RBSA_ROSDO
ID RBSA_ROSDO Reviewed; 511 AA.
AC Q164K3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=RD1_3079;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000362; ABG32590.1; -; Genomic_DNA.
DR RefSeq; WP_011569206.1; NZ_FOOO01000004.1.
DR AlphaFoldDB; Q164K3; -.
DR SMR; Q164K3; -.
DR STRING; 375451.RD1_3079; -.
DR EnsemblBacteria; ABG32590; ABG32590; RD1_3079.
DR KEGG; rde:RD1_3079; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_5; -.
DR OMA; QFMSELV; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000007029; 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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..511
FT /note="Ribose import ATP-binding protein RbsA"
FT /id="PRO_0000261094"
FT DOMAIN 13..249
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 260..503
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 511 AA; 54817 MW; 2FA0C7E9DC758E24 CRC64;
MSKHTLSADV PVVSMDAITK TFPGVKALDQ VRLDLYPGQV TALVGENGAG KSTTVKILTG
IYQPDGGTIR IAGAPVILNT PNDASAAGIT AIHQETVLFD ELTVAENIFI GHAPRTKWGL
IDKAAMHRKA RGLLDEIGAP FDTGAYLREL GIANKHLVAI ARALSVDARV VIMDEPTAAL
SHKEIEELYE LVETLKAQGK AILFISHKFD EIFRIADRYT VFRDGAFVSD GLISDIDQDA
LVKMMVGRAV DHIFPERQAA LGEEVLQVAG YAHPTEFAGI GFTLKRGEIL GFYGLVGAGR
SELMQALFGI TRPSKGVTKI NGDIRVIRSP ADAVNNGIVY VPEDRGKQGV VIGLPIFQNI
TLPSLGRTSQ SGFLRMAEEF KLARDYAERL DLRAAALDQD VGNLSGGNQQ KVVIAKWLAT
QPQVIILDEP TKGIDIGSKA AVHEFMAELA GQGLAVIMVS SEIPEVIGMS DRVIVMREGR
IAAEVQGEDL TPETLVRHAA GIAPAPESIP A