ARAG_ECOLI
ID ARAG_ECOLI Reviewed; 504 AA.
AC P0AAF3; P08531;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 131.
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};
GN OrderedLocusNames=b1900, JW1888;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BEK 180;
RX PubMed=2445996; DOI=10.1016/0022-2836(87)90607-3;
RA Scripture J.B., Voelker C., Miller S., O'Donnell R.T., Polgar L., Rade J.,
RA Horazdovsky B.F., Hogg R.W.;
RT "High-affinity L-arabinose transport operon. Nucleotide sequence and
RT analysis of gene products.";
RL J. Mol. Biol. 197:37-46(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN ARABINOSE TRANSPORT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=7028715; DOI=10.1128/jb.148.2.472-479.1981;
RA Kolodrubetz D., Schleif R.;
RT "L-arabinose transport systems in Escherichia coli K-12.";
RL J. Bacteriol. 148:472-479(1981).
RN [6]
RP FUNCTION IN ARABINOSE TRANSPORT.
RC STRAIN=BEK 180;
RX PubMed=2656640; DOI=10.1128/jb.171.6.3053-3059.1989;
RA Horazdovsky B.F., Hogg R.W.;
RT "Genetic reconstitution of the high-affinity L-arabinose transport
RT system.";
RL J. Bacteriol. 171:3053-3059(1989).
RN [7]
RP INDUCTION.
RX PubMed=2231717; DOI=10.1016/s0022-2836(05)80163-9;
RA Hendrickson W., Stoner C., Schleif R.;
RT "Characterization of the Escherichia coli araFGH and araJ promoters.";
RL J. Mol. Biol. 215:497-510(1990).
CC -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in
CC arabinose import. Responsible for energy coupling to the transport
CC system (Probable). {ECO:0000305|PubMed:2656640,
CC ECO:0000305|PubMed:7028715}.
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 -!- INTERACTION:
CC P0AAF3; P28635: metQ; NbExp=3; IntAct=EBI-559586, EBI-1114713;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01721, ECO:0000269|PubMed:7028715}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01721, ECO:0000269|PubMed:7028715}.
CC -!- INDUCTION: Induced by arabinose. Transcription is dependent on the
CC transcription factor AraC, the cAMP receptor protein (CRP) and cAMP.
CC {ECO:0000269|PubMed:2231717}.
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; X06091; CAA29477.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74970.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15720.1; -; Genomic_DNA.
DR PIR; S01074; S01074.
DR RefSeq; NP_416413.1; NC_000913.3.
DR RefSeq; WP_001187819.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0AAF3; -.
DR SMR; P0AAF3; -.
DR BioGRID; 4261851; 4.
DR BioGRID; 850765; 4.
DR ComplexPortal; CPX-4314; Arabinose ABC transporter complex.
DR DIP; DIP-48055N; -.
DR IntAct; P0AAF3; 7.
DR STRING; 511145.b1900; -.
DR TCDB; 3.A.1.2.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AAF3; -.
DR PRIDE; P0AAF3; -.
DR EnsemblBacteria; AAC74970; AAC74970; b1900.
DR EnsemblBacteria; BAA15720; BAA15720; BAA15720.
DR GeneID; 946408; -.
DR KEGG; ecj:JW1888; -.
DR KEGG; eco:b1900; -.
DR PATRIC; fig|1411691.4.peg.350; -.
DR EchoBASE; EB0056; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_6; -.
DR InParanoid; P0AAF3; -.
DR OMA; NVHLGHE; -.
DR PhylomeDB; P0AAF3; -.
DR BioCyc; EcoCyc:ARAG-MON; -.
DR BioCyc; MetaCyc:ARAG-MON; -.
DR PRO; PR:P0AAF3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0016887; F:ATP hydrolysis activity; ISM:EcoCyc.
DR GO; GO:0042882; P:L-arabinose transmembrane transport; IC:ComplexPortal.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..504
FT /note="Arabinose import ATP-binding protein AraG"
FT /id="PRO_0000091936"
FT DOMAIN 8..243
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT DOMAIN 256..499
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ SEQUENCE 504 AA; 55018 MW; 23B401BCF34CFA3A CRC64;
MQQSTPYLSF RGIGKTFPGV KALTDISFDC YAGQVHALMG ENGAGKSTLL KILSGNYAPT
TGSVVINGQE MSFSDTTAAL NAGVAIIYQE LHLVPEMTVA ENIYLGQLPH KGGIVNRSLL
NYEAGLQLKH LGMDIDPDTP LKYLSIGQWQ MVEIAKALAR NAKIIAFDEP TSSLSAREID
NLFRVIRELR KEGRVILYVS HRMEEIFALS DAITVFKDGR YVKTFTDMQQ VDHDALVQAM
VGRDIGDIYG WQPRSYGEER LRLDAVKAPG VRTPISLAVR SGEIVGLFGL VGAGRSELMK
GMFGGTQITA GQVYIDQQPI DIRKPSHAIA AGMMLCPEDR KAEGIIPVHS VRDNINISAR
RKHVLGGCVI NNGWEENNAD HHIRSLNIKT PGAEQLIMNL SGGNQQKAIL GRWLSEEMKV
ILLDEPTRGI DVGAKHEIYN VIYALAAQGV AVLFASSDLP EVLGVADRIV VMREGEIAGE
LLHEQADERQ ALSLAMPKVS QAVA
