ARAE_ECOLI
ID ARAE_ECOLI Reviewed; 472 AA.
AC P0AE24; P09830; Q2M9Z6; Q46937;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Arabinose-proton symporter {ECO:0000305};
DE AltName: Full=Arabinose transporter {ECO:0000305};
GN Name=araE; OrderedLocusNames=b2841, JW2809;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3543693; DOI=10.1038/325641a0;
RA Maiden M.C.J., Davis E.O., Baldwin S.A., Moore D.C.M., Henderson P.J.F.;
RT "Mammalian and bacterial sugar transport proteins are homologous.";
RL Nature 325:641-643(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / JM2433;
RX PubMed=2836407; DOI=10.1016/s0021-9258(18)68433-9;
RA Maiden M.C.J., Jones-Mortimer M.C., Henderson P.J.F.;
RT "The cloning, DNA sequence, and overexpression of the gene araE coding for
RT arabinose-proton symport in Escherichia coli K12.";
RL J. Biol. Chem. 263:8003-8010(1988).
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND INDUCTION.
RX PubMed=6319708; DOI=10.1016/0022-2836(83)90035-9;
RA Stoner C., Schleif R.F.;
RT "The araE low affinity L-arabinose transport promoter. Cloning, sequence,
RT transcription start site and DNA binding sites of regulatory proteins.";
RL J. Mol. Biol. 171:369-381(1983).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=7030324; DOI=10.1042/bj1960269;
RA MacPherson A.J., Jones-Mortimer M.C., Henderson P.J.;
RT "Identification of the AraE transport protein of Escherichia coli.";
RL Biochem. J. 196:269-283(1981).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND INDUCTION.
RX PubMed=6282256; DOI=10.1042/bj2000611;
RA Daruwalla K.R., Paxton A.T., Henderson P.J.;
RT "Energization of the transport systems for arabinose and comparison with
RT galactose transport in Escherichia coli.";
RL Biochem. J. 200:611-627(1981).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Uptake of L-arabinose across the cytoplasmic membrane with
CC the concomitant transport of protons into the cell (symport system)
CC (PubMed:7030324, PubMed:6282256, PubMed:2836407). D-fucose, a
CC nonmetabolizable analog of L-arabinose, is also a good substrate
CC (PubMed:6282256). {ECO:0000269|PubMed:2836407,
CC ECO:0000269|PubMed:6282256, ECO:0000269|PubMed:7030324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-arabinose(in) = H(+)(out) + L-arabinose(out);
CC Xref=Rhea:RHEA:28951, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535;
CC Evidence={ECO:0000269|PubMed:2836407, ECO:0000269|PubMed:6282256};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28953;
CC Evidence={ECO:0000269|PubMed:2836407, ECO:0000269|PubMed:6282256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fucose(in) + H(+)(in) = D-fucose(out) + H(+)(out);
CC Xref=Rhea:RHEA:35011, ChEBI:CHEBI:2179, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:6282256};
CC -!- ACTIVITY REGULATION: Symport activity is inhibited in the presence of
CC the uncoupling agents carbonyl cyanide m-chlorophenylhydrazone (CCCP)
CC and tetrachlorosalicylanilide and 2,4-dinitrophenol (PubMed:6282256).
CC Activity is partially inhibited by N-ethylmaleimide (PubMed:7030324).
CC {ECO:0000269|PubMed:6282256, ECO:0000269|PubMed:7030324}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=316.6 uM for arabinose (in membrane vesicles)
CC {ECO:0000269|PubMed:6282256};
CC Vmax=24.8 nmol/min/mg enzyme (in membrane vesicles)
CC {ECO:0000269|PubMed:6282256};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2836407,
CC ECO:0000269|PubMed:7030324}; Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by arabinose (PubMed:6282256, PubMed:6319708).
CC Transcription is dependent on the transcription factor AraC, the cAMP
CC receptor protein (CRP) and cAMP (PubMed:6319708).
CC {ECO:0000269|PubMed:6282256, ECO:0000269|PubMed:6319708}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; J03732; AAA23469.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40488.1; -; Genomic_DNA.
DR EMBL; X00272; CAA25075.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75880.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76910.1; -; Genomic_DNA.
DR PIR; B26430; B26430.
DR RefSeq; NP_417318.1; NC_000913.3.
DR RefSeq; WP_000256438.1; NZ_SSUV01000026.1.
DR AlphaFoldDB; P0AE24; -.
DR SMR; P0AE24; -.
DR BioGRID; 4259474; 16.
DR STRING; 511145.b2841; -.
DR TCDB; 2.A.1.1.2; the major facilitator superfamily (mfs).
DR PaxDb; P0AE24; -.
DR PRIDE; P0AE24; -.
DR EnsemblBacteria; AAC75880; AAC75880; b2841.
DR EnsemblBacteria; BAE76910; BAE76910; BAE76910.
DR GeneID; 66673292; -.
DR GeneID; 947341; -.
DR KEGG; ecj:JW2809; -.
DR KEGG; eco:b2841; -.
DR PATRIC; fig|1411691.4.peg.3893; -.
DR EchoBASE; EB0054; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_30_5_6; -.
DR InParanoid; P0AE24; -.
DR OMA; WAITASF; -.
DR PhylomeDB; P0AE24; -.
DR BioCyc; EcoCyc:ARAE-MON; -.
DR BioCyc; MetaCyc:ARAE-MON; -.
DR PRO; PR:P0AE24; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015150; F:fucose transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015147; F:L-arabinose transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IMP:EcoCyc.
DR GO; GO:0015756; P:fucose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0042882; P:L-arabinose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..472
FT /note="Arabinose-proton symporter"
FT /id="PRO_0000050289"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..63
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..114
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..178
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..297
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..361
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT CONFLICT 26..28
FT /note="SVA -> YDR (in Ref. 5; CAA25075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51684 MW; 411990A441D44393 CRC64;
MVTINTESAL TPRSLRDTRR MNMFVSVAAA VAGLLFGLDI GVIAGALPFI TDHFVLTSRL
QEWVVSSMML GAAIGALFNG WLSFRLGRKY SLMAGAILFV LGSIGSAFAT SVEMLIAARV
VLGIAVGIAS YTAPLYLSEM ASENVRGKMI SMYQLMVTLG IVLAFLSDTA FSYSGNWRAM
LGVLALPAVL LIILVVFLPN SPRWLAEKGR HIEAEEVLRM LRDTSEKARE ELNEIRESLK
LKQGGWALFK INRNVRRAVF LGMLLQAMQQ FTGMNIIMYY APRIFKMAGF TTTEQQMIAT
LVVGLTFMFA TFIAVFTVDK AGRKPALKIG FSVMALGTLV LGYCLMQFDN GTASSGLSWL
SVGMTMMCIA GYAMSAAPVV WILCSEIQPL KCRDFGITCS TTTNWVSNMI IGATFLTLLD
SIGAAGTFWL YTALNIAFVG ITFWLIPETK NVTLEHIERK LMAGEKLRNI GV
