RBSA_LACLS
ID RBSA_LACLS Reviewed; 492 AA.
AC Q02XM9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=LACR_1800;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000425; ABJ73293.1; -; Genomic_DNA.
DR RefSeq; WP_011676541.1; NC_008527.1.
DR AlphaFoldDB; Q02XM9; -.
DR SMR; Q02XM9; -.
DR EnsemblBacteria; ABJ73293; ABJ73293; LACR_1800.
DR KEGG; llc:LACR_1800; -.
DR HOGENOM; CLU_000604_92_3_9; -.
DR OMA; AKREIYQ; -.
DR Proteomes; UP000000240; 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; 2.
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; Repeat;
KW Sugar transport; Translocase; Transport.
FT CHAIN 1..492
FT /note="Ribose import ATP-binding protein RbsA"
FT /id="PRO_0000277516"
FT DOMAIN 3..239
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 249..492
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 492 AA; 54163 MW; 141A6A5D8350D03B CRC64;
MKIEMKNISK SFGTNKVLEA IDLPINSGEV HALMGENGAG KSTLMNILTG LFPASGGEIE
IDKEDKTFKN PQEAEGFGIS FIHQEMNTWP DLTVLENLFL GREIKNKFGV LDTKAMRKKA
TFAFEQLGVT IDLDKEIGNL SVGQQQMVEI AKSFLSDLKI LIMDEPTAAL TERETERLFS
VIAGLKAQGV GIIYISHRME EIFKITDCVT VMRDGLVIDT KKTKETNVDE LVRKMVGRSI
TDYYPQKNAE IREIVFEAEN LSTADFKNIS FSVRSGEILG FAGLMGAGRT EVMRAIFGID
KLKSGTIKIN GKSLTINNPA QAIKAGIGFL TEDRKDEGLV LDFSIKDNIT LPSTKDFIHH
GLFDDKTATT FVKQLSERLN VKATDEEQMV GSLSGGNQQK VVLAKWIGIA PKVLILDEPT
RGVDVGAKRE IYQLMNELAE RGVPIIMISS DLPEILGVAD RIAVMHEGKI AGFLNKKEAT
QENVMQLATG GK