RGMG2_RHIEC
ID RGMG2_RHIEC Reviewed; 513 AA.
AC Q2K353;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=RHE_CH03989;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000133; ABC92733.1; -; Genomic_DNA.
DR RefSeq; WP_011427177.1; NC_007761.1.
DR AlphaFoldDB; Q2K353; -.
DR SMR; Q2K353; -.
DR STRING; 347834.RHE_CH03989; -.
DR EnsemblBacteria; ABC92733; ABC92733; RHE_CH03989.
DR KEGG; ret:RHE_CH03989; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_5; -.
DR OMA; EGMAVIM; -.
DR Proteomes; UP000001936; Chromosome.
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..513
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein 2"
FT /id="PRO_0000262988"
FT DOMAIN 24..260
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 270..510
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ SEQUENCE 513 AA; 56859 MW; 21F53BB4967DFB9F CRC64;
MAVSPTTMAA VRASGAVPNA EFLLSAEGVR KEFPGVVALD DVQFRLKRAS VHALMGENGA
GKSTLMKILA GIYTPDKGDI RLKGVEIQLK SPLDALENGI AMIHQELNLM PFMTVAENIW
IRREPKNRFG FIDHGVMHSM TEELFARLNI DIDPDIEVRH LSVANRQMVE IAKAVSYNSD
VLIMDEPTSA LTEREVEHLF RIIRDLRSQG IGIVYITHKM NELFEIADEF SVFRDGRYIG
THASTDVTRD DIIRMMVGRE ITQMFPKEEV PIGEIVLSVK DLCLKGVFRN VSFEVRAGEI
LGVAGLVGSG RSNVAETLFG VTPPSSGTVE LFGKPVTISS PTEAIRHQMA FLTEDRKDTG
CLLILDILEN MQIAVLQDKF VKGGFVQQGA LEATCEDMAK RLRVKTPNLY ERVENLSGGN
QQKVLIGRWL LTHPKILILD EPTRGIDVGA KAEIHRLVTE MARNGVAVIM ISSEMPEVLG
MSDRIMVMHE GLVTGFLNRD EATQIKVMEL AAR