ID   ARAG_AZOBR              Reviewed;         520 AA.
AC   Q1JUP7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Arabinose import ATP-binding protein AraG {ECO:0000255|HAMAP-Rule:MF_01721};
DE            EC=7.5.2.12 {ECO:0000255|HAMAP-Rule:MF_01721};
GN   Name=araG {ECO:0000255|HAMAP-Rule:MF_01721}; Synonyms=araY;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA   Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT   "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT   3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT   alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT   into sugar metabolism.";
RL   J. Biol. Chem. 281:33521-33536(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in L-
CC       arabinose import. Responsible for energy coupling to the transport
CC       system (Probable). {ECO:0000305}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01721};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (AraG),
CC       two transmembrane proteins (AraH) and a solute-binding protein (AraF).
CC       {ECO:0000255|HAMAP-Rule:MF_01721}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01721}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01721}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Arabinose
CC       importer (TC 3.A.1.2.2) family. {ECO:0000255|HAMAP-Rule:MF_01721}.
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DR   EMBL; AB241136; BAE94273.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1JUP7; -.
DR   SMR; Q1JUP7; -.
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   GO; GO:0042882; P:L-arabinose transmembrane transport; IGC:UniProtKB.
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; IPR017917; ABC_transptr_Ara_ATP-bd_AraG.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43790:SF6; PTHR43790:SF6; 1.
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.
DR   PROSITE; PS51268; ARAG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..520
FT                   /note="Arabinose import ATP-binding protein AraG"
FT                   /id="PRO_0000270454"
FT   DOMAIN          30..265
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT   DOMAIN          265..516
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ   SEQUENCE   520 AA;  55986 MW;  C4E68047974A73A1 CRC64;
     MTTQTMTAVS GNDGDTGGDA AESPPGGPLL ALDGITVTFP GVRALDAVSL SVRAGEVHGL
     MGENGAGKST LLKVLSGVNQ PQAGTLTLNG TEQRFASTRA ALEAGIAIIY QELHLVPELT
     VAENLMLGQL PSRLGVVDER TLAARALDAL ERLGEHIDPG IPVKYLSIGQ RQMIEIGKAL
     MRDARVIAFD EPTSSLSARE TTQLFRIIRA LRAEGRAIIY VTHRMEEVYE LCDRVTVFRD
     GRRIDTFDSV TDLDRDRLIG CMVGRSIEDV YGYRPRAAGD VLIEAKGLAG PGLSEPVSFT
     ARRGEIVGFF GLVGAGRSEL MKLLYGAARP SAGHVELNGK RVAFGSPRDA VRAGLALCPE
     DRKQEGIVAI ASVADNLNIS ARRHFSPARV LLDGRREREL AQRYIERLAI KTRDGDTPIG
     ALSGGNQQKV VLARWLAERI DVFLMDEPTR GIDVGARAEI YNLFYELAEA GRTVILVSSD
     LAEVIGVSDR IIVMKEGRIA GEVAKAHATP DALIKLALPR