ID   ARAG_GEOSE              Reviewed;         513 AA.
AC   Q9S472;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=L-arabinose transport ATP-binding protein AraG;
DE            EC=7.5.2.12;
GN   Name=araG;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T-6 / NCIMB 40222;
RA   Gilead-Gropper S., Shoham Y.;
RT   "The L-arabinose utilization gene cluster from Bacillus stearothermophilus
RT   T-6.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the binding-protein-dependent transport system for L-
CC       arabinose. Probably responsible for energy coupling to the transport
CC       system.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-arabinose(out) = ADP + H(+) + L-arabinose(in) +
CC         phosphate; Xref=Rhea:RHEA:30007, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17535, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.5.2.12;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AF160811; AAD45713.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S472; -.
DR   SMR; Q9S472; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015612; F:ABC-type L-arabinose transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW   Sugar transport; Translocase; Transport.
FT   CHAIN           1..513
FT                   /note="L-arabinose transport ATP-binding protein AraG"
FT                   /id="PRO_0000091935"
FT   DOMAIN          6..243
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          264..508
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   513 AA;  57160 MW;  182CDB7129B00290 CRC64;
     MSEFILEMRG ITKQFPGVKA LDNVNFKVRE GEIHALCGEN GAGKSTLMKV LSGVYPYGTY
     DGEIVFKGEV CKFKNIKQSE QLGIVIIHQE LALIPYLSIA ENIFLGNERA KKGIINWNET
     IAQTKKLLQK VGLEESPHTL VGQLGVGKQQ LVEIAKALAK DVKLLILDEP TAALNEDDSE
     NLLNLLLELK KQGLSAIIIS HKLNEITKVA DSITILRDGK TIETLDMKHD EVTEDRIIRG
     MVGRDLTNRY PARTPKIGEV IFEVKNWTVY HPIYSERKVL DHINLSIRRG EIVGIAGLMG
     AGRTELAMSI FGRSYGKKIS GEIWKNGVKI DVSDVSKAIA NGIAYVTEDR KGNGLILMED
     IRKNITLSRL GKISNHFVVD ENQEIVESER FRDQFKIKTP SVFQKVEALS GGNQQKVVLS
     KWIFAEPDIL ILDEPTRGID VGAKYEIYTI IQQLADAGKG ILMISSELPE ILGMCDRIYV
     MSEGRITGEV SREEATQEKL MRLMTKTAIQ EGA