ID   PNUC_SHIFL              Reviewed;         239 AA.
AC   P0AFK3; P31215; P77227;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Nicotinamide riboside transporter PnuC;
GN   Name=pnuC; OrderedLocusNames=SF0553, S0561;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Required for nicotinamide riboside transport across the inner
CC       membrane. {ECO:0000250|UniProtKB:Q57425}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q57425}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q57425}.
CC   -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake
CC       permease (TC 4.B.1) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005674; AAN42197.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16070.1; -; Genomic_DNA.
DR   RefSeq; NP_706490.1; NC_004337.2.
DR   RefSeq; WP_000345410.1; NZ_WPGW01000046.1.
DR   AlphaFoldDB; P0AFK3; -.
DR   SMR; P0AFK3; -.
DR   STRING; 198214.SF0553; -.
DR   EnsemblBacteria; AAN42197; AAN42197; SF0553.
DR   EnsemblBacteria; AAP16070; AAP16070; S0561.
DR   GeneID; 1023463; -.
DR   GeneID; 66670978; -.
DR   KEGG; sfl:SF0553; -.
DR   KEGG; sfx:S0561; -.
DR   PATRIC; fig|198214.7.peg.642; -.
DR   HOGENOM; CLU_076589_1_0_6; -.
DR   OMA; WPDAYIF; -.
DR   OrthoDB; 1301128at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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:0034257; F:nicotinamide riboside transmembrane transporter activity; IEA:InterPro.
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   3: Inferred from homology;
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_0000058489"
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:0000255"
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"
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