ARAN_BACSU
ID ARAN_BACSU Reviewed; 433 AA.
AC P94528; O05093;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Arabinooligosaccharide-binding protein {ECO:0000305};
DE Flags: Precursor;
GN Name=araN {ECO:0000303|PubMed:9084180}; Synonyms=yseC;
GN OrderedLocusNames=BSU28750;
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 SEQUENCE REVISION TO 42.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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, SUBUNIT, 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: 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). AraN captures the substrate and delivers it to the
CC two transmembrane components (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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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 -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect growth on
CC glucose and arabinose, but it has a negative effect on the ability of
CC the mutant to grow on the alpha-1,5-arabinose oligomers alpha-1,5-
CC arabinobiose, alpha-1,5-arabinotriose and alpha-1,5-arabinotetraose.
CC AraE/araN double mutant is unable to grow in the presence of alpha-1,5-
CC arabinobiose. {ECO:0000269|PubMed:20693325}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {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; CAA61934.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99592.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14835.2; -; Genomic_DNA.
DR PIR; A69588; A69588.
DR RefSeq; NP_390753.2; NC_000964.3.
DR RefSeq; WP_004399072.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94528; -.
DR SMR; P94528; -.
DR STRING; 224308.BSU28750; -.
DR TCDB; 3.A.1.1.34; the atp-binding cassette (abc) superfamily.
DR PaxDb; P94528; -.
DR PRIDE; P94528; -.
DR EnsemblBacteria; CAB14835; CAB14835; BSU_28750.
DR GeneID; 937433; -.
DR KEGG; bsu:BSU28750; -.
DR PATRIC; fig|224308.179.peg.3123; -.
DR eggNOG; COG1653; Bacteria.
DR InParanoid; P94528; -.
DR OMA; WVSAVWA; -.
DR PhylomeDB; P94528; -.
DR BioCyc; BSUB:BSU28750-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR006059; SBP.
DR Pfam; PF01547; SBP_bac_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..433
FT /note="Arabinooligosaccharide-binding protein"
FT /id="PRO_0000031689"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 42
FT /note="N -> S (in Ref. 2; CAA99592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 48674 MW; 7BD6B69B40B19086 CRC64;
MKKMTVCFLV LMMLLTLVIA GCSAEKSSGK SGETELTFWT FNGLHEQFYV EMVKEWNKKY
PDRKIKLNTV VYPYGQMHDN LSISLIAGEG VPDIADVELA RFSNFLKGSD IPLADLTPLI
EKDRDKFVEA RLTLYSKNGK LYGLDTHVGT TVMFYNMDVM KKAGVNPDDI KTWDDYHKAG
QKVRKVTGKP MGTVETNDSA TFLSMISQQN SGYFDKNGKL ILNNDTNVKT LQYLKDMIND
KTMIPAPGGG HHSEEYYGFM NQGGAASVLM PIWYMGRFID YMPDLKGKIA IRPLPAWKEG
GDRSAGLGGT ATVVPKQSKH VELAKEFLAF AKGSEEGNKK LWSVLGFDPL RWDVWSSKEL
KEKNKYTDYF QNGTGIFSVL LDIKDEINPI YLHEDFAKAS DLVNRSVLFD ALKSQQKTPK
QALDRAAGEL KQK
