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P0A7R5 (RS10_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S10
Gene names
Name:rpsJ
Synonyms:nusE
Ordered Locus Names:b3321, JW3283
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the binding of tRNA to the ribosomes. HAMAP-Rule MF_00508

Subunit structure

Part of the 30S ribosomal subunit By similarity. HAMAP-Rule MF_00508

Sequence similarities

Belongs to the ribosomal protein S10P family.

Mass spectrometry

Molecular mass is 11734.5 Da from positions 1 - 103. Determined by MALDI. Ref.9

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10310330S ribosomal protein S10 HAMAP-Rule MF_00508
PRO_0000146529

Secondary structure

................. 103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7R5 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DAEB35A2557F1D59

FASTA10311,736
        10         20         30         40         50         60 
MQNQRIRIRL KAFDHRLIDQ ATAEIVETAK RTGAQVRGPI PLPTRKERFT VLISPHVNKD 

        70         80         90        100 
ARDQYEIRTH LRLVDIVEPT EKTVDALMRL DLAAGVDVQI SLG 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of protein S10 from the small ribosomal subunit of Escherichia coli."
Yaguchi M., Roy C., Wittmann H.G.
FEBS Lett. 121:113-116(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon."
Olins P.O., Nomura M.
Cell 26:205-211(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"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 1-12.
Strain: K12 / EMG2.
[7]Noorani S.M., Lindahl L., Zengel J.M.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
Strain: ECOR 30.
[8]"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.
[9]"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
Arnold R.J., Reilly J.P.
Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[10]"All-atom homology model of the Escherichia coli 30S ribosomal subunit."
Tung C.-S., Joseph S., Sanbonmatsu K.Y.
Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[12]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00344 Genomic DNA. Translation: CAA23633.1.
X02613 Genomic DNA. Translation: CAA26459.1.
U18997 Genomic DNA. Translation: AAA58118.1.
U00096 Genomic DNA. Translation: AAC76346.1.
AP009048 Genomic DNA. Translation: BAE77970.1.
AF058450 Genomic DNA. Translation: AAC14290.1.
PIRR3EC10. A02720.
RefSeqNP_417780.1. NC_000913.3.
YP_492111.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-J5-102[»]
1P6Gelectron microscopy12.30J1-103[»]
1P87electron microscopy11.50J1-103[»]
1VS5X-ray3.46J1-103[»]
1VS7X-ray3.46J1-103[»]
2AVYX-ray3.46J1-103[»]
2AW7X-ray3.46J1-103[»]
2GY9electron microscopy15.00J5-100[»]
2GYBelectron microscopy15.00J5-100[»]
2I2PX-ray3.22J1-103[»]
2I2UX-ray3.22J1-103[»]
2KVQNMR-E1-103[»]
2QALX-ray3.21J1-103[»]
2QANX-ray3.21J1-103[»]
2QB9X-ray3.54J1-103[»]
2QBBX-ray3.54J1-103[»]
2QBDX-ray3.30J1-103[»]
2QBFX-ray3.30J1-103[»]
2QBHX-ray4.00J1-103[»]
2QBJX-ray4.00J1-103[»]
2QOUX-ray3.93J1-103[»]
2QOWX-ray3.93J1-103[»]
2QOYX-ray3.50J1-103[»]
2QP0X-ray3.50J1-103[»]
2VHOX-ray3.74J1-103[»]
2VHPX-ray3.74J1-103[»]
2WWLelectron microscopy5.80J5-102[»]
2YKRelectron microscopy9.80J5-102[»]
2Z4KX-ray4.45J1-103[»]
2Z4MX-ray4.45J1-103[»]
3D3BX-ray1.30J1-103[»]
3D3CX-ray2.60J/K/L1-103[»]
3DF1X-ray3.50J1-103[»]
3DF3X-ray3.50J1-103[»]
3E1Aelectron microscopy-X1-103[»]
3E1Celectron microscopy-X1-103[»]
3FIHelectron microscopy6.70J5-102[»]
3I1MX-ray3.19J1-103[»]
3I1OX-ray3.19J1-103[»]
3I1QX-ray3.81J1-103[»]
3I1SX-ray3.81J1-103[»]
3I1ZX-ray3.71J1-103[»]
3I21X-ray3.71J1-103[»]
3IMQX-ray2.50J/K/L1-103[»]
3IZVelectron microscopy-N1-103[»]
3IZWelectron microscopy-N1-103[»]
3J00electron microscopy-J1-103[»]
3J0Uelectron microscopy12.10M1-103[»]
3J0Velectron microscopy14.70M1-103[»]
3J0Xelectron microscopy13.50M1-103[»]
3J0Zelectron microscopy11.50M1-103[»]
3J10electron microscopy11.50M1-103[»]
3J13electron microscopy13.10L1-103[»]
3J18electron microscopy8.30J5-102[»]
3J36electron microscopy9.80J1-103[»]
3J4Velectron microscopy12.00J5-102[»]
3J4Welectron microscopy12.00J5-102[»]
3J4Yelectron microscopy17.00J5-102[»]
3J4Zelectron microscopy20.00J5-102[»]
3J53electron microscopy13.00J5-102[»]
3J55electron microscopy15.00J5-102[»]
3J57electron microscopy17.00J5-102[»]
3J59electron microscopy12.00J5-102[»]
3J5Belectron microscopy17.00J5-102[»]
3J5Delectron microscopy17.00J5-102[»]
3J5Felectron microscopy20.00J5-102[»]
3J5Helectron microscopy15.00J5-102[»]
3J5Jelectron microscopy9.00J5-102[»]
3J5Nelectron microscopy6.80J1-103[»]
3J5Telectron microscopy7.60J1-103[»]
3J5Xelectron microscopy7.60J1-103[»]
3KC4electron microscopy-J1-103[»]
3OAQX-ray3.25J5-102[»]
3OARX-ray3.25J5-102[»]
3OFAX-ray3.19J5-102[»]
3OFBX-ray3.19J5-102[»]
3OFOX-ray3.10J5-102[»]
3OFPX-ray3.10J5-102[»]
3OFXX-ray3.29J5-102[»]
3OFYX-ray3.29J5-102[»]
3OR9X-ray3.30J1-103[»]
3ORAX-ray3.30J1-103[»]
3SFSX-ray3.20J1-103[»]
3UOQX-ray3.70J1-103[»]
3W1YX-ray2.30C1-103[»]
4A2Ielectron microscopy16.50J5-102[»]
4ADVelectron microscopy13.50J1-103[»]
4GAQX-ray3.30J1-103[»]
4GASX-ray3.30J1-103[»]
4GD1X-ray3.00J5-102[»]
4GD2X-ray3.00J5-102[»]
4KIYX-ray2.90J1-103[»]
4KJ0X-ray2.90J1-103[»]
4KJ2X-ray2.90J1-103[»]
4KJ4X-ray2.90J1-103[»]
4KJ6X-ray2.90J1-103[»]
4KJ8X-ray2.90J1-103[»]
4KJAX-ray2.90J1-103[»]
4KJCX-ray2.90J1-103[»]
ProteinModelPortalP0A7R5.
SMRP0A7R5. Positions 5-100.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852128. 1 interaction.
DIPDIP-35797N.
IntActP0A7R5. 98 interactions.
MINTMINT-1283940.
STRING511145.b3321.

