ID   RBSA_CLOTE              Reviewed;         505 AA.
AC   Q891M1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=CTC_02350;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO36824.1; -; Genomic_DNA.
DR   RefSeq; WP_011100485.1; NC_004557.1.
DR   AlphaFoldDB; Q891M1; -.
DR   SMR; Q891M1; -.
DR   STRING; 212717.CTC_02350; -.
DR   EnsemblBacteria; AAO36824; AAO36824; CTC_02350.
DR   GeneID; 64179574; -.
DR   KEGG; ctc:CTC_02350; -.
DR   HOGENOM; CLU_000604_92_3_9; -.
DR   OMA; RIYTIFE; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000001412; 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..505
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261059"
FT   DOMAIN          12..249
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          259..504
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   505 AA;  56614 MW;  1081E2D7383FBD17 CRC64;
     MKKENLEEKP FLQMKGISKF FSGVQALDNV ELKVYRGEVL ALLGENGAGK STLMKILSGV
     YTKDEGDIFI DEKKVDIKGI KEAEELGISI IHQELSLLSN LKIYENIFLG SEKYKGIFNK
     LDKDYMRSES EKLLSTIGFT ADVDILAKDI NIGEMQMIEI IKAISKKSKL IIMDEPTTAL
     TEVETERLFK VINKLKSEGI CIIYISHRLD EIFQICDRVN VLRDGKYVGE VKVKDTTKDD
     LITMMVGRKL EEQFPYKKVK KGDALLAVNN LSYKNKVKNI SFEVRAGEIL GLAGLMGSGR
     TELAKTIFGE YKKSSGDIYI NDKKINITSP KEAIENGIAY LSEDRKKEGL ILNMSVGNNI
     SLCNLKKYEN SIKKINKEKE SKEIDDYIKK LSVKTPSANQ IIKNLSGGNQ QKAIIAKWIM
     ISPNILIIDE PTRGIDVGAK KEIYEVLNEI KSLGKAIIMI SSDMPEVLGI SDRILVMSEG
     NLSGELSREE ATQEKIMKYA VAFSN