ID   XYLG_BRUAB              Reviewed;         511 AA.
AC   Q576H3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Xylose import ATP-binding protein XylG {ECO:0000255|HAMAP-Rule:MF_01722};
DE            EC=7.5.2.10 {ECO:0000255|HAMAP-Rule:MF_01722};
GN   Name=xylG {ECO:0000255|HAMAP-Rule:MF_01722}; OrderedLocusNames=BruAb2_1088;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
CC   -!- FUNCTION: Part of the ABC transporter complex XylFGH involved in xylose
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01722}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-xylose(out) + H2O = ADP + D-xylose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:29899, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:456216; EC=7.5.2.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01722};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (XylG),
CC       two transmembrane proteins (XylH) and a solute-binding protein (XylF).
CC       {ECO:0000255|HAMAP-Rule:MF_01722}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01722}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01722}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Xylose importer
CC       (TC 3.A.1.2.4) family. {ECO:0000255|HAMAP-Rule:MF_01722}.
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DR   EMBL; AE017224; AAX76461.1; -; Genomic_DNA.
DR   RefSeq; WP_002966631.1; NC_006933.1.
DR   AlphaFoldDB; Q576H3; -.
DR   SMR; Q576H3; -.
DR   EnsemblBacteria; AAX76461; AAX76461; BruAb2_1088.
DR   GeneID; 3827457; -.
DR   GeneID; 55592770; -.
DR   KEGG; bmb:BruAb2_1088; -.
DR   HOGENOM; CLU_000604_92_3_5; -.
DR   OMA; LPGGRMH; -.
DR   Proteomes; UP000000540; Chromosome II.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015614; F:ABC-type D-xylose 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; IPR013455; ABC_transptr_xylose_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR02633; xylG; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS51280; XYLG; 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..511
FT                   /note="Xylose import ATP-binding protein XylG"
FT                   /id="PRO_0000271493"
FT   DOMAIN          6..244
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
FT   DOMAIN          261..506
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
SQ   SEQUENCE   511 AA;  55814 MW;  F43939057F24F395 CRC64;
     MSEYLLEMRN IGKEFNGVKA LDGIYLKVRA GECVGLCGEN GAGKSTLMKV LSGVYPHGTW
     TGEIFWEGKE LKASGIRDTE AAGIVIIHQE LMMVPHLSVA ENIFLGCEPT TGGFIDYDQM
     NARAAELLAR LKINDINVAL PVYHYSGGKQ QLIEIAKAIN KNAKLLILDE PTSALTASET
     RVLIDLIKDF KKQGMACVYI SHKLDEVAEI SDTVTVIRDG AHIATRPMSE LTTPDIITMM
     VGREMKNLFP REPHDIGEVM FEARNISCWD VTNPGRKVVD DVSFALRRGE ILGIAGLVGA
     GRTELVSSLF GVWPGACQGQ VFLEGKEIKI RTPRDAVRQG ICMVPEDRKR DGILPIMPVG
     HNMTISVLDR FSLRGLIDKD AELVAIQREI LRLKVKTADP MLAIASLSGG NQQKAVLSKM
     MLPDPKVLIL DEPTRGVDVG AKYEIYKLIF ALARQGVSIL MVSSEMPEVL GISDRVLVIG
     EGKLRGDFPN ENLTQEKVLA AAIGKPATNA A