RBSC_ECOLI
ID RBSC_ECOLI Reviewed; 321 AA.
AC P0AGI1; P04984; Q2M868;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribose import permease protein RbsC {ECO:0000305};
GN Name=rbsC {ECO:0000303|PubMed:6327617}; OrderedLocusNames=b3750, JW3729;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3011793; DOI=10.1016/s0021-9258(19)57448-8;
RA Bell A.W., Buckel S.D., Groarke J.M., Hope J.N., Kingsley D.H.,
RA Hermodson M.A.;
RT "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia
RT coli K12.";
RL J. Biol. Chem. 261:7652-7658(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=6327617; DOI=10.1128/jb.158.2.674-682.1984;
RA Iida A., Harayama S., Iino T., Hazelbauer G.L.;
RT "Molecular cloning and characterization of genes required for ribose
RT transport and utilization in Escherichia coli K-12.";
RL J. Bacteriol. 158:674-682(1984).
RN [6]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=9922273; DOI=10.1128/jb.181.3.1039-1042.1999;
RA Park Y., Park C.;
RT "Topology of RbsC, a membrane component of the ribose transporter,
RT belonging to the AraH superfamily.";
RL J. Bacteriol. 181:1039-1042(1999).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25533465; DOI=10.1074/jbc.m114.621573;
RA Clifton M.C., Simon M.J., Erramilli S.K., Zhang H., Zaitseva J.,
RA Hermodson M.A., Stauffacher C.V.;
RT "In vitro reassembly of the ribose ATP-binding cassette transporter reveals
RT a distinct set of transport complexes.";
RL J. Biol. Chem. 290:5555-5565(2015).
RN [9]
RP RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT "Contact-dependent growth inhibition toxins exploit multiple independent
RT cell-entry pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC import. Probably responsible for the translocation of the substrate
CC across the membrane. {ECO:0000269|PubMed:25533465,
CC ECO:0000269|PubMed:6327617}.
CC -!- FUNCTION: (Microbial infection) Probably transports the toxic C-
CC terminal region of CdiA from D.dadantii strain 3937 across the inner
CC membrane to the cytoplasm, where CdiA has a toxic effect. Toxin
CC transport is strain-specific, mutations in this gene do not confer
CC resistance to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
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:0000269|PubMed:25533465}.
CC -!- INTERACTION:
CC P0AGI1; P04983: rbsA; NbExp=5; IntAct=EBI-21444614, EBI-1132449;
CC P0AGI1; P02925: rbsB; NbExp=6; IntAct=EBI-21444614, EBI-369930;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:9922273}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:9922273}.
CC -!- DISRUPTION PHENOTYPE: Disruption confers resistance to cellular
CC contact-dependent growth inhibition (CDI) CdiA of D.dadantii strain
CC 3937, but not to several other tested CdiA toxins.
CC {ECO:0000269|PubMed:26305955}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. AraH/RbsC subfamily. {ECO:0000305}.
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DR EMBL; M13169; AAA51474.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62103.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76773.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77538.1; -; Genomic_DNA.
DR PIR; G65178; G65178.
DR RefSeq; NP_418206.1; NC_000913.3.
DR RefSeq; WP_000211858.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0AGI1; -.
DR BioGRID; 4263450; 34.
DR ComplexPortal; CPX-4284; RbsABC ribose ABC transporter.
DR IntAct; P0AGI1; 2.
DR STRING; 511145.b3750; -.
DR TCDB; 3.A.1.2.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P0AGI1; -.
DR PaxDb; P0AGI1; -.
DR PRIDE; P0AGI1; -.
DR EnsemblBacteria; AAC76773; AAC76773; b3750.
DR EnsemblBacteria; BAE77538; BAE77538; BAE77538.
DR GeneID; 67417737; -.
DR GeneID; 948262; -.
DR KEGG; ecj:JW3729; -.
DR KEGG; eco:b3750; -.
DR PATRIC; fig|1411691.4.peg.2950; -.
DR EchoBASE; EB0809; -.
DR eggNOG; COG1172; Bacteria.
DR HOGENOM; CLU_028880_2_2_6; -.
DR InParanoid; P0AGI1; -.
DR OMA; FDVWNKR; -.
DR PhylomeDB; P0AGI1; -.
DR BioCyc; EcoCyc:RBSC-MON; -.
DR BioCyc; MetaCyc:RBSC-MON; -.
DR PRO; PR:P0AGI1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015591; F:D-ribose transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015752; P:D-ribose transmembrane transport; IDA:ComplexPortal.
DR InterPro; IPR001851; ABC_transp_permease.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Ribose import permease protein RbsC"
FT /id="PRO_0000060223"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 44..56
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 78..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 146..168
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 191..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 241..294
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9922273"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:9922273"
FT TOPO_DOM 317..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:9922273"
FT CONFLICT 202
FT /note="L -> V (in Ref. 1; AAA51474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 33452 MW; C7292EE5F0C78781 CRC64;
MTTQTVSGRR YFTKAWLMEQ KSLIALLVLI AIVSTLSPNF FTINNLFNIL QQTSVNAIMA
VGMTLVILTS GIDLSVGSLL ALTGAVAASI VGIEVNALVA VAAALALGAA IGAVTGVIVA
KGRVQAFIAT LVMMLLLRGV TMVYTNGSPV NTGFTENADL FGWFGIGRPL GVPTPVWIMG
IVFLAAWYML HHTRLGRYIY ALGGNEAATR LSGINVNKIK IIVYSLCGLL ASLAGIIEVA
RLSSAQPTAG TGYELDAIAA VVLGGTSLAG GKGRIVGTLI GALILGFLNN GLNLLGVSSY
YQMIVKAVVI LLAVLVDNKK Q
