RGMG_ALKHC
ID RGMG_ALKHC Reviewed; 522 AA.
AC Q9KAG5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=BH2322;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01717};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; BA000004; BAB06041.1; -; Genomic_DNA.
DR PIR; B83940; B83940.
DR RefSeq; WP_010898478.1; NC_002570.2.
DR AlphaFoldDB; Q9KAG5; -.
DR SMR; Q9KAG5; -.
DR STRING; 272558.10174942; -.
DR DNASU; 891696; -.
DR EnsemblBacteria; BAB06041; BAB06041; BAB06041.
DR KEGG; bha:BH2322; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_9; -.
DR OMA; RIDHKAT; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000001258; 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 membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT CHAIN 1..522
FT /note="Putative ribose/galactose/methyl galactoside import
FT ATP-binding protein"
FT /id="PRO_0000262973"
FT DOMAIN 7..244
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT DOMAIN 254..498
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ SEQUENCE 522 AA; 58463 MW; 5DA05E440B599342 CRC64;
MGEHFLLEMV DITKEFPGVK ALDRVQLKVR KGSVHALMGE NGAGKSTLMK ILIGMYKPNE
GKIIFDGEEV TFNSINDALD KGISMIHQEL SPIPEMTVAE NIFLGREPTF GKSGLVDNKK
LIEMTRNLLE SLEINIDPRK KMGELSIANT QMIEIAKAIS FHSKLVIMDE PTSAITEKEV
AQLFKMIESL KKKGVGIIYI THKMSELDEI ADDISVFRDG KYIGTDTAKN LTRDDLIKMM
VGRELNQIFD KPEPKLGEVI LSVKSLTKQD YFEDVSFEVR KGEIVGFAGL MGSGRTEVLE
TIFGVKEAES GEIFVNGQKA RIKSPQDAVK NNMGFLTEDR KLTGLFLPLS VRENMITVNI
DKYINMGWLN GKRVKKDCEQ QKQKLYIKTP SIEQIVENLS GGNQQKVLLA RWLLKNPDIL
FLDEPTRGID VGAKSEFYNL IFELASQGKA IVVVSSEMAE ILGLCDRILV MHEGKVTGEL
TREEANQEKI MQYATGQAKM AKKLHVHNNF EQTVTANKIE IG