ID   RGMG_PARXL              Reviewed;         504 AA.
AC   Q13FD9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_01717};
DE            EC=7.5.2.11 {ECO:0000255|HAMAP-Rule:MF_01717};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01717};
GN   OrderedLocusNames=Bxeno_C1272; ORFNames=Bxe_C1350;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in carbohydrate
CC       import. Could be involved in ribose, galactose and/or methyl
CC       galactoside import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60156, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.5.2.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01717};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01717}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate
CC       importer 2 (CUT2) (TC 3.A.1.2) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01717}.
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DR   EMBL; CP000272; ABE37200.1; -; Genomic_DNA.
DR   RefSeq; WP_011494426.1; NZ_CP008761.1.
DR   AlphaFoldDB; Q13FD9; -.
DR   SMR; Q13FD9; -.
DR   STRING; 266265.Bxe_C1350; -.
DR   EnsemblBacteria; ABE37200; ABE37200; Bxe_C1350.
DR   KEGG; bxb:DR64_8459; -.
DR   KEGG; bxe:Bxe_C1350; -.
DR   PATRIC; fig|266265.5.peg.9105; -.
DR   eggNOG; COG1129; Bacteria.
DR   OMA; AKREIYQ; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
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.
DR   PROSITE; PS51260; MGLA; 1.
DR   PROSITE; PS51254; RBSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW   Translocase; Transport.
FT   CHAIN           1..504
FT                   /note="Putative ribose/galactose/methyl galactoside import
FT                   ATP-binding protein"
FT                   /id="PRO_0000262979"
FT   DOMAIN          5..242
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   DOMAIN          241..498
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ   SEQUENCE   504 AA;  54974 MW;  12D30B8861E18EC7 CRC64;
     MTSLISVKRL NKSFPGVRAL HEVQFELMAG EVHALMGENG AGKSTLMKIL AGVYTRDSGE
     ILYDGQPVEF LSPRDAQAVG VGIIHQELQL MNHLTVAQNI FIGREPRGRL GLLLDEDRLN
     AQAAAILARM HVSLDPRAVV GALTVARQQM VEIAKALSFD SRVLIMDEPT SALNDAEIAE
     LFRIIRELKS RGVGIVYISH KMDELKQIAD RVTVMRDGEY VATVAARDTS VEAIIGMMVG
     RTLTDIAPSH SVADQGEIAL EVRNLNAGPL VRDVSFALRK GEILGFAGLM GAGRTEVARA
     VFGADPVESG EIVVNGARAT IRTPSDAVAH GIGYLSEDRK RFGLATGMDV ESNIVMSNLR
     KFLSLNFFLR RAQIRRTASH FISLLGIRTP SATQAVRLLS GGNQQKIVIA KWLERDCDVL
     FFDEPTRGID VGAKNEIYKL LRSLAGEGKA VVMISSELPE ILRMSDRVIV MCEGRITGEL
     SAAEATQERI MHLATRRETL KTAA