ARAH_AZOBR
ID ARAH_AZOBR Reviewed; 339 AA.
AC Q1JUP6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=L-arabinose ABC transporter permease protein AraH;
GN Name=araH; Synonyms=araZ;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT 3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT into sugar metabolism.";
RL J. Biol. Chem. 281:33521-33536(2006).
CC -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in L-
CC arabinose import. Responsible for the translocation of the substrate
CC across the membrane (Probable). {ECO:0000305}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. AraH/RbsC subfamily. {ECO:0000305}.
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DR EMBL; AB241136; BAE94274.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1JUP6; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042882; P:L-arabinose transmembrane transport; IGC:UniProtKB.
DR InterPro; IPR001851; ABC_transp_permease.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..339
FT /note="L-arabinose ABC transporter permease protein AraH"
FT /id="PRO_0000418503"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 339 AA; 35372 MW; 7158D2EC4A6CB999 CRC64;
MSQAMQPQRT SPSPDAAIAP ARARGGVWQL INRSGIVMVF LVLFATLSLT VPDFLTPRNI
QGLLLSVTLI GSIAVTMMFV LALGEVDLSV ASIVAFSGVV ASTLITATHS VVLGIAGGVL
AGGAVGLVNG VLIARWRINS LIVTLAMMEV VRGLAFITSN GDAVMISEER FFDLGGGSFL
GISYPIWSNI VGFVVFGFLL RKTVFGKNVL AVGGNGEAAL LAGLPVMRIK ITVFVLQGLV
TGFAGVMLAS RMSLGDPKTS VGLELGVISA CVLGGVSLTG GVATISGVLV GVLIMGSVQD
AMSLLNVPTF YQYLIRGGIL LLAVLFDQYR RNQRRAMKI