RBSA1_STRAW
ID RBSA1_STRAW Reviewed; 522 AA.
AC Q82CM5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribose import ATP-binding protein RbsA 1 {ECO:0000255|HAMAP-Rule:MF_01716};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN Name=rbsA1 {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=SAV_5319;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01716}.
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_01716};
CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
CC {ECO:0000255|HAMAP-Rule:MF_01716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01716};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01716}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer
CC (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}.
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DR EMBL; BA000030; BAC73031.1; -; Genomic_DNA.
DR RefSeq; WP_010986723.1; NZ_JZJK01000072.1.
DR AlphaFoldDB; Q82CM5; -.
DR SMR; Q82CM5; -.
DR STRING; 227882.SAV_5319; -.
DR EnsemblBacteria; BAC73031; BAC73031; SAVERM_5319.
DR KEGG; sma:SAVERM_5319; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_0_11; -.
DR OMA; IKMLSGA; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000000428; 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; 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="Ribose import ATP-binding protein RbsA 1"
FT /id="PRO_0000261108"
FT DOMAIN 8..243
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 249..496
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT REGION 492..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 522 AA; 55641 MW; B69A182E5EB9689A CRC64;
MSNADELLRI EGIRKTFPGV VALDGVDFDL RRGEVHVLLG ENGAGKSTLI KMLSGAYRPD
GGRVLVEGEE VRIHGAQDSE ALGIATIYQE FNLVPDLTVA ENIFLGRQPR RLGLIDRKKM
EADAAELLAR VGVQVSPRAR VRELGIARLQ MVEIAKALSL NARVLIMDEP TAVLTSEEVE
KLFAIVRQLR EDGVGIVFIT HHLEEIAALG DRVTVIRDGK SVGQVPASTS EDELVRLMVG
RSIEQQYPRE RPDSGAALLS VEGLTRDGVF HDVSFEVRAG EVVGVAGLVG AGRTEVVRAV
FGADPYDRGS VQVAGARVPR HDVSAAMSAG IGLVPEDRKG QGLVLDASVE ENLGLVTMRA
ATRGGLVDLK GQRDAAARVA GQLGVRMAGL GQHVRTLSGG NQQKVVIGKW LLADTKVLIL
DEPTRGIDVG AKVEIYQLIN ELTAAGAAVL MISSDLPEVL GMSDRVLVMA QGRIAGELGA
DEATQDSVMA LAVSTNQYKP DKSDKPDASA GKTDQKEAPR GH