PNUC_ECOLI
ID PNUC_ECOLI Reviewed; 239 AA.
AC P0AFK2; P31215; P77227;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nicotinamide riboside transporter PnuC;
GN Name=pnuC; OrderedLocusNames=b0751, JW0734;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 1-66.
RX PubMed=2841129; DOI=10.1111/j.1432-1033.1988.tb14187.x;
RA Flachmann R., Kunz N., Seifert J., Guetlich M., Wientjes F.-J., Laeufer A.,
RA Gassen H.G.;
RT "Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli.
RT Cloning and characterization of quinolinate synthesis genes nadA and
RT nadB.";
RL Eur. J. Biochem. 175:221-228(1988).
RN [5]
RP IDENTIFICATION.
RX PubMed=2198247; DOI=10.1128/jb.172.8.4187-4196.1990;
RA Foster J.W., Park Y.K., Penfound T., Fenger T., Spector M.P.;
RT "Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence
RT analysis of the bifunctional nadR regulator and the nadA-pnuC operon.";
RL J. Bacteriol. 172:4187-4196(1990).
RN [6]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=15561822; DOI=10.1128/aac.48.12.4532-4541.2004;
RA Sauer E., Merdanovic M., Mortimer A.P., Bringmann G., Reidl J.;
RT "PnuC and the utilization of the nicotinamide riboside analog 3-
RT aminopyridine in Haemophilus influenzae.";
RL Antimicrob. Agents Chemother. 48:4532-4541(2004).
RN [7]
RP 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).
CC -!- FUNCTION: Required for nicotinamide riboside transport across the inner
CC membrane. {ECO:0000269|PubMed:15561822}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15561822}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15561822, ECO:0000305|PubMed:15919996}.
CC -!- INDUCTION: Repressed by NadR.
CC -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake
CC permease (TC 4.B.1) family. {ECO:0000305}.
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DR EMBL; U00096; AAC73838.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35413.1; -; Genomic_DNA.
DR EMBL; X12713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64810; G64810.
DR RefSeq; NP_415272.1; NC_000913.3.
DR RefSeq; WP_000345410.1; NZ_STEB01000028.1.
DR AlphaFoldDB; P0AFK2; -.
DR SMR; P0AFK2; -.
DR BioGRID; 4259938; 8.
DR STRING; 511145.b0751; -.
DR PaxDb; P0AFK2; -.
DR PRIDE; P0AFK2; -.
DR EnsemblBacteria; AAC73838; AAC73838; b0751.
DR EnsemblBacteria; BAA35413; BAA35413; BAA35413.
DR GeneID; 66670978; -.
DR GeneID; 945350; -.
DR KEGG; ecj:JW0734; -.
DR KEGG; eco:b0751; -.
DR PATRIC; fig|1411691.4.peg.1528; -.
DR EchoBASE; EB1651; -.
DR eggNOG; COG3201; Bacteria.
DR HOGENOM; CLU_076589_1_0_6; -.
DR InParanoid; P0AFK2; -.
DR OMA; WPDAYIF; -.
DR PhylomeDB; P0AFK2; -.
DR BioCyc; EcoCyc:PNUC-MON; -.
DR BioCyc; MetaCyc:PNUC-MON; -.
DR PRO; PR:P0AFK2; -.
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:0034257; F:nicotinamide riboside transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0034258; P:nicotinamide riboside transport; IDA:EcoCyc.
DR InterPro; IPR006419; NMN_transpt_PnuC.
DR PANTHER; PTHR36122; PTHR36122; 1.
DR Pfam; PF04973; NMN_transporter; 1.
DR TIGRFAMs; TIGR01528; NMN_trans_PnuC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..239
FT /note="Nicotinamide riboside transporter PnuC"
FT /id="PRO_0000058488"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..109
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..183
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT BINDING 188
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0000250|UniProtKB:D2ZZC1"
FT BINDING 192
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0000250|UniProtKB:D2ZZC1"
FT CONFLICT 6..7
FT /note="VQ -> TH (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="V -> I (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26996 MW; 5A01FC261A16CF61 CRC64;
MDFFSVQNIL VHIPIGAGGY DLSWIEAVGT IAGLLCIGLA SLEKISNYFF GLINVTLFGI
IFFQIQLYAS LLLQVFFFAA NIYGWYAWSR QTSQNEAELK IRWLPLPKAL SWLAVCVVSI
GLMTVFINPV FAFLTRVAVM IMQALGLQVV MPELQPDAFP FWDSCMMVLS IVAMILMTRK
YVENWLLWVI INVISVVIFA LQGVYAMSLE YIILTFIALN GSRMWINSAR ERGSRALSH
