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Protein

Ribose import binding protein RbsB

Gene

rbsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:RBSB-MONOMER.
ECOL316407:JW3730-MONOMER.
MetaCyc:RBSB-MONOMER.

Protein family/group databases

TCDBi3.A.1.2.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose import binding protein RbsBCurated
Gene namesi
Name:rbsB1 Publication
Synonyms:prlB, rbsP
Ordered Locus Names:b3751, JW3730
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10815. rbsB.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

  • integral component of membrane Source: GO_Central
  • membrane Source: UniProtKB
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 PublicationsAdd
BLAST
Chaini26 – 296271Ribose import binding protein RbsBPRO_0000031732Add
BLAST

Proteomic databases

EPDiP02925.
PaxDbiP02925.
PRIDEiP02925.

2D gel databases

SWISS-2DPAGEP02925.

Interactioni

Subunit structurei

The complex is composed of an ATP-binding protein (RbsA), two transmembrane proteins (RbsC) and a solute-binding protein (RbsB).1 Publication

Protein-protein interaction databases

BioGridi4262120. 14 interactions.
DIPiDIP-10641N.
IntActiP02925. 16 interactions.
MINTiMINT-1244685.
STRINGi511145.b3751.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 347Combined sources
Beta strandi36 – 383Combined sources
Helixi39 – 5517Combined sources
Beta strandi58 – 636Combined sources
Helixi68 – 7811Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 886Combined sources
Turni93 – 964Combined sources
Helixi97 – 1059Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1286Combined sources
Helixi130 – 14516Combined sources
Beta strandi150 – 1556Combined sources
Helixi161 – 17717Combined sources
Beta strandi180 – 1867Combined sources
Helixi191 – 20414Combined sources
Beta strandi210 – 2156Combined sources
Helixi216 – 22914Combined sources
Beta strandi235 – 2406Combined sources
Helixi243 – 2508Combined sources
Beta strandi256 – 2594Combined sources
Helixi262 – 27716Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi291 – 2933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BA2X-ray2.10A/B26-296[»]
1DBPX-ray2.20A26-296[»]
1DRJX-ray2.50A26-296[»]
1DRKX-ray2.00A26-296[»]
1URPX-ray2.30A/B/C/D26-296[»]
2DRIX-ray1.60A26-296[»]
2GX6X-ray1.97A26-296[»]
ProteinModelPortaliP02925.
SMRiP02925. Positions 26-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02925.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E9V. Bacteria.
COG1879. LUCA.
HOGENOMiHOG000212345.
InParanoidiP02925.
KOiK10439.
OMAiMENILQS.
OrthoDBiEOG61P6T8.
PhylomeDBiP02925.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMKKLATLV SAVALSATVS ANAMAKDTIA LVVSTLNNPF FVSLKDGAQK
60 70 80 90 100
EADKLGYNLV VLDSQNNPAK ELANVQDLTV RGTKILLINP TDSDAVGNAV
110 120 130 140 150
KMANQANIPV ITLDRQATKG EVVSHIASDN VLGGKIAGDY IAKKAGEGAK
160 170 180 190 200
VIELQGIAGT SAARERGEGF QQAVAAHKFN VLASQPADFD RIKGLNVMQN
210 220 230 240 250
LLTAHPDVQA VFAQNDEMAL GALRALQTAG KSDVMVVGFD GTPDGEKAVN
260 270 280 290
DGKLAATIAQ LPDQIGAKGV ETADKVLKGE KVQAKYPVDL KLVVKQ
Length:296
Mass (Da):30,950
Last modified:July 21, 1986 - v1
Checksum:iE5FA305A64EF3ACE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00511 Genomic DNA. Translation: AAA50966.1.
M13169 Genomic DNA. Translation: AAA51475.1.
L10328 Genomic DNA. Translation: AAA62104.1.
U00096 Genomic DNA. Translation: AAC76774.1.
AP009048 Genomic DNA. Translation: BAE77537.1.
PIRiA03425. JGECR.
RefSeqiNP_418207.1. NC_000913.3.
WP_001056271.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76774; AAC76774; b3751.
BAE77537; BAE77537; BAE77537.
GeneIDi948261.
KEGGiecj:JW3730.
eco:b3751.
PATRICi32123001. VBIEscCol129921_3876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00511 Genomic DNA. Translation: AAA50966.1.
M13169 Genomic DNA. Translation: AAA51475.1.
L10328 Genomic DNA. Translation: AAA62104.1.
U00096 Genomic DNA. Translation: AAC76774.1.
AP009048 Genomic DNA. Translation: BAE77537.1.
PIRiA03425. JGECR.
RefSeqiNP_418207.1. NC_000913.3.
WP_001056271.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BA2X-ray2.10A/B26-296[»]
1DBPX-ray2.20A26-296[»]
1DRJX-ray2.50A26-296[»]
1DRKX-ray2.00A26-296[»]
1URPX-ray2.30A/B/C/D26-296[»]
2DRIX-ray1.60A26-296[»]
2GX6X-ray1.97A26-296[»]
ProteinModelPortaliP02925.
SMRiP02925. Positions 26-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262120. 14 interactions.
DIPiDIP-10641N.
IntActiP02925. 16 interactions.
MINTiMINT-1244685.
STRINGi511145.b3751.

