ARAP_BACSU
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}.
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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
