PNUC_NEIMU
ID PNUC_NEIMU Reviewed; 263 AA.
AC D2ZZC1;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Nicotinamide riboside transporter PnuC {ECO:0000305};
GN Name=pnuC {ECO:0000312|EMBL:EFC87623.1};
GN ORFNames=NEIMUCOT_05996 {ECO:0000312|EMBL:EFC87623.1};
OS Neisseria mucosa.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25996 {ECO:0000312|EMBL:EFC87623.1};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4QTN}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 28-263 IN COMPLEX WITH
RP NICOTINAMIDE RIBOSIDE, SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
RX PubMed=25291599; DOI=10.1038/nsmb.2909;
RA Jaehme M., Guskov A., Slotboom D.J.;
RT "Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET
RT homolog.";
RL Nat. Struct. Mol. Biol. 21:1013-1015(2014).
CC -!- FUNCTION: Required for nicotinamide riboside transport across the inner
CC membrane. {ECO:0000250|UniProtKB:Q57425}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:25291599}.
CC -!- INTERACTION:
CC D2ZZC1; D2ZZC1: pnuC; NbExp=3; IntAct=EBI-16123343, EBI-16123343;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:25291599}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25291599}.
CC -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake
CC permease (TC 4.B.1) family. {ECO:0000305}.
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DR EMBL; ACDX02000017; EFC87623.1; -; Genomic_DNA.
DR PDB; 4QTN; X-ray; 2.80 A; A/B/C=28-263.
DR PDBsum; 4QTN; -.
DR AlphaFoldDB; D2ZZC1; -.
DR SMR; D2ZZC1; -.
DR DIP; DIP-61055N; -.
DR EnsemblBacteria; EFC87623; EFC87623; NEIMUCOT_05996.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0034257; F:nicotinamide riboside transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
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 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..263
FT /note="Nicotinamide riboside transporter PnuC"
FT /id="PRO_0000432586"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 62
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 84..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 108..109
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 132..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 178..180
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 202..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 227..232
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25291599"
FT TOPO_DOM 254..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 124
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0007744|PDB:4QTN"
FT BINDING 196
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0007744|PDB:4QTN"
FT BINDING 210
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0007744|PDB:4QTN"
FT BINDING 214
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0007744|PDB:4QTN"
FT BINDING 242
FT /ligand="beta-nicotinamide D-riboside"
FT /ligand_id="ChEBI:CHEBI:15927"
FT /evidence="ECO:0007744|PDB:4QTN"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 42..61
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4QTN"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 153..175
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 206..226
FT /evidence="ECO:0007829|PDB:4QTN"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4QTN"
FT HELIX 233..259
FT /evidence="ECO:0007829|PDB:4QTN"
SQ SEQUENCE 263 AA; 29908 MW; EFFE201F5C0EB43F CRC64;
MQYGMDSFGL RGIPHQVFIK KKEGKIMSLA WWKRELFGGW THFEAVWLLM FLGIQAVVFV
FNPDSWLASV AAVTGILCVV FVGKGKISNY LFGLISVSLY AYVSYTFKLY GEMMLNLLVY
VPVQFVGFAM WRKHMALGET AETEEVKAKA LTVRQWLLVV AASVVGTSVY IEWLHHLGSA
LPTLDGVTVV VSIVAQVLMI LRYREQWALW IVVNILTISL WAVAWFKNGE TSLPLLLMYV
MYLCNSVYGY INWTKLVKRH SGQ
