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 11-DEC-2019, entry version 119. DE RecName: Full=L-arabinose transport system permease protein AraP; GN Name=araP; Synonyms=yseD; 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]. 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). CC -!- FUNCTION: Part of the binding-protein-dependent transport system for L- CC arabinose. Probably responsible for the translocation of the substrate CC across the membrane. 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}. 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 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; BSU28740. DR GeneID; 937432; -. DR KEGG; bsu:BSU28740; -. DR PATRIC; fig|224308.179.peg.3122; -. DR eggNOG; COG1175; LUCA. DR HOGENOM; HOG000220406; -. DR InParanoid; P94529; -. DR KO; K17235; -. DR OMA; IIATMQV; -. DR PhylomeDB; P94529; -. DR BioCyc; BSUB:BSU28740-MONOMER; -. 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 2: Evidence at transcript level; KW Cell membrane; Membrane; Reference proteome; Sugar transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..313 FT /note="L-arabinose transport system permease 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 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 //