ID   NUPC_ECOL6              Reviewed;         400 AA.
AC   P0AFF3; P33031; P77236;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Nucleoside permease NupC {ECO:0000250|UniProtKB:P0AFF2};
DE   AltName: Full=Nucleoside-transport system protein NupC {ECO:0000250|UniProtKB:P0AFF2};
GN   Name=nupC {ECO:0000250|UniProtKB:P0AFF2}; OrderedLocusNames=c2932;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Nucleoside transport protein that can transport adenosine,
CC       uridine, thymidine, cytidine and deoxycytidine (By similarity).
CC       Transport is driven by a proton motive force (By similarity).
CC       {ECO:0000250|UniProtKB:P0AFF2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(in) + H(+)(in) = adenosine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29987, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335;
CC         Evidence={ECO:0000250|UniProtKB:P0AFF2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + uridine(in) = H(+)(out) + uridine(out);
CC         Xref=Rhea:RHEA:29951, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704;
CC         Evidence={ECO:0000250|UniProtKB:P0AFF2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + thymidine(in) = H(+)(out) + thymidine(out);
CC         Xref=Rhea:RHEA:29955, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748;
CC         Evidence={ECO:0000250|UniProtKB:P0AFF2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(in) + H(+)(in) = cytidine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29983, ChEBI:CHEBI:15378, ChEBI:CHEBI:17562;
CC         Evidence={ECO:0000250|UniProtKB:P0AFF2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine(in) + H(+)(in) = 2'-deoxycytidine(out) +
CC         H(+)(out); Xref=Rhea:RHEA:29975, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15698; Evidence={ECO:0000250|UniProtKB:P0AFF2};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AFF2}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC       (TC 2.A.41) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81382.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000376337.1; NC_004431.1.
DR   AlphaFoldDB; P0AFF3; -.
DR   SMR; P0AFF3; -.
DR   STRING; 199310.c2932; -.
DR   PRIDE; P0AFF3; -.
DR   EnsemblBacteria; AAN81382; AAN81382; c2932.
DR   GeneID; 66673737; -.
DR   KEGG; ecc:c2932; -.
DR   eggNOG; COG1972; Bacteria.
DR   HOGENOM; CLU_016813_0_0_6; -.
DR   OMA; WFFLNSN; -.
DR   Proteomes; UP000001410; 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:0005337; F:nucleoside transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR008276; C_nuclsd_transpt.
DR   InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR   InterPro; IPR011657; CNT_C_dom.
DR   InterPro; IPR002668; CNT_N_dom.
DR   InterPro; IPR011642; Gate_dom.
DR   PANTHER; PTHR10590; PTHR10590; 1.
DR   Pfam; PF07670; Gate; 1.
DR   Pfam; PF07662; Nucleos_tra2_C; 1.
DR   Pfam; PF01773; Nucleos_tra2_N; 1.
DR   TIGRFAMs; TIGR00804; nupC; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..400
FT                   /note="Nucleoside permease NupC"
FT                   /id="PRO_0000070455"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..36
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..168
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..250
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..341
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFF2"
SQ   SEQUENCE   400 AA;  43476 MW;  1EA1DE138C4351CE CRC64;
     MDRVLHFVLA LAVVAILALL VSSDRKKIRI RYVIQLLVIE VLLAWFFLNS DVGLGFVKGF
     SEMFEKLLGF ANEGTNFVFG SMNDQGLAFF FLKVLCPIVF ISALIGILQH IRVLPVIIRA
     IGFLLSKVNG MGKLESFNAV SSLILGQSEN FIAYKDILGK ISRNRMYTMA ATAMSTVSMS
     IVGAYMTMLE PKYVVAALVL NMFSTFIVLS LINPYRVDAS EENIQMSNLH EGQSFFEMLG
     EYILAGFKVA IIVAAMLIGF IALIAALNAL FATVTGWFGY SISFQGILGY IFYPIAWVMG
     VPSSEALQVG SIMATKLVSN EFVAMMDLQK IASTLSPRAE GIISVFLVSF ANFSSIGIIA
     GAVKGLNEEQ GNVVSRFGLK LVYGSTLVSV LSASIAALVL