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 03-AUG-2022, entry version 129.
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}.
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; 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 AlphaFoldDB; O34691; -.
DR SMR; O34691; -.
DR STRING; 224308.BSU02950; -.
DR TCDB; 2.A.1.82.4; the major facilitator superfamily (mfs).
DR PaxDb; O34691; -.
DR EnsemblBacteria; CAB12089; CAB12089; BSU_02950.
DR GeneID; 938365; -.
DR KEGG; bsu:BSU02950; -.
DR PATRIC; fig|224308.179.peg.307; -.
DR eggNOG; COG0477; Bacteria.
DR InParanoid; O34691; -.
DR OMA; EIFPTKD; -.
DR PhylomeDB; O34691; -.
DR BioCyc; BSUB:BSU02950-MON; -.
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 Gene3D; 1.20.1250.20; -; 2.
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;
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
