PBUE_BACAM
ID PBUE_BACAM Reviewed; 386 AA.
AC Q0GQS6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Purine efflux pump PbuE;
GN Name=pbuE;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN EFFLUX PUMP, AND
RP INDUCTION.
RC STRAIN=DSM 1061 / JCM 20197 / IAM 1523 / K;
RX PubMed=17935948; DOI=10.1016/j.resmic.2007.08.003;
RA Zakataeva N.P., Gronskiy S.V., Sheremet A.S., Kutukova E.A., Novikova A.E.,
RA Livshits V.A.;
RT "A new function for the Bacillus PbuE purine base efflux pump: efflux of
RT purine nucleosides.";
RL Res. Microbiol. 158:659-665(2007).
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 and
CC 6-mercaptopurine. Therefore plays a role in maintaining the cellular
CC purine base pools and protecting cells against toxic purine base
CC analogs. Modulates expression of the purR and G-box regulons (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17935948}.
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. {ECO:0000269|PubMed:17935948}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC PbuE (TC 2.A.1.2.25) subfamily. {ECO:0000305}.
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DR EMBL; DQ662404; ABG49512.1; -; Genomic_DNA.
DR RefSeq; WP_013351164.1; NZ_VRTX01000015.1.
DR AlphaFoldDB; Q0GQS6; -.
DR SMR; Q0GQS6; -.
DR STRING; 692420.BAMF_0515; -.
DR eggNOG; COG2814; Bacteria.
DR OMA; SAHFTAY; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..386
FT /note="Purine efflux pump PbuE"
FT /id="PRO_0000367244"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
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..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..306
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 386 AA; 41014 MW; 462F65B8A293B0F7 CRC64;
MNFKVFLLAA STIAVGLVEL IVGGILPQIA SDLDISIVSA GQLISVFALG YAVSGPLLLA
VTAKAERKRL YLIALFVFFL SNLVAYFSPN FAVLMVSRVL ASMSTGLIVV LSLTIAPKIV
APEYRARAIG IIFMGFSSAI ALGVPVGIII SNAFGWRVLF LGIGVLSLVS MLIISVFFEK
IPAEKMIPFR EQIKTIGNAK IASAHLVTLF TLAGHYTLYA YFAPFLETTL HLSSVWVSVC
YFLFGLSAVC GGPFGGWLYD RLGSFKSIML VTVSFALILF ILPLSTVSLI VFLPAMVIWG
LLSWSLAPAQ QSYLIKIAPE SSDIQQSFNT SALQIGIALG SAIGGGVIGQ TGSVTATAWC
GGLIVIIAVS LAVFSLTRPA LKRKSA