ARAG_ALKHC
ID ARAG_ALKHC Reviewed; 517 AA.
AC Q9K7C3;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=L-arabinose transport ATP-binding protein AraG;
DE EC=7.5.2.12;
GN Name=araG; OrderedLocusNames=BH3441;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for L-
CC arabinose. Probably responsible for energy coupling to the transport
CC system (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; BA000004; BAB07160.1; -; Genomic_DNA.
DR PIR; A84080; A84080.
DR AlphaFoldDB; Q9K7C3; -.
DR SMR; Q9K7C3; -.
DR STRING; 272558.10176064; -.
DR EnsemblBacteria; BAB07160; BAB07160; BAB07160.
DR KEGG; bha:BH3441; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_9; -.
DR OMA; LPGGRMH; -.
DR PRO; PR:Q9K7C3; -.
DR Proteomes; UP000001258; Chromosome.
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 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; IPR027417; P-loop_NTPase.
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.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT CHAIN 1..517
FT /note="L-arabinose transport ATP-binding protein AraG"
FT /id="PRO_0000091934"
FT DOMAIN 8..245
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 264..510
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 309..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 517 AA; 57148 MW; B95DD8FE4027B1BC CRC64;
MNMPNCLLEM RNITKAFPGV KALNNVNLKV EQGEIHALVG ENGAGKSTLM KVLSGVYPHG
TYEGDILFEG RVCQFKDIKE SEQLGIVIIH QELALVPELS IAENIFLGNE QAKNGVIDWN
QTITEAAKLL KKVGLSDSPR TLAMNIGVGK QQLVEIAKAL SKKVKLLILD EPTAALNEED
SQNLLHLLLE FKKQGMTSII ISHKLNEISY VADHLTILRD GQSIETLSLQ SGEVTEDRII
KGMVGRDLEN RFPPREPKIG DVILEVNHWH VDDPLHPDRS LIKDVNLYLK RGEIVGVAGL
MGAGRTELAM SIFGKSYGKN IRGQLIKDGK EIKVHSVKDA IDHGLAYVTE DRKTYGLILI
DDIKHNISLT SLEKLSKNGV VDKTREVKEA EDFRKKMNIR TPSIDQKTGN LSGGNQQKVV
LSKWILSGPD ILILDEPTRG IDVGAKYEIY SVIHELAAQG KAVLVISSEL PELLGLSDRI
YALCEGRITG EVTREEANQE ILMKYMTRTG GNGHEVS