NUPC_ECOLI
ID NUPC_ECOLI Reviewed; 400 AA.
AC P0AFF2; P33031; P77236;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Nucleoside permease NupC {ECO:0000305};
DE AltName: Full=Nucleoside-transport system protein NupC {ECO:0000305};
GN Name=nupC {ECO:0000303|PubMed:374403}; Synonyms=cru;
GN OrderedLocusNames=b2393, JW2389;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=8022285; DOI=10.1111/j.1365-2958.1994.tb00392.x;
RA Craig J.E., Zhang Y., Gallagher M.P.;
RT "Cloning of the nupC gene of Escherichia coli encoding a nucleoside
RT transport system, and identification of an adjacent insertion element, IS
RT 186.";
RL Mol. Microbiol. 11:1159-1168(1994).
RN [2]
RP SEQUENCE REVISION TO 15.
RA Witzemann V.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=374403; DOI=10.1016/s0021-9258(18)50647-5;
RA Munch-Petersen A., Mygind B., Nicolaisen A., Pihl N.J.;
RT "Nucleoside transport in cells and membrane vesicles from Escherichia coli
RT K12.";
RL J. Biol. Chem. 254:3730-3737(1979).
RN [7]
RP FUNCTION.
RX PubMed=11466294; DOI=10.1128/jb.183.16.4900-4904.2001;
RA Noerholm M.H., Dandanell G.;
RT "Specificity and topology of the Escherichia coli xanthosine permease, a
RT representative of the NHS subfamily of the major facilitator superfamily.";
RL J. Bacteriol. 183:4900-4904(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14668133; DOI=10.1080/0968768031000140836;
RA Loewen S.K., Yao S.Y., Slugoski M.D., Mohabir N.N., Turner R.J.,
RA Mackey J.R., Weiner J.H., Gallagher M.P., Henderson P.J., Baldwin S.A.,
RA Cass C.E., Young J.D.;
RT "Transport of physiological nucleosides and anti-viral and anti-neoplastic
RT nucleoside drugs by recombinant Escherichia coli nucleoside-H(+)
RT cotransporter (NupC) produced in Xenopus laevis oocytes.";
RL Mol. Membr. Biol. 21:1-10(2004).
RN [9]
RP FUNCTION.
RX PubMed=15678184; DOI=10.1039/b414739a;
RA Patching S.G., Baldwin S.A., Baldwin A.D., Young J.D., Gallagher M.P.,
RA Henderson P.J., Herbert R.B.;
RT "The nucleoside transport proteins, NupC and NupG, from Escherichia coli:
RT specific structural motifs necessary for the binding of ligands.";
RL Org. Biomol. Chem. 3:462-470(2005).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Nucleoside transport protein that can transport adenosine,
CC uridine, thymidine, cytidine and deoxycytidine (PubMed:374403,
CC PubMed:11466294, PubMed:14668133, PubMed:15678184). Shows weak activity
CC with inosine and xanthosine (PubMed:11466294, PubMed:14668133).
CC Transport is driven by a proton motive force (PubMed:374403,
CC PubMed:14668133). Does not transport guanosine, deoxyguanosine,
CC hypoxanthine or uracil (PubMed:374403, PubMed:14668133). Also shows
CC activity with the chemotherapeutic drugs 3'-azido-3'-deoxythymidine
CC (AZT), 2',3'- dideoxycytidine (ddC) and 2'-deoxy-2',2'-difluorocytidine
CC (gemcitabine) (PubMed:14668133). {ECO:0000269|PubMed:11466294,
CC ECO:0000269|PubMed:14668133, ECO:0000269|PubMed:15678184,
CC ECO:0000269|PubMed:374403}.
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:0000269|PubMed:14668133};
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:0000269|PubMed:14668133, ECO:0000269|PubMed:374403};
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:0000269|PubMed:14668133};
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:0000269|PubMed:14668133, ECO:0000269|PubMed:374403};
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:0000269|PubMed:374403};
CC -!- ACTIVITY REGULATION: Transport is inhibited by the proton uncoupler
CC dinitrophenol (PubMed:374403). Inhibited by the nucleoside antibiotic
CC showdomycin (PubMed:374403). {ECO:0000269|PubMed:374403}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for uridine (at pH 5.5) {ECO:0000269|PubMed:14668133};
CC KM=10 uM for uridine (at pH 6.5) {ECO:0000269|PubMed:14668133};
CC KM=15 uM for uridine (at pH 7.5) {ECO:0000269|PubMed:14668133};
CC KM=44 uM for uridine (at pH 8.5) {ECO:0000269|PubMed:14668133};
CC KM=1.6 uM for adenosine (at pH 5.5) {ECO:0000269|PubMed:14668133};
CC KM=112 uM for AZT (at pH 5.5) {ECO:0000269|PubMed:14668133};
CC KM=130 uM for ddC (at pH 5.5) {ECO:0000269|PubMed:14668133};
CC KM=6.3 uM for gemcitabine (at pH 5.5) {ECO:0000269|PubMed:14668133};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:8022285}; Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Binding of nucleosides to NupC requires the presence of
CC hydroxyl groups at the C-3' position of ribose.
CC {ECO:0000269|PubMed:15678184}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; X74825; CAA52821.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75452.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16263.1; -; Genomic_DNA.
DR PIR; F65013; F65013.
DR RefSeq; NP_416894.1; NC_000913.3.
DR RefSeq; WP_000376337.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0AFF2; -.
DR SMR; P0AFF2; -.
DR BioGRID; 4259184; 18.
DR STRING; 511145.b2393; -.
DR TCDB; 2.A.41.1.1; the concentrative nucleoside transporter (cnt) family.
DR jPOST; P0AFF2; -.
DR PaxDb; P0AFF2; -.
DR PRIDE; P0AFF2; -.
DR EnsemblBacteria; AAC75452; AAC75452; b2393.
DR EnsemblBacteria; BAA16263; BAA16263; BAA16263.
DR GeneID; 66673737; -.
DR GeneID; 946895; -.
DR KEGG; ecj:JW2389; -.
DR KEGG; eco:b2393; -.
DR PATRIC; fig|1411691.4.peg.4336; -.
DR EchoBASE; EB1914; -.
DR eggNOG; COG1972; Bacteria.
DR HOGENOM; CLU_016813_0_0_6; -.
DR InParanoid; P0AFF2; -.
DR OMA; WFFLNSN; -.
DR PhylomeDB; P0AFF2; -.
DR BioCyc; EcoCyc:NUPC-MON; -.
DR BioCyc; MetaCyc:NUPC-MON; -.
DR PRO; PR:P0AFF2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015506; F:nucleoside:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:1901642; P:nucleoside transmembrane transport; IMP:EcoliWiki.
DR GO; GO:0015858; P:nucleoside transport; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..400
FT /note="Nucleoside permease NupC"
FT /id="PRO_0000070454"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..36
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..168
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..250
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..341
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 82
FT /note="Missing (in Ref. 1; CAA52821)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> AE (in Ref. 1; CAA52821)"
FT /evidence="ECO:0000305"
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
