ARAE_KLEOX
ID ARAE_KLEOX Reviewed; 472 AA.
AC P45598;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Arabinose-proton symporter {ECO:0000305};
DE AltName: Full=Arabinose transporter {ECO:0000305};
GN Name=araE {ECO:0000303|PubMed:7665532};
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=8017;
RX PubMed=7665532; DOI=10.1128/jb.177.18.5379-5380.1995;
RA Shatwell K.P., Charalambous B.M., McDonald T.P., Henderson P.J.F.;
RT "Cloning, sequencing, and expression of the araE gene of Klebsiella oxytoca
RT 8017, which encodes arabinose-H+ symport activity.";
RL J. Bacteriol. 177:5379-5380(1995).
CC -!- FUNCTION: Uptake of L-arabinose across the cytoplasmic membrane with
CC the concomitant transport of protons into the cell (symport system)
CC (PubMed:7665532). D-fucose, a nonmetabolizable analog of L-arabinose,
CC is also a good substrate (PubMed:7665532).
CC {ECO:0000269|PubMed:7665532}.
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:0000305|PubMed:7665532};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28953;
CC Evidence={ECO:0000305|PubMed:7665532};
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:0000305|PubMed:7665532};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AE24}; Multi-pass membrane protein
CC {ECO:0000255}.
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; X79598; CAA56110.1; -; Genomic_DNA.
DR PIR; S47089; S47089.
DR RefSeq; WP_014226687.1; NZ_PQKQ01000004.1.
DR AlphaFoldDB; P45598; -.
DR SMR; P45598; -.
DR STRING; 571.MC52_03315; -.
DR GeneID; 66558028; -.
DR eggNOG; COG2814; Bacteria.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..472
FT /note="Arabinose-proton symporter"
FT /id="PRO_0000050291"
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:0000250|UniProtKB:P0AE24"
SQ SEQUENCE 472 AA; 51732 MW; 410021E1BEE3D96E CRC64;
MTTLSHDSTT MPRTQRDTRR MNQFVSIAAA VAGLLFGLDI GVIAGALPFI TDHFVLSSRL
QEWVVSSMML GAAIGALFNG WLSFRLGRKY SLMVGAVLFV AGSVGSAFAT SVEMLLVARI
VLGVAVGIAS YTAPLYLSEM ASENVRGKMI SMYQLMVTLG IVMAFLSDTA FSYSGNWRAM
LGVLALPAVV LIILVIFLPN SPRWLAEKGR HVEAEEVLRM LRDTSEKARD ELNEIRESLK
LKQGGWALFK VNRNVRRAVF LGMLLQAMQQ FTGMNIIMYY APRIFKMAGF TTTEQQMVAT
LVVGLTFMFA TFIAVFTVDK AGRKPALKIG FSVMAIGTLV LGYCLMQFDN GTASSGLSWL
SVGMTMMCIA GYAMSAAPVV WILCSEIQPL KCRDFGITCS TTTNWVSNMI IGATFLTLLD
AIGAAGTFWL YTALNVAFIG VTFWLIPETK NVTLEHIERR LMSGEKLRNI GN
