RBSB_BACSU
ID RBSB_BACSU Reviewed; 305 AA.
AC P36949; P96730;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ribose import binding protein RbsB {ECO:0000250|UniProtKB:P02925};
DE Flags: Precursor;
GN Name=rbsB; OrderedLocusNames=BSU35960;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213.
RC STRAIN=168;
RX PubMed=7921236; DOI=10.1099/13500872-140-8-1829;
RA Woodson K., Devine K.M.;
RT "Analysis of a ribose transport operon from Bacillus subtilis.";
RL Microbiology 140:1829-1838(1994).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [5]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC import. Binds ribose. {ECO:0000250|UniProtKB:P02925}.
CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC transmembrane proteins (RbsC) and a solute-binding protein (RbsB) (By
CC similarity). Interacts with FloT (PubMed:23651456).
CC {ECO:0000250|UniProtKB:P02925, ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}; Lipid-anchor {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}; Lipid-
CC anchor. Note=Present in detergent-resistant membrane (DRM) fractions
CC that may be equivalent to eukaryotic membrane rafts; these rafts
CC include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; Z92953; CAB07461.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15613.1; -; Genomic_DNA.
DR EMBL; Z25798; CAA81053.1; -; Genomic_DNA.
DR PIR; A69690; A69690.
DR RefSeq; NP_391477.1; NC_000964.3.
DR RefSeq; WP_003242760.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P36949; -.
DR SMR; P36949; -.
DR IntAct; P36949; 1.
DR STRING; 224308.BSU35960; -.
DR jPOST; P36949; -.
DR PaxDb; P36949; -.
DR PRIDE; P36949; -.
DR EnsemblBacteria; CAB15613; CAB15613; BSU_35960.
DR GeneID; 936848; -.
DR KEGG; bsu:BSU35960; -.
DR PATRIC; fig|224308.179.peg.3893; -.
DR eggNOG; COG1879; Bacteria.
DR InParanoid; P36949; -.
DR OMA; QAVFAHN; -.
DR PhylomeDB; P36949; -.
DR BioCyc; BSUB:BSU35960-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..305
FT /note="Ribose import binding protein RbsB"
FT /id="PRO_0000031731"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 25..29
FT /note="QWAKP -> NGKR (in Ref. 3; CAA81053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 32227 MW; 5029290F1426090C CRC64;
MKKAVSVILT LSLFLLTACS LEPPQWAKPS NSGNKKEFTI GLSVSTLNNP FFVSLKKGIE
KEAKKRGMKV IIVDAQNDSS KQTSDVEDLI QQGVDALLIN PTDSSAISTA VESANAVGVP
VVTIDRSAEQ GKVETLVASD NVKGGEMAAA FIADKLGKGA KVAELEGVPG ASATRERGSG
FHNIADQKLQ VVTKQSADFD RTKGLTVMEN LLQGHPDIQA VFAHNDEMAL GALEAINSSG
KDILVIGFDG NKDALASIKD RKLSATVAQQ PELIGKLATE AADDILHGKK VQKTISAPLK
LETQK
