ARAG2_BURTA
ID ARAG2_BURTA Reviewed; 525 AA.
AC Q2T4S8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=BTH_II1627;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000085; ABC34189.1; -; Genomic_DNA.
DR RefSeq; WP_009897554.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T4S8; -.
DR SMR; Q2T4S8; -.
DR PRIDE; Q2T4S8; -.
DR EnsemblBacteria; ABC34189; ABC34189; BTH_II1627.
DR KEGG; bte:BTH_II1627; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; MRDARVI; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000001930; Chromosome II.
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..525
FT /note="Arabinose import ATP-binding protein AraG 2"
FT /id="PRO_0000270463"
FT DOMAIN 35..270
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT DOMAIN 281..524
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ SEQUENCE 525 AA; 56397 MW; BC8C516EA06C8CBF CRC64;
MTDTTIRARG AQAAGSPAGA GPLDAPDGAP RAACLELDGI TVTFPGVRAL DAVSLSVRAG
EVHGLMGENG AGKSTLLKVL SGVNQPQAGT LRLNGLAQRF GSTRAALEAG IAIIYQELHL
VPELTVAENL MLGQLPNRAG VLDERALVAR ATAELERLGE RIDPNTPVKL LSIGQRQMIE
IGKALMRDAR VIAFDEPTSS LSARETERLF RIIHALRADG RAIIYVTHRM EEVDALCDRV
TVFRDGRRIE TFESVADLDR DRLIGCMVGR PIADVYGYRP REPGDVAIEA KGLRGPGLAE
PVSFSARRGE IVGFFGLVGA GRSELMKLLY GAARPSAGHV ELNGRRVSFA SPRDAVRAGI
ALCPEDRKQE GIVAIASVAD NLNLSARRHF SPARLLLDAR RERELAARYI ARLAIKTRDA
DTPIGALSGG NQQKVILARW LAERIDVFLM DEPTRGIDVG ARAEIYNLFY ELADAGRTVL
IVSSDLAEVI GVSDRIVVMK QGRIAGCVAK AQASPDALIK LALPR