RGMG_ALBFT
ID RGMG_ALBFT Reviewed; 504 AA.
AC Q21TR5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Rfer_3129;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-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; CP000267; ABD70838.1; -; Genomic_DNA.
DR RefSeq; WP_011465401.1; NC_007908.1.
DR AlphaFoldDB; Q21TR5; -.
DR SMR; Q21TR5; -.
DR STRING; 338969.Rfer_3129; -.
DR EnsemblBacteria; ABD70838; ABD70838; Rfer_3129.
DR KEGG; rfr:Rfer_3129; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_4; -.
DR OMA; AKREIYQ; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000008332; 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..504
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein"
FT /id="PRO_0000262992"
FT DOMAIN 5..242
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 252..497
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; 55119 MW; DF1A00EB30BDE21C CRC64;
MTSLISVKNL SKSFPGVKAL DQVHFDLRAG EVHALMGENG AGKSTLMKIL AGVYRKDSGE
MLLDGQPVEI ESPAHAQSLA IGIVHQELHL MNHLTAAQNI YLGREPRHCG GLFLDEARLN
QDTQILFDRL NLALAPTTAI GELTVARQQM VEIAKALSFK SRVLIMDEPT AALNNAEIDE
LFRIIRQLKS EGVGIVYISH KMDEIQRIAD RITVMRDGST IGTVPASTPM QQVIAMMVGR
NLEQAEKHIP DTSANEVLLE VRGLNRGRVI RDVNFSVRRG EILGFAGLMG AGRTEVARAV
FGADPIDSGE VRVRGELIRL ASPQDAVQAG IGYLSEDRKH FGLATGMDVE SNITLPSLKR
WLKWGLFLNQ PAIHHISQQM VGKLRIKTPS LTQTARLLSG GNQQKVVVAK WLVQDCDVLI
FDEPTRGIDV GAKSEIYKLL NELATQGKAI IVISSELPEV LLLSHRVLVM CEGRITGEVA
GDVATQETLM ALATRRESLA STVH