ID ARAP_BACSU Reviewed; 313 AA. AC P94529; O05094; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 03-AUG-2022, entry version 129. DE RecName: Full=Arabinooligosaccharides transport system permease protein AraP {ECO:0000305}; GN Name=araP {ECO:0000303|PubMed:9084180}; Synonyms=yseD; GN OrderedLocusNames=BSU28740; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION. RC STRAIN=168; RX PubMed=9084180; DOI=10.1099/00221287-143-3-957; RA Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.; RT "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, RT genetic organization and expression."; RL Microbiology 143:957-969(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067; RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., RA Emmerson P.T., Harwood C.R.; RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis RT chromosome containing genes responsible for stress responses, the RT utilization of plant cell walls and primary metabolism."; RL Microbiology 142:3067-3078(1996). RN [3] 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 [4] 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 [5] RP FUNCTION, AND SUBUNIT. 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). RN [6] RP MUTAGENESIS OF GLU-205; GLU-208 AND ASP-213. RX PubMed=29240795; DOI=10.1371/journal.pone.0189483; RA Ferreira M.J., Mendes A.L., de Sa-Nogueira I.; RT "The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus RT subtilis."; RL PLoS ONE 12:e0189483-e0189483(2017). CC -!- FUNCTION: Part of the ABC transporter complex AraNPQ involved in the CC uptake of arabinooligosaccharides. Transports alpha-1,5- CC arabinooligosaccharides, at least up to four L-arabinosyl units CC (PubMed:20693325). Responsible for the translocation of the substrate CC across the membrane (Probable). {ECO:0000269|PubMed:20693325, CC ECO:0000305|PubMed:20693325}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX), CC two transmembrane proteins (AraP and AraQ) and a solute-binding protein CC (AraN). {ECO:0000269|PubMed:20693325}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- INDUCTION: Transcription is repressed by glucose and by the binding of CC AraR to the operon promoter. L-arabinose acts as an inducer by CC inhibiting the binding of AraR to the DNA, thus allowing expression of CC the gene. {ECO:0000269|PubMed:10417639, ECO:0000269|PubMed:9084180}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system CC permease family. MalFG subfamily. {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; X89810; CAA61935.1; -; Genomic_DNA. DR EMBL; Z75208; CAA99593.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14834.1; -; Genomic_DNA. DR PIR; B69588; B69588. DR RefSeq; NP_390752.1; NC_000964.3. DR RefSeq; WP_003229507.1; NZ_JNCM01000036.1. DR AlphaFoldDB; P94529; -. DR SMR; P94529; -. DR STRING; 224308.BSU28740; -. DR TCDB; 3.A.1.1.34; the atp-binding cassette (abc) superfamily. DR PaxDb; P94529; -. DR PRIDE; P94529; -. DR EnsemblBacteria; CAB14834; CAB14834; BSU_28740. DR GeneID; 937432; -. DR KEGG; bsu:BSU28740; -. DR PATRIC; fig|224308.179.peg.3122; -. DR eggNOG; COG1175; Bacteria. DR InParanoid; P94529; -. DR OMA; CSFPFVM; -. DR PhylomeDB; P94529; -. DR BioCyc; BSUB:BSU28740-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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR CDD; cd06261; TM_PBP2; 1. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR035906; MetI-like_sf. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 1: Evidence at protein level; KW Cell membrane; Membrane; Reference proteome; Sugar transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..313 FT /note="Arabinooligosaccharides transport system permease FT protein AraP" FT /id="PRO_0000059954" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 91..111 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 224..244 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 281..301 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 87..302 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT MUTAGEN 205 FT /note="E->A: Has no effect on the growth rate." FT /evidence="ECO:0000269|PubMed:29240795" FT MUTAGEN 208 FT /note="E->A: Small negative impact in the uptake of FT arabinotriose. Shows an increase of about 10% in the FT doubling time." FT /evidence="ECO:0000269|PubMed:29240795" FT MUTAGEN 213 FT /note="D->A: Severely impairs the uptake of arabinotriose. FT Shows a 3.6-fold increase of the doubling time." FT /evidence="ECO:0000269|PubMed:29240795" FT CONFLICT 186 FT /note="R -> K (in Ref. 1; CAA61935)" FT /evidence="ECO:0000305" SQ SEQUENCE 313 AA; 35035 MW; F140CF2D7566F5A7 CRC64; MKPVKTGTVH PVPSAAKQSG WRDLFYSKKA APYLFTAPFV LSFLVFFLYP IISVFIMSFQ RILPGEVSFV GLSNYTALNN PTFYTALWNT LEYTFWTLIV LIPVPLLLAI FLNSKLVKFR NIFKSALFIP ALTSTIVAGI IFRLIFGEME TSLANSILLK LGFSPQNWMN NEHTGMFLMV LLASWRWMGI NILYFLAGLQ NVPKELYEAA DIDGANTMKK FLHITLPFLK PVTVYVLTIS IIGGFRMFEE SYVLWQNNSP GNIGLTLVGY LYQQGLAYNE MGYGAAIGIV LLIVILVVSL ISLKLSGSFK GEG //