ID   RBSA_CLOPS              Reviewed;         501 AA.
AC   Q0SSJ0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=CPR_1601;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000312; ABG85910.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SSJ0; -.
DR   SMR; Q0SSJ0; -.
DR   PRIDE; Q0SSJ0; -.
DR   EnsemblBacteria; ABG85910; ABG85910; CPR_1601.
DR   KEGG; cpr:CPR_1601; -.
DR   OMA; AKREIYQ; -.
DR   Proteomes; UP000001824; 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; Repeat;
KW   Sugar transport; Translocase; Transport.
FT   CHAIN           1..501
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261058"
FT   DOMAIN          8..245
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          255..500
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   501 AA;  55560 MW;  2B78F152234D65CC CRC64;
     MGERTPMLKM VGVSKSFPGV KALDNVSLMA YGGEVTALMG ENGAGKSTLM KILSGVYKKD
     EGKIFIEGRE VEVKGIKSAE EAGITIIHQE LSVLNNLTVS ENIFLGNEKH SKFTGRINKK
     LLDERSKMFL EQIGCDIDPN RLVSTLNVGE KQMIEIAKAL TKNARIIIMD EPTTALTDVE
     TENLFKVIEN LRKKGIAIIY ISHRMEEIFK ICHRVEVLRD GKYTGSAEIK DIDNDKLIAM
     MVGRTIEDQF PYRDVKKGDL ALEVKNLSCK EGVKGASFTL RKGEILGIAG LMGSGRTELA
     KTIFGEYKKT SGEISLNGSL ININCISDAI NNGICYLSED RKKEGCILGM SVGENMTLCN
     LKKYENKFKS LDKKEEAKDI EYYIKKINIK TPNKEQFIKN LSGGNQQKVI LAKWLMLSPE
     VLIIDEPTRG IDVGAKKEIY ELLNELKASG KAIIMISSDL PEVLGISDRI MVMSEGRISG
     ELNRDEANQE SIMKLAVGIN N