(data stored in ACNUC7421 zone)

SWISSPROT: NAIP_BACSU

ID   NAIP_BACSU              Reviewed;         400 AA.
AC   O34691;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Putative niacin/nicotinamide transporter NaiP;
GN   Name=naiP; Synonyms=yceI; OrderedLocusNames=BSU02950;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274031; DOI=10.1099/00221287-143-8-2775;
RA   Kumano M., Tamakoshi A., Yamane K.;
RT   "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT   gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT   identification of the site of the lin-2 mutation.";
RL   Microbiology 143:2775-2782(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   EXPRESSION IN E.COLI, POSSIBLE FUNCTION AS A NICOTINAMIDE TRANSPORTER, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18276644; DOI=10.1093/nar/gkn046;
RA   Rodionov D.A., Li X., Rodionova I.A., Yang C., Sorci L., Dervyn E.,
RA   Martynowski D., Zhang H., Gelfand M.S., Osterman A.L.;
RT   "Transcriptional regulation of NAD metabolism in bacteria: genomic
RT   reconstruction of NiaR (YrxA) regulon.";
RL   Nucleic Acids Res. 36:2032-2046(2008).
CC   -!- FUNCTION: Probably involved in the uptake of amidated and deamidated
CC       forms of niacin. Increases the growth rate of E.coli that is unable to
CC       make niacin de novo; confers increased sensitivity to the toxic niacin
CC       analog 6-amino-nicotinamide to wild-type E.coli. There is probably
CC       another mechanism for niacin uptake.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Partially reduces sensitivity to the toxic niacin
CC       analog 6-amino-nicotinamide. {ECO:0000269|PubMed:18276644}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. {ECO:0000305}.
DR   EMBL; AB000617; BAA22256.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12089.1; -; Genomic_DNA.
DR   PIR; C69757; C69757.
DR   RefSeq; NP_388177.1; NC_000964.3.
DR   RefSeq; WP_003246397.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU02950; -.
DR   TCDB; 2.A.1.82.4; the major facilitator superfamily (mfs).
DR   PaxDb; O34691; -.
DR   PRIDE; O34691; -.
DR   EnsemblBacteria; CAB12089; CAB12089; BSU02950.
DR   GeneID; 938365; -.
DR   KEGG; bsu:BSU02950; -.
DR   PATRIC; fig|224308.179.peg.307; -.
DR   eggNOG; ENOG41079KZ; Bacteria.
DR   eggNOG; ENOG410ZVDE; LUCA.
DR   HOGENOM; HOG000114540; -.
DR   InParanoid; O34691; -.
DR   KO; K08369; -.
DR   OMA; EYVLIMT; -.
DR   PhylomeDB; O34691; -.
DR   BioCyc; BSUB:BSU02950-MONOMER; -.
DR   Proteomes; UP000001570; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O34691.
DR   SWISS-2DPAGE; O34691.
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..400
FT                   /note="Putative niacin/nicotinamide transporter NaiP"
FT                   /id="PRO_0000050491"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..253
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..370
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..400
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  43709 MW;  E0AE0CEE5DD27395 CRC64;
     MGKQQPISQR KLLGVAGLGW LFDAMDVGIL SFIIAALHVE WNLSPEEMKW IGSVNSIGMA
     AGAFLFGLLA DRIGRKKVFI ITLLCFSIGS GISAFVTSLS AFLILRFVIG MGLGGELPVA
     STLVSEAVVP EKRGRVIVLL ESFWAVGWLA AALISYFVIP SFGWQAALLL TALTAFYALY
     LRTSLPDSPK YESLSAKKRS MWENVKSVWA RQYIRPTVML SIVWFCVVFS YYGMFLWLPS
     VMLLKGFSMI QSFEYVLLMT LAQLPGYFSA AWLIEKAGRK WILVVYLIGT AGSAYFFGTA
     DSLSLLLTAG VLLSFFNLGA WGVLYAYTPE QYPTAIRATG SGTTAAFGRI GGIFGPLLVG
     TLAARHISFS VIFSIFCIAI LLAVACILIM GKETKQTELE
//

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