Chemistry

ChEMBLCHEMBL2363135.
DrugBankDB00698. Nitrofurantoin.

Proteomic databases

PaxDbP0A7R5.
PRIDEP0A7R5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76346; AAC76346; b3321.
BAE77970; BAE77970; BAE77970.
GeneID12932299.
947816.
KEGGecj:Y75_p3855.
eco:b3321.
PATRIC32122074. VBIEscCol129921_3414.

Organism-specific databases

EchoBASEEB0902.
EcoGeneEG10909. rpsJ.

Phylogenomic databases

eggNOGCOG0051.
HOGENOMHOG000270246.
KOK02946.
OMAIESLMHI.
OrthoDBEOG6VXFHB.
PhylomeDBP0A7R5.
ProtClustDBPRK00596.

Enzyme and pathway databases

BioCycEcoCyc:EG10909-MONOMER.
ECOL316407:JW3283-MONOMER.

Gene expression databases

GenevestigatorP0A7R5.

Family and domain databases

Gene3D3.30.70.600. 1 hit.
HAMAPMF_00508. Ribosomal_S10.
InterProIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
[Graphical view]
PANTHERPTHR11700. PTHR11700. 1 hit.
PfamPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSPR00971. RIBOSOMALS10.
SUPFAMSSF54999. SSF54999. 1 hit.
TIGRFAMsTIGR01049. rpsJ_bact. 1 hit.
PROSITEPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7R5.
PROP0A7R5.

Entry information

Entry nameRS10_ECOLI
AccessionPrimary (citable) accession number: P0A7R5
Secondary accession number(s): P02364, Q2M6Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene