RBSA_BACCR
ID RBSA_BACCR Reviewed; 496 AA.
AC Q81HW8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=BC_0662;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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; AE016877; AAP07677.1; -; Genomic_DNA.
DR RefSeq; NP_830476.1; NC_004722.1.
DR AlphaFoldDB; Q81HW8; -.
DR SMR; Q81HW8; -.
DR STRING; 226900.BC_0662; -.
DR EnsemblBacteria; AAP07677; AAP07677; BC_0662.
DR KEGG; bce:BC0662; -.
DR PATRIC; fig|226900.8.peg.622; -.
DR HOGENOM; CLU_000604_92_3_9; -.
DR OMA; AKREIYQ; -.
DR Proteomes; UP000001417; 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..496
FT /note="Ribose import ATP-binding protein RbsA"
FT /id="PRO_0000261038"
FT DOMAIN 5..242
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 252..496
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 496 AA; 54587 MW; 0C72DE153539C0CE CRC64;
MGMHIEMKNI SKAFNGNPVL KNAQFMIETG EVHALMGENG AGKSTLMKIL TGVYKKDGGT
IKIDGQERTF KNAKEAEEYG IAFIHQELNI LPNLTVAENM FLGKELMYGK TGILRTRQMN
AIAQQQLAEL GLHVRGAMLA EELSVGQQQI IEIAKALMTN ASVIIMDEPT AALTDREIET
LFTVINKLRK EGVSFVYISH RMEEIFSICD AITILRDGEY VGKRLIPETS FDEVVSMMVG
RSIGERYPER NSQIGDVIFE MRNGTKKGKF ENVSFQVRKG EILGVAGLMG AGRTDIMKAI
FGYEPLDSGQ IFINGQEVKI DSPIDAIRQR IAFITEDRKS EGLVLDFSIR ENLALPNLEN
LSKGSVLSNE LEQQFTEDMM KLLNVKASSG EQAVKSLSGG NQQKIVIAKW LGIHPQLLIL
DEPTRGVDVG AKKEIYSIMN KLTEQGDAVI MVSSELPEVL GMSDRVLVIH EGKVGGILGK
DEASQESIMA LATGGE