ARAE_BACSU
ID ARAE_BACSU Reviewed; 464 AA.
AC P96710;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Arabinose-proton symporter {ECO:0000305};
DE AltName: Full=Arabinose transporter {ECO:0000305};
GN Name=araE; Synonyms=yvbR; OrderedLocusNames=BSU33960;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-223.
RC STRAIN=168;
RX PubMed=9045819; DOI=10.1128/jb.179.5.1598-1608.1997;
RA Sa-Nogueira I.M.G., Mota L.J.;
RT "Negative regulation of L-arabinose metabolism in Bacillus subtilis:
RT characterization of the araR (araC) gene.";
RL J. Bacteriol. 179:1598-1608(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-464, AND FUNCTION.
RC STRAIN=168;
RX PubMed=9401028; DOI=10.1128/jb.179.24.7705-7711.1997;
RA Sa-Nogueira I., Ramos S.S.;
RT "Cloning, functional analysis, and transcriptional regulation of the
RT Bacillus subtilis araE gene involved in L-arabinose utilization.";
RL J. Bacteriol. 179:7705-7711(1997).
RN [4]
RP FUNCTION IN D-GALACTOSE AND D-XYLOSE IMPORT.
RX PubMed=9620981; DOI=10.1128/jb.180.12.3250-3252.1998;
RA Krispin O., Allmansberger R.;
RT "The Bacillus subtilis AraE protein displays a broad substrate specificity
RT for several different sugars.";
RL J. Bacteriol. 180:3250-3252(1998).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT Bacillus subtilis.";
RL Mol. Microbiol. 33:476-489(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20693325; DOI=10.1128/jb.00832-10;
RA Ferreira M.J., Sa-Nogueira I.D.;
RT "A multitask ATPase serving different ABC-type sugar importers in Bacillus
RT subtilis.";
RL J. Bacteriol. 192:5312-5318(2010).
CC -!- FUNCTION: Uptake of L-arabinose across the cytoplasmic membrane with
CC the concomitant transport of protons into the cell (symport system)
CC (PubMed:9401028). In the presence of inducing amounts of L-arabinose,
CC can import both D-galactose and D-xylose (PubMed:9620981). Can also
CC transport the disaccharide alpha-1,5-arabinobiose (PubMed:20693325).
CC {ECO:0000269|PubMed:20693325, ECO:0000269|PubMed:9401028,
CC ECO:0000269|PubMed:9620981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-arabinose(in) = H(+)(out) + L-arabinose(out);
CC Xref=Rhea:RHEA:28951, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535;
CC Evidence={ECO:0000305|PubMed:9401028};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28953;
CC Evidence={ECO:0000305|PubMed:9401028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) + H(+)(in) = D-galactose(out) + H(+)(out);
CC Xref=Rhea:RHEA:29019, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000305|PubMed:9620981};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29021;
CC Evidence={ECO:0000305|PubMed:9620981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose(in) + H(+)(in) = D-xylose(out) + H(+)(out);
CC Xref=Rhea:RHEA:28959, ChEBI:CHEBI:15378, ChEBI:CHEBI:53455;
CC Evidence={ECO:0000305|PubMed:9620981};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28961;
CC Evidence={ECO:0000305|PubMed:9620981};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Transcription is repressed by the binding of AraR to the
CC promoter. L-arabinose acts as an inducer by inhibiting the binding of
CC AraR to the DNA, thus allowing expression of the gene.
CC {ECO:0000269|PubMed:10417639}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect growth on
CC glucose, but the mutant cannot grow in the presence of arabinose.
CC Deletion has a negative effect on the ability of the mutant to grow on
CC alpha-1,5-arabinobiose. AraE/araN double mutant is unable to grow in
CC the presence of alpha-1,5-arabinobiose. {ECO:0000269|PubMed:20693325}.
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; AL009126; CAB15401.1; -; Genomic_DNA.
DR EMBL; X98354; CAA66998.1; -; Genomic_DNA.
DR EMBL; Y12105; CAA72812.1; -; Genomic_DNA.
DR PIR; F69587; F69587.
DR RefSeq; NP_391276.1; NC_000964.3.
DR RefSeq; WP_003243899.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P96710; -.
DR SMR; P96710; -.
DR STRING; 224308.BSU33960; -.
DR TCDB; 2.A.1.1.55; the major facilitator superfamily (mfs).
DR PaxDb; P96710; -.
DR EnsemblBacteria; CAB15401; CAB15401; BSU_33960.
DR GeneID; 938567; -.
DR KEGG; bsu:BSU33960; -.
DR PATRIC; fig|224308.179.peg.3682; -.
DR eggNOG; COG2814; Bacteria.
DR InParanoid; P96710; -.
DR OMA; WNCILAF; -.
DR PhylomeDB; P96710; -.
DR BioCyc; BSUB:BSU33960-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..464
FT /note="Arabinose-proton symporter"
FT /id="PRO_0000050288"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 464 AA; 50411 MW; 13B417061CB61DA2 CRC64;
MKNTPTQLEP NVPVTRSHSM GFVILISCAA GLGGLLYGYD TAVISGAIGF LKDLYSLSPF
MEGLVISSIM IGGVVGVGIS GFLSDRFGRR KILMTAALLF AISAIVSALS QDVSTLIIAR
IIGGLGIGMG SSLSVTYITE AAPPAIRGSL SSLYQLFTIL GISATYFINL AVQRSGTYEW
GVHTGWRWML AYGMVPSVIF FLVLLVVPES PRWLAKAGKT NEALKILTRI NGETVAKEEL
KNIENSLKIE QMGSLSQLFK PGLRKALVIG ILLALFNQVI GMNAITYYGP EIFKMMGFGQ
NAGFVTTCIV GVVEVIFTVI AVLLIDKVGR KKLMSIGSAF MAIFMILIGT SFYFELTSGI
MMIVLILGFV AAFCVSVGPI TWIMISEIFP NHLRARAAGI ATIFLWGANW AIGQFVPMMI
DSFGLAYTFW IFAVINILCF LFVVTICPET KNKSLEEIEK LWIK
