ARAG2_BURL3
ID ARAG2_BURL3 Reviewed; 522 AA.
AC Q39BJ8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Arabinose import ATP-binding protein AraG 2 {ECO:0000255|HAMAP-Rule:MF_01721};
DE EC=7.5.2.12 {ECO:0000255|HAMAP-Rule:MF_01721};
GN Name=araG2 {ECO:0000255|HAMAP-Rule:MF_01721};
GN OrderedLocusNames=Bcep18194_B0046;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in
CC arabinose import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01721}.
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; CP000152; ABB10163.1; -; Genomic_DNA.
DR RefSeq; WP_011353661.1; NC_007511.1.
DR AlphaFoldDB; Q39BJ8; -.
DR SMR; Q39BJ8; -.
DR PRIDE; Q39BJ8; -.
DR EnsemblBacteria; ABB10163; ABB10163; Bcep18194_B0046.
DR GeneID; 45096435; -.
DR KEGG; bur:Bcep18194_B0046; -.
DR PATRIC; fig|482957.22.peg.3605; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; MRDARVI; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000002705; Chromosome 2.
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; IEA:InterPro.
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..522
FT /note="Arabinose import ATP-binding protein AraG 2"
FT /id="PRO_0000270461"
FT DOMAIN 32..267
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT DOMAIN 267..518
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ SEQUENCE 522 AA; 56222 MW; 77692DFEA7AE3533 CRC64;
MTTQTMTAVS GNDGDTGADV DAGARKPGGP LLALDGITVT FPGVRALDAV SLSVRAGEVH
GLMGENGAGK STLLKVLSGV NQPQAGTLAL NGTAQRFAST RAALEAGIAI IYQELHLVPE
LTVAENLMLG QLPSRLGVVD ERTLAARALD ALERLGEHID PGIPVKYLSI GQRQMIEIGK
ALMRDARVIA FDEPTSSLSA RETTQLFRII RALRAEGRAI IYVTHRMEEV YELCDRVTVF
RDGRRIDTFD SVTDLDRDRL IGCMVGRSIE DVYGYRPRTA GDVLIEAKGL AGPGLSEPVS
FTARRGEIVG FFGLVGAGRS ELMKLLYGAA RPSAGHVELN GKRVAFGSPR DAVRAGLALC
PEDRKQEGIV AIASVADNLN ISARRHFSPA RMLLDARRER ELAQRYIERL AIKTRDGDTP
IGALSGGNQQ KVVLARWLAE RIDVFLMDEP TRGIDVGARA EIYNLFYELA EAGRTVILVS
SDLAEVIGVS DRIIVMKEGR IAGEVAKAQA TPDALIKLAL PR
