ID   NUPN_BACSU              Reviewed;         359 AA.
AC   O05252;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=ABC transporter guanosine-binding protein NupN {ECO:0000305};
DE   Flags: Precursor;
GN   Name=nupN {ECO:0000303|PubMed:21926227}; Synonyms=yufN;
GN   OrderedLocusNames=BSU31540;
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=9274030; DOI=10.1099/00221287-143-8-2769;
RA   Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA   Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT   "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT   of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL   Microbiology 143:2769-2774(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   FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / SMY;
RX   PubMed=21926227; DOI=10.1128/jb.05899-11;
RA   Belitsky B.R., Sonenshein A.L.;
RT   "CodY-mediated regulation of guanosine uptake in Bacillus subtilis.";
RL   J. Bacteriol. 193:6276-6287(2011).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA   Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA   Ramamurthi K.S., Vlamakis H., Lopez D.;
RT   "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT   mutant involves the protease FtsH.";
RL   Mol. Microbiol. 86:457-471(2012).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in the uptake of
CC       guanosine (PubMed:21926227). Is probably the substrate-binding protein
CC       of the system (PubMed:21926227). May be a nucleoside transporter of
CC       broad specificity but with various affinities for different substrates
CC       (PubMed:21926227). {ECO:0000269|PubMed:21926227}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (NupO),
CC       two transmembrane proteins (NupP and NupQ) and a solute-binding protein
CC       (NupN). {ECO:0000305|PubMed:21926227}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:22882210}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}. Membrane raft
CC       {ECO:0000269|PubMed:22882210}. Note=Present in detergent-resistant
CC       membrane (DRM) fractions that may be equivalent to eukaryotic membrane
CC       rafts; these rafts include proteins involved in signaling, molecule
CC       trafficking and protein secretion. {ECO:0000269|PubMed:22882210}.
CC   -!- INDUCTION: Transcriptionally regulated by CodY.
CC       {ECO:0000269|PubMed:21926227}.
CC   -!- DISRUPTION PHENOTYPE: A null mutation does not lead to any detectable
CC       defect in guanosine uptake. However, in the nupG-nupN double mutant,
CC       guanosine uptake is reduced to an almost undetectable level.
CC       {ECO:0000269|PubMed:21926227}.
CC   -!- SIMILARITY: Belongs to the BMP lipoprotein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB07936.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z93937; CAB07936.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB15143.2; -; Genomic_DNA.
DR   PIR; C70009; C70009.
DR   RefSeq; NP_391032.2; NC_000964.3.
DR   RefSeq; WP_003228831.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O05252; -.
DR   SMR; O05252; -.
DR   STRING; 224308.BSU31540; -.
DR   PaxDb; O05252; -.
DR   PRIDE; O05252; -.
DR   DNASU; 938870; -.
DR   EnsemblBacteria; CAB15143; CAB15143; BSU_31540.
DR   GeneID; 938870; -.
DR   KEGG; bsu:BSU31540; -.
DR   PATRIC; fig|224308.179.peg.3419; -.
DR   eggNOG; COG1744; Bacteria.
DR   InParanoid; O05252; -.
DR   OMA; LASMMKR; -.
DR   PhylomeDB; O05252; -.
DR   BioCyc; BSUB:BSU31540-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR003760; PnrA-like.
DR   Pfam; PF02608; Bmp; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..359
FT                   /note="ABC transporter guanosine-binding protein NupN"
FT                   /id="PRO_0000018010"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   359 AA;  38361 MW;  738CE4BA43C2AD8B CRC64;
     MNKRKIGLAM SLVIAAGTIL GACGNSEKSS GSGEGKNKFS VAMVTDVGGV DDKSFNQSAW
     EGIQAFGKEN GLKKGKNGYD YLQSKSDADY TTNLNKLARE NFDLIYGVGY LMEDSISEIA
     DQRKNTNFAI IDAVVDKDNV ASITFKEQEG SFLVGVAAAL SSKSGKIGFV GGMESELIKK
     FEVGFRAGVQ AVNPKAVVEV KYAGGFDKAD VGKATAESMY KSGVDVIYHS AGATGTGVFT
     EAKNLKKEDP KRDVWVIGVD KDQYAEGQVE GTDDNVTLTS MVKKVDTVVE DVTKKASDGK
     FPGGETLTYG LDQDGVGISP SKQNLSDDVI KAVDKWKKKI IDGLEIPATE KELKTFKAE