RBSA2_THEMA
ID RBSA2_THEMA Reviewed; 523 AA.
AC Q9X051;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ribose import ATP-binding protein RbsA 2 {ECO:0000255|HAMAP-Rule:MF_01716};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN Name=rbsA2 {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=TM_0956;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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DR EMBL; AE000512; AAD36035.1; -; Genomic_DNA.
DR PIR; E72314; E72314.
DR RefSeq; NP_228764.1; NC_000853.1.
DR RefSeq; WP_004080606.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X051; -.
DR SMR; Q9X051; -.
DR STRING; 243274.THEMA_09565; -.
DR TCDB; 3.A.1.2.19; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAD36035; AAD36035; TM_0956.
DR KEGG; tma:TM0956; -.
DR eggNOG; COG1129; Bacteria.
DR InParanoid; Q9X051; -.
DR OMA; AKREIYQ; -.
DR OrthoDB; 551294at2; -.
DR Proteomes; UP000008183; 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..523
FT /note="Ribose import ATP-binding protein RbsA 2"
FT /id="PRO_0000261114"
FT DOMAIN 13..249
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 266..513
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 523 AA; 58545 MW; 0037F39AECBC647C CRC64;
MMLNTEKERE VLLEARNITK TFPGVIAVNN VTLQIYKGEV CALVGENGAG KSTLMKILAG
VYPDYEGQIF LEGKEVRFRN PREAQENGIA LIPQELDLVP NLSSAENIFL SREPVNEFGV
IEYQKMFEQA SKLFSKLGVN IDPKTKVEDL STSQQQMVAI AKALSLDAKI IIMDEPTSAI
GKRETEQLFN IIRSLKNEGK SVIYISHRLE EIFEIADRVV VMRDGRKVGE GPIEEFDHDK
LVRLMVGRSI DQFFIKERAT ITDEIFRVEG IKLWSLDRKK LLVDDVSFYV RKGEVLGIYG
LVGAGRTELL EAIFGAHPGR TEGKVFIGGK EIKIHSPRDA VKNGIGLVPE DRKTAGLILQ
MSVLHNITLP SVVMKLIVRK FGLIDSQLEK EIVRSFIEKL NIKTPSPYQI VENLSGGNQQ
KVVLAKWLAI KPKVLLLDEP TRGIDVNAKS EIYKLISEMA VSGMGVVMVS SELPEILAMS
DRILVMSEGR KTAEFLREEV TEEDLLKAAI PRSVKVETTQ REE