RGMG2_BURCH
ID RGMG2_BURCH Reviewed; 512 AA.
AC A0B297;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein 2 {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=Bcen2424_5039;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000459; ABK11773.1; -; Genomic_DNA.
DR RefSeq; WP_011547136.1; NC_008543.1.
DR AlphaFoldDB; A0B297; -.
DR SMR; A0B297; -.
DR KEGG; bch:Bcen2424_5039; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; AKREIYQ; -.
DR OrthoDB; 551294at2; -.
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; Repeat; Sugar transport; Translocase; Transport.
FT CHAIN 1..512
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein 2"
FT /id="PRO_0000277554"
FT DOMAIN 14..251
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 262..507
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ SEQUENCE 512 AA; 56304 MW; 7F32EA39BFEC416D CRC64;
MQPDLNPNTT QPLIALTGIG KRFPGVQALD DCRFDLRAGE VHALMGENGA GKSTLMKILA
GVYQRDAGEI RMDGRPVEIA DPRAAQALGI GIIHQELNLM NHLSVAQNIF IGREPRGRFG
VFVDEEKLNR DAAAIFQRMR LDLDPRTPVG RLTVAKQQMV EIAKALSFDS RALIMDEPTA
ALNNAEIAEL FRIIRDLRAH GVGIIYISHK MDELRQIADR VTVMRDGKYV ATVPMADTSM
ESIISMMVGR QLDTETRTPP DTSGNEIALE VRGLSRGRAI RDVGFTLRRG EILGFAGLMG
AGRTEVARAV FGADPVDAGE IRVHGRAVTI RTPADAVKYG IGYLSEDRKH FGLAIGMDVQ
NNIALSSMRR FVRRGLFLDA RGMRDAARSY VRQLAIRTPS VAQPARLLSG GNQQKIVIAK
WLLRDCDILF FDEPTRGIDV GAKSEIYKLL DALAADGKAI VMISSELPEV LRMSHRILVM
CEGRVTGELR AADATQEKIM QLATQRESTV LS