ID   ARAG_YERPA              Reviewed;         523 AA.
AC   Q1C7J0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=YPA_1616;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex AraFGH involved in
CC       arabinose import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01721}.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01721}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01721}.
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; CP000308; ABG13582.1; -; Genomic_DNA.
DR   RefSeq; WP_002210588.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C7J0; -.
DR   SMR; Q1C7J0; -.
DR   EnsemblBacteria; ABG13582; ABG13582; YPA_1616.
DR   GeneID; 66841392; -.
DR   KEGG; ypa:YPA_1616; -.
DR   OMA; NVHLGHE; -.
DR   Proteomes; UP000001971; 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   GO; GO:0042882; P:L-arabinose transmembrane transport; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..523
FT                   /note="Arabinose import ATP-binding protein AraG"
FT                   /id="PRO_0000270484"
FT   DOMAIN          20..255
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT   DOMAIN          268..511
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
FT   BINDING         52..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01721"
SQ   SEQUENCE   523 AA;  56873 MW;  F79AABDF2D43F7B5 CRC64;
     MSAPHSALQA ELDAAQSPYL AFRGIGKSFP GVLALDDISF TCQAGQIHAL MGENGAGKST
     LLKILSGNYT PTQGEIHIKG KAVNFTNTTD ALDAGVAIIY QELHLVPEMT VAENIYLGQL
     PTKMGMVDRK LLRYESRIQL SHLGLDIDPD TPLKYLSIGQ WQMVEIAKAL ARNAKIIAFD
     EPTSSLSARE IEQLFRVIRE LRAEGRVILY VSHRMEEIFA LSDAITVFKD GRYVRTFDDM
     TQVNNASLVQ AMVGRNLGDI YGYQPREIGS ERLTLQAVKA IGVASPISLT VHQGEIVGLF
     GLVGAGRSEL LKGLFGDTKL TSGKLLLDGQ PLTIRSPIDA ISAGIMLCPE DRKADGIIPV
     HSVQDNINIS ARRKTLTAGC LINNRWEADN ALLRIQSLNI KTPGPQQLIM NLSGGNQQKA
     ILGRWLSEDM KVILLDEPTR GIDVGAKHEI YNVIYQLAKQ GIAVLFASSD LPEVLGLADR
     IVVMREGAIS GELDHEYATE EQALSLAMLR TPNIATNTAS AVA