFA LVPVGWSTWI TRSLADQAEK AGSIQVAVIQ LANTCGAAVG
GYALDNFGLL SPLALSGGLM LLTALVVAAK VRITPMS
