PBUG_BACSU
ID PBUG_BACSU Reviewed; 440 AA.
AC O34987; Q79C44;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Guanine/hypoxanthine permease PbuG;
GN Name=pbuG; Synonyms=yebB; OrderedLocusNames=BSU06370;
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=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(1996).
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 PURINE UPTAKE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=3110131; DOI=10.1128/jb.169.7.2977-2983.1987;
RA Saxild H.H., Nygaard P.;
RT "Genetic and physiological characterization of Bacillus subtilis mutants
RT resistant to purine analogs.";
RL J. Bacteriol. 169:2977-2983(1987).
RN [4]
RP FUNCTION IN HYPOXANTHINE UPTAKE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11591660; DOI=10.1128/jb.183.21.6175-6183.2001;
RA Saxild H.H., Brunstedt K., Nielsen K.I., Jarmer H., Nygaard P.;
RT "Definition of the Bacillus subtilis PurR operator using genetic and
RT bioinformatic tools and expansion of the PurR regulon with glyA, guaC,
RT pbuG, xpt-pbuX, yqhZ-folD, and pbuO.";
RL J. Bacteriol. 183:6175-6183(2001).
RN [5]
RP 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).
CC -!- FUNCTION: Involved in the uptake of the purine bases hypoxanthine and
CC guanine. {ECO:0000269|PubMed:11591660, ECO:0000269|PubMed:3110131}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expression is regulated by both purR and xptR regulons.
CC Negatively regulated by hypoxanthine and guanine.
CC {ECO:0000269|PubMed:11591660, ECO:0000269|PubMed:12923093}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show normal growth on
CC inosine as the purine source, normal hypoxanthine-guanine
CC phosphoribosyltransferase activity, and are resistant to azaguanine.
CC {ECO:0000269|PubMed:11591660, ECO:0000269|PubMed:3110131}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
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DR EMBL; U51115; AAB62312.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12456.1; -; Genomic_DNA.
DR PIR; F69791; F69791.
DR RefSeq; NP_388518.1; NC_000964.3.
DR RefSeq; WP_003243780.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O34987; -.
DR SMR; O34987; -.
DR STRING; 224308.BSU06370; -.
DR TCDB; 2.A.40.7.2; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; O34987; -.
DR PRIDE; O34987; -.
DR DNASU; 936043; -.
DR EnsemblBacteria; CAB12456; CAB12456; BSU_06370.
DR GeneID; 936043; -.
DR KEGG; bsu:BSU06370; -.
DR PATRIC; fig|224308.179.peg.692; -.
DR eggNOG; COG2252; Bacteria.
DR InParanoid; O34987; -.
DR OMA; YVDIIDC; -.
DR PhylomeDB; O34987; -.
DR BioCyc; BSUB:BSU06370-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR026033; Azg-like_bact_archaea.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PIRSF; PIRSF005353; PbuG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..440
FT /note="Guanine/hypoxanthine permease PbuG"
FT /id="PRO_0000375868"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 440 AA; 46191 MW; 28605FC8249EA379 CRC64;
MKTFFQFDEL GTSYRNEIIG GLTTFLSMAY ILFVNPITLA LESVKDFPEA LRIDQGAVFT
ATALASAAGC ILMGLIARYP IAIAPGMGLN AFFAFSVVLG MGISWQAALS GVFISGLIFV
ALSLTGFREK IINAIPPELK LAVGAGIGLF ITFVGLQGSG IITANPSTLV TIGNIHSGPV
LLTIFGVIVT VILMVLRVNA GVFIGMLLTA VAGMIFGLVP VPTQIIGSVP SLAPTFGQAW
IHLPDIFSVQ MLIVILTFLF VGFFDTAGTL VAVATQAGLM KENKLPRAGR ALLADSSSIV
IGAVLGTSTT TSYVESSSGV AAGARSGFAA IVTGILFLLA TFFSPLLSVV TSNVTAPALI
IVGALMVAPL GKIAWDKFEV AVPAFLTMIM MPLTYSIATG IAIGFIFYPI TMVCKGKAKE
VHPIMYGLFV VFILYFIFLK
