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 15-MAR-2017, entry version 106. 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 RT subtilis chromosome containing genes responsible for stress responses, RT the 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., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 RT in Bacillus subtilis."; RL Mol. Microbiol. 33:476-489(1999). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for L-arabinose. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- INDUCTION: Transcription is repressed by glucose and by the CC binding of AraR to the operon promoter. L-arabinose acts as an CC inducer by inhibiting the binding of AraR to the DNA, thus CC allowing expression of the gene. {ECO:0000269|PubMed:10417639}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system 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 ProteinModelPortal; P94529; -. DR STRING; 224308.Bsubs1_010100015691; -. DR TCDB; 3.A.1.1.34; the atp-binding cassette (abc) superfamily. DR PaxDb; P94529; -. DR EnsemblBacteria; CAB14834; CAB14834; BSU28740. DR GeneID; 937432; -. DR KEGG; bsu:BSU28740; -. DR PATRIC; 18977640; VBIBacSub10457_3008. DR eggNOG; COG1175; LUCA. DR HOGENOM; HOG000220406; -. DR InParanoid; P94529; -. DR KO; K17235; -. DR OMA; VIMLLHI; -. 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 CDD; cd06261; TM_PBP2; 1. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. 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; Complete proteome; Membrane; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 313 L-arabinose transport system permease FT protein AraP. FT /FTId=PRO_0000059954. FT TRANSMEM 39 59 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 91 111 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 126 146 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 176 196 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 224 244 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 281 301 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 87 302 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT CONFLICT 186 186 R -> K (in Ref. 1; CAA61935). FT {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 //