ID   XYLG_SHIBS              Reviewed;         513 AA.
AC   Q31V51;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SBO_3575;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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; CP000036; ABB68057.1; -; Genomic_DNA.
DR   RefSeq; WP_001146509.1; NC_007613.1.
DR   AlphaFoldDB; Q31V51; -.
DR   SMR; Q31V51; -.
DR   EnsemblBacteria; ABB68057; ABB68057; SBO_3575.
DR   KEGG; sbo:SBO_3575; -.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   OMA; VGREMSH; -.
DR   Proteomes; UP000007067; Chromosome.
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..513
FT                   /note="Xylose import ATP-binding protein XylG"
FT                   /id="PRO_0000271514"
FT   DOMAIN          5..242
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
FT   DOMAIN          259..505
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01722"
SQ   SEQUENCE   513 AA;  56440 MW;  255A50627E724093 CRC64;
     MPYLLEMKNI TKTFGSVKAI DNVSLRLNAG EIVSLCGENG SGKSTLMKVL CGIYPHGSYE
     GEIIFAGEEI QASHIRDTER KGIAIIHQEL ALVKELTVLE NIFLGNEITH NGIMDYDLMT
     LRCQKLLAQV SLSISPDTRV GDLGLGQQQL VEIAKALNKQ VRLLILDEPT ASLTEQETSV
     LLDIIRDLQQ HGIACIYISH KLNEVKAISD TICVIRDGQH IGTRDAAGMS EDDIITMMVG
     RELTALYPNE PHTTGDEILR IEHLTAWHPV NRHIKRVNDV SFSLKRGEIL GIAGLVGAGR
     TETIQCLFGV WPGQWEGKIY IDGKQVDIRN CQQAIAQGIA MVPEDRKRDG IVPVMAVGKN
     ITLAALNKFT GGISQLDDAA EQKCILESIQ QLKVKTSSPD LAIGRLSGGN QQKAILARCL
     LLNPRILILD EPTRGIDIGA KYEIYKLINQ LVQQGIAVIV ISSELPEVLG LSDRVLVMHE
     GKLKANLINH NLTQEQVMEA ALRSEHHVEK QSV