PBUE_BACSU
ID PBUE_BACSU Reviewed; 388 AA.
AC Q797E3; O05504;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Purine efflux pump PbuE;
GN Name=pbuE; Synonyms=ydhL; OrderedLocusNames=BSU05800;
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=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(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 IN EFFLUX, AND INDUCTION.
RC STRAIN=168;
RX PubMed=12923093; DOI=10.1128/jb.185.17.5200-5209.2003;
RA Johansen L.E., Nygaard P., Lassen C., Agersoe Y., Saxild H.H.;
RT "Definition of a second Bacillus subtilis pur regulon comprising the pur
RT and xpt-pbuX operons plus pbuG, nupG (yxjA), and pbuE (ydhL).";
RL J. Bacteriol. 185:5200-5209(2003).
RN [4]
RP INDUCTION.
RX PubMed=14718920; DOI=10.1038/nsmb710;
RA Mandal M., Breaker R.R.;
RT "Adenine riboswitches and gene activation by disruption of a transcription
RT terminator.";
RL Nat. Struct. Mol. Biol. 11:29-35(2004).
RN [5]
RP FUNCTION AS AN EFFLUX PUMP, AND INDUCTION.
RC STRAIN=168;
RX PubMed=15629952; DOI=10.1128/jb.187.2.791-794.2005;
RA Nygaard P., Saxild H.H.;
RT "The purine efflux pump PbuE in Bacillus subtilis modulates expression of
RT the PurR and G-box (XptR) regulons by adjusting the purine base pool
RT size.";
RL J. Bacteriol. 187:791-794(2005).
CC -!- FUNCTION: Involved in the efflux of purine ribonucleosides, such as
CC guanosine, adenosine and inosine, as well as purine bases guanine,
CC adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine, 6-
CC mercaptopurine and 2-fluoroadenine. Therefore plays a role in
CC maintaining the cellular purine base pools and protecting cells against
CC toxic purine base analogs. Modulates expression of the purR and G-box
CC regulons. {ECO:0000269|PubMed:12923093, ECO:0000269|PubMed:15629952}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by adenine, via the adenine-dependent
CC riboswitch. Also up-regulated by hypoxanthine and guanine.
CC {ECO:0000269|PubMed:12923093, ECO:0000269|PubMed:14718920,
CC ECO:0000269|PubMed:15629952}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC PbuE (TC 2.A.1.2.25) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D88802; BAA19704.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12399.2; -; Genomic_DNA.
DR PIR; H69784; H69784.
DR RefSeq; NP_388461.2; NC_000964.3.
DR RefSeq; WP_003234105.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; Q797E3; -.
DR SMR; Q797E3; -.
DR STRING; 224308.BSU05800; -.
DR TCDB; 2.A.1.2.25; the major facilitator superfamily (mfs).
DR PaxDb; Q797E3; -.
DR EnsemblBacteria; CAB12399; CAB12399; BSU_05800.
DR GeneID; 937996; -.
DR KEGG; bsu:BSU05800; -.
DR PATRIC; fig|224308.179.peg.624; -.
DR eggNOG; COG2814; Bacteria.
DR InParanoid; Q797E3; -.
DR OMA; SAHFTAY; -.
DR PhylomeDB; Q797E3; -.
DR BioCyc; BSUB:BSU05800-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 Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..388
FT /note="Purine efflux pump PbuE"
FT /id="PRO_0000367245"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 41535 MW; 6639D1DA8FA3A690 CRC64;
MNFKVFLLAA STIAVGLVEL IVGGILPQIA NDLDISIVSA GQLISVFALG YAVSGPLLLA
LTAKIERKRL YLIALFVFFL SNLVAYFSPN FATLMVSRVL AAMSTGLIVV LSLTIAPKIV
APEYRARAIG IIFMGFSSAI ALGVPLGILI SDSFGWRILF LGIGLLALIS MLIISIFFER
IPAEKMIPFR EQLKTIGNLK IASSHLVTMF TLAGHYTLYA YFAPFLEETL HLSSFWVSIC
YFLFGISAVC GGPFGGALSD RLGSFKSILL VTGSFAIIMF LLPLSTSSMI FFLPVMVIWG
LLSWSLAPAQ QSYLIEIAPD SSDIQQSFNT SALQVGIALG SAIGGVVLDQ TGTVVSTAWC
GGSIVIIAVL FAFISLTRPV QTAKKSSL