Protein family/group databases

TCDBi3.A.1.2.1. the atp-binding cassette (abc) superfamily.

2D gel databases

SWISS-2DPAGEP02925.

Proteomic databases

EPDiP02925.
PaxDbiP02925.
PRIDEiP02925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76774; AAC76774; b3751.
BAE77537; BAE77537; BAE77537.
GeneIDi948261.
KEGGiecj:JW3730.
eco:b3751.
PATRICi32123001. VBIEscCol129921_3876.

Organism-specific databases

EchoBASEiEB0808.
EcoGeneiEG10815. rbsB.

Phylogenomic databases

eggNOGiENOG4105E9V. Bacteria.
COG1879. LUCA.
HOGENOMiHOG000212345.
InParanoidiP02925.
KOiK10439.
OMAiMENILQS.
OrthoDBiEOG61P6T8.
PhylomeDBiP02925.

Enzyme and pathway databases

BioCyciEcoCyc:RBSB-MONOMER.
ECOL316407:JW3730-MONOMER.
MetaCyc:RBSB-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02925.
PROiP02925.

Family and domain databases

InterProiIPR028082. Peripla_BP_I.
IPR025997. SBP_2_dom.
[Graphical view]
PfamiPF13407. Peripla_BP_4. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The amino acid sequence of D-ribose-binding protein from Escherichia coli K12."
    Groarke J.M., Mahoney W.C., Hope J.N., Furlong C.E., Robb F.T., Zalkin H., Hermodson M.A.
    J. Biol. Chem. 258:12952-12956(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Mauzy C.A.
    Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12."
    Bell A.W., Buckel S.D., Groarke J.M., Hope J.N., Kingsley D.H., Hermodson M.A.
    J. Biol. Chem. 261:7652-7658(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
    Strain: K12.
  7. "Ribokinase from Escherichia coli K12. Nucleotide sequence and overexpression of the rbsK gene and purification of ribokinase."
    Hope J.N., Bell A.W., Hermodson M.A., Groarke J.M.
    J. Biol. Chem. 261:7663-7668(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-296.
    Strain: K12.
  8. "FIS is a regulator of metabolism in Escherichia coli."
    Gonzalez-Gil G., Bringmann P., Kahmann R.
    Mol. Microbiol. 22:21-29(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-39.
    Strain: K12.
  9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-37.
    Strain: K12 / EMG2.
  10. "Purification and properties of a ribose-binding protein from Escherichia coli."
    Willis R.C., Furlong C.E.
    J. Biol. Chem. 249:6926-6929(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Molecular cloning and characterization of genes required for ribose transport and utilization in Escherichia coli K-12."
    Iida A., Harayama S., Iino T., Hazelbauer G.L.
    J. Bacteriol. 158:674-682(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes."
    Clifton M.C., Simon M.J., Erramilli S.K., Zhang H., Zaitseva J., Hermodson M.A., Stauffacher C.V.
    J. Biol. Chem. 290:5555-5565(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  14. "1.7-A X-ray structure of the periplasmic ribose receptor from Escherichia coli."
    Mowbray S.L., Cole L.B.
    J. Mol. Biol. 225:155-175(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBCELLULAR LOCATION.
  15. "Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis."
    Bjoerkman A.J., Binnie R.A., Zhang H., Cole L.B., Hermodson M.A., Mowbray S.L.
    J. Biol. Chem. 269:30206-30211(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION.
  16. "Multiple open forms of ribose-binding protein trace the path of its conformational change."
    Bjoerkman A.J., Mowbray S.L.
    J. Mol. Biol. 279:651-664(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiRBSB_ECOLI
AccessioniPrimary (citable) accession number: P02925
Secondary accession number(s): Q2M869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.