ARAG2_BURCA
ID ARAG2_BURCA Reviewed; 515 AA.
AC Q1BJW2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Bcen_5219;
OS Burkholderia cenocepacia (strain AU 1054).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU 1054;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054.";
RL Submitted (MAY-2006) 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; CP000379; ABF80093.1; -; Genomic_DNA.
DR RefSeq; WP_011548801.1; NC_008061.1.
DR AlphaFoldDB; Q1BJW2; -.
DR SMR; Q1BJW2; -.
DR EnsemblBacteria; ABF80093; ABF80093; Bcen_5219.
DR KEGG; bcn:Bcen_5219; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; MRDARVI; -.
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..515
FT /note="Arabinose import ATP-binding protein AraG 2"
FT /id="PRO_0000270456"
FT DOMAIN 25..260
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT DOMAIN 260..511
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ SEQUENCE 515 AA; 55558 MW; D8638BA177848A5E CRC64;
MTMQTMTAAS GHDAEAGTPP DGPLLALDGI TVTFPGVRAL DAVSLSVRAG EVHGLMGENG
AGKSTLLKVL SGVNQPQAGT LTLNGTAQRF ASTRAALEAG IAIIYQELHL VPELTVAENL
MLGQLPSRLG VVDERTLAAR ALDALERLGE HIDPGIPVKY LSIGQRQMIE IGKALMRHAR
VIAFDEPTSS LSARETTQLF RIIRALRAEG RAIIYVTHRM EEVYELCDRV TVFRDGRRID
TFDSVADLDR DRLIGCMVGR SIEDVYGYRS RPAGDVLIEA KGLAGPGLAE PVSFTARRGE
IVGFFGLVGA GRSELMKLLY GAVRPSAGHV ELNGKRVAFG SPRDAVRAGI ALCPEDRKQE
GIVAIASVAD NLNISARRHF SPARVLLDGR RERELAQKYI ERLAIKTRDG DTPIGALSGG
NQQKVVLARW LAERIDVFLM DEPTRGIDVG ARAEIYNLFY ELAEAGRTVI LVSSDLAEVI
GVSDRIVVMK EGRIAGEVAK AHATPDALIK LALPR