RBSA1_BURP1
ID RBSA1_BURP1 Reviewed; 859 AA.
AC Q3JSI8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ribose import ATP-binding protein RbsA 1 {ECO:0000255|HAMAP-Rule:MF_01716};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN Name=rbsA1 {ECO:0000255|HAMAP-Rule:MF_01716};
GN OrderedLocusNames=BURPS1710b_2070;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000124; ABA47978.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3JSI8; -.
DR SMR; Q3JSI8; -.
DR EnsemblBacteria; ABA47978; ABA47978; BURPS1710b_2070.
DR KEGG; bpm:BURPS1710b_2070; -.
DR HOGENOM; CLU_000604_92_3_4; -.
DR Proteomes; UP000002700; Chromosome I.
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; Repeat; Sugar transport; Translocase; Transport.
FT CHAIN 1..859
FT /note="Ribose import ATP-binding protein RbsA 1"
FT /id="PRO_0000261048"
FT DOMAIN 358..594
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 607..851
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT REGION 1..353
FT /note="Unknown"
FT REGION 1..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 859 AA; 96153 MW; 1A3DED56C5BDDDB8 CRC64;
MRASLENGDD HDAHRLVDAG FRPPGRPRAA RRRAFARARR GERRARGTAE DRHDVPGAEQ
PVLRDDAKGA RRGGRVDRRA GDRHRRASRR EQAGERRRGH AAEEDRHPAR EPDRFDGHPV
GRRVGEEGGR RRRRGGRERE RPGRRVRRLE EFRRGRDVVR LPREGDRRRR RSRDPRRHPG
RADSRARARL PRGAREIPER EDRRRAERQA GARERARRHR EHDPGAPVAQ GRLQRQRRRL
DGRAVRDRGV GPRHQAHERR RRAGGDRGDA EAELEVHRDV RAVPARPDSP RDRHRAREEV
GRQCAEGDSG RREADRQGQR EDVQLVSGPR DEADDMDEAS GAARAPDEAS EEAMDTILAL
TGITKRFPGV VALRGIDLRV ARGEIHALLG ENGAGKSTLM KILCGIHPPD EGVIALDGEP
RRFANHHDAI AAGVGIVFQE FSLIPELNAV DNLFLGREWR GRLGLRERAR MRRAAADIFA
RLDVAIDLSA PVRELSVAQQ QFVEIGKALS LDARLLILDE PTATLTPAEA AHLFGVMREL
KRRGVAMIFI SHHLDEIFEV CDRITVLRDG QYVGTTEVAR TDVGALVEMM VGRRIEQSFP
PKPRLARDAA PVLEVDALQV RENGPVNRFA LREGEILGFA GLVGSGRTSS ALALIGAKPA
RVRRMRVRGR PVCLADPAAA LAAGIGLLPE SRKTQGLIPA FSIRHNIAIN NLGKHRRLRW
FVDAAAETRT TLELMQRLGV KAPTPHTRVD TLSGGNQQKV VIARWLNHHT RILIFDEPTR
GIDIGAKAEI YQLMRELSAR GYSIVLISSE LPEIVGLCDR VAVFRQGRIE AMLEGEAIEP
NTVMTYATSD VRGANHEHA
