RGMG1_BURL3
ID RGMG1_BURL3 Reviewed; 512 AA.
AC Q399X3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein 1 {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=Bcep18194_B0624;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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; CP000152; ABB10738.1; -; Genomic_DNA.
DR RefSeq; WP_011354232.1; NC_007511.1.
DR AlphaFoldDB; Q399X3; -.
DR EnsemblBacteria; ABB10738; ABB10738; Bcep18194_B0624.
DR GeneID; 45096997; -.
DR KEGG; bur:Bcep18194_B0624; -.
DR PATRIC; fig|482957.22.peg.4235; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; KTYAQPV; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000002705; Chromosome 2.
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 1"
FT /id="PRO_0000262977"
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; 55872 MW; 1698282BC6A86FB2 CRC64;
MQPDLTPNPA PPLIALTGIG KRFPGVQALD DCHFDLRAGE VHALMGENGA GKSTLMKILA
GVYQRDDGEI RMDGRAVEIA DPRAAQALGI GIIHQELNLM NHLSVAQNIF IGREPRGRFG
VFVDEAALNR DAAAIFARMR LDLDPRTPVG QLTVAKQQMV EIAKALSFDS RVLIMDEPTA
ALNNAEIAEL FRIIGDLRAH GVGIVYISHK MDELRQIADR VTVMRDGKYV ATVPMADTSM
DAIIAMMVGR QLATEFRTPP DTSANDVALE VRGLSRGRAI RDVGFTLRRG EILGFAGLMG
AGRTEVARAV FGADPVDAGE IRVHGKTVSI RSPADAVRHG IGYLSEDRKH FGLAVGMDVQ
NNIALSSMRR FVRRGLFLDA RALRDTAQSY VRQLAIRTPS VTQPARLLSG GNQQKIVIAK
WLLRDCDILF FDEPTRGIDV GAKSEIYKLL DALAADGKAI VMISSELPEV LRMSHRILVM
CEGRVTGELR AADATQEKIM QLATQRESTV LS