NEPI_ECOLI
ID NEPI_ECOLI Reviewed; 396 AA.
AC P0ADL1; P31438; P76725; Q2M7X5; Q5I3I1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Purine ribonucleoside efflux pump NepI {ECO:0000255|HAMAP-Rule:MF_01189, ECO:0000305};
DE AltName: Full=Nucleoside efflux permease-inosine {ECO:0000303|PubMed:16040204};
GN Name=nepI {ECO:0000255|HAMAP-Rule:MF_01189, ECO:0000303|PubMed:16040204};
GN Synonyms=yicM; OrderedLocusNames=b3662, JW5938;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-396.
RC STRAIN=BEN2908 / O2:K1:H5 / APEC;
RX PubMed=16428402; DOI=10.1128/jb.188.3.977-987.2006;
RA Chouikha I., Germon P., Bree A., Gilot P., Moulin-Schouleur M.,
RA Schouler C.;
RT "A selC-associated genomic island of the extraintestinal avian pathogenic
RT Escherichia coli strain BEN2908 is involved in carbohydrate uptake and
RT virulence.";
RL J. Bacteriol. 188:977-987(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND CHARACTERIZATION OF TRANSLATIONAL START SITE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16040204; DOI=10.1016/j.femsle.2005.06.051;
RA Gronskiy S.V., Zakataeva N.P., Vitushkina M.V., Ptitsyn L.R., Altman I.B.,
RA Novikova A.E., Livshits V.A.;
RT "The yicM (nepI) gene of Escherichia coli encodes a major facilitator
RT superfamily protein involved in efflux of purine ribonucleosides.";
RL FEMS Microbiol. Lett. 250:39-47(2005).
CC -!- FUNCTION: Involved in the efflux of purine ribonucleosides, such as
CC inosine and guanosine (PubMed:16040204). Adenosine may also be a
CC substrate (PubMed:16040204). Confers resistance to the hypoxanthine
CC analog 6-mercaptopurine, however the level of resistance is rather low
CC (PubMed:16040204). {ECO:0000269|PubMed:16040204}.
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 ECO:0000269|PubMed:16040204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29212;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01189,
CC ECO:0000269|PubMed:16040204};
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 ECO:0000269|PubMed:16040204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29584;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01189,
CC ECO:0000269|PubMed:16040204};
CC -!- ACTIVITY REGULATION: Reducing the electrochemical proton gradient
CC across the plasma membrane by the addition of the protonophore carbonyl
CC cyanide m-chlorophenylhydrazone (CCCP) leads to a drastic reduction in
CC the rate of inosine excretion. {ECO:0000269|PubMed:16040204}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01189, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: In stationary phase. {ECO:0000269|PubMed:16040204}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to increased
CC susceptibility to purine ribonucleosides.
CC {ECO:0000269|PubMed:16040204}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62014.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAW51767.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE77631.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L10328; AAA62014.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76685.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77631.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY857617; AAW51767.1; ALT_FRAME; Genomic_DNA.
DR PIR; G65167; G65167.
DR RefSeq; NP_418118.2; NC_000913.3.
DR RefSeq; WP_001288549.1; NZ_SSZK01000043.1.
DR AlphaFoldDB; P0ADL1; -.
DR SMR; P0ADL1; -.
DR BioGRID; 4261472; 10.
DR DIP; DIP-48180N; -.
DR STRING; 511145.b3662; -.
DR TCDB; 2.A.1.2.26; the major facilitator superfamily (mfs).
DR PaxDb; P0ADL1; -.
DR PRIDE; P0ADL1; -.
DR EnsemblBacteria; AAC76685; AAC76685; b3662.
DR EnsemblBacteria; BAE77631; BAE77631; BAE77631.
DR GeneID; 66672441; -.
DR GeneID; 948213; -.
DR KEGG; ecj:JW5938; -.
DR KEGG; eco:b3662; -.
DR PATRIC; fig|511145.12.peg.3784; -.
DR EchoBASE; EB1640; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_61_1_6; -.
DR InParanoid; P0ADL1; -.
DR PhylomeDB; P0ADL1; -.
DR BioCyc; EcoCyc:YICM-MON; -.
DR BioCyc; MetaCyc:YICM-MON; -.
DR PRO; PR:P0ADL1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000169616"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..54
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..175
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..255
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..305
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..366
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT VARIANT 158
FT /note="V -> M (in strain: BEN2908 / O2:K1:H5 / APEC)"
FT VARIANT 182
FT /note="V -> A (in strain: BEN2908 / O2:K1:H5 / APEC)"
FT VARIANT 267
FT /note="I -> V (in strain: BEN2908 / O2:K1:H5 / APEC)"
FT VARIANT 289..290
FT /note="LI -> FV (in strain: BEN2908 / O2:K1:H5 / APEC)"
FT VARIANT 293
FT /note="V -> L (in strain: BEN2908 / O2:K1:H5 / APEC)"
FT VARIANT 322
FT /note="V -> I (in strain: BEN2908 / O2:K1:H5 / APEC)"
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
