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P0A7V0 (RS2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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 S2
Gene names
Name:rpsB
Ordered Locus Names:b0169, JW0164
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Part of the 30S ribosomal subunit. Some nascent polypeptide chains are able to cross-link to this protein in situ.

Sequence similarities

Belongs to the ribosomal protein S2P family.

Mass spectrometry

Molecular mass is 26610.5 Da from positions 2 - 241. Determined by MALDI. Ref.12

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hslRP0ACG82EBI-543439,EBI-562824

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8
Chain2 – 24124030S ribosomal protein S2 HAMAP-Rule MF_00291_B
PRO_0000134165

Amino acid modifications

Modified residue1151N6-succinyllysine Ref.14

Secondary structure

....................................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7V0 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 87A38C696115212E

FASTA24126,744
        10         20         30         40         50         60 
MATVSMRDML KAGVHFGHQT RYWNPKMKPF IFGARNKVHI INLEKTVPMF NEALAELNKI 

        70         80         90        100        110        120 
ASRKGKILFV GTKRAASEAV KDAALSCDQF FVNHRWLGGM LTNWKTVRQS IKRLKDLETQ 

       130        140        150        160        170        180 
SQDGTFDKLT KKEALMRTRE LEKLENSLGG IKDMGGLPDA LFVIDADHEH IAIKEANNLG 

       190        200        210        220        230        240 
IPVFAIVDTN SDPDGVDFVI PGNDDAIRAV TLYLGAVAAT VREGRSQDLA SQAEESFVEA 


E 

« Hide

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts."
An G., Bendiak D.S., Mamelak L.A., Friesen J.D.
Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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]"Primary structure of protein S2 from the Escherichia coli ribosome."
Wittmann-Liebold B., Bosserhoff A.
FEBS Lett. 129:10-16(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-241.
Strain: K12.
[7]"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit."
Ueshima R., Fujita N., Ishihama A.
Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
[8]"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 2-13.
Strain: K12 / EMG2.
[9]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-35, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[10]"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.
[11]"Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
[12]"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.
[13]"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.
[14]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-115.
Strain: K12.
[15]"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.
[16]"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
V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.
PIRR3EC2. A02696.
RefSeqNP_414711.1. NC_000913.3.
YP_488471.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-B6-214[»]
1P87electron microscopy11.50B2-241[»]
1VS5X-ray3.46B1-241[»]
1VS7X-ray3.46B1-241[»]
2AVYX-ray3.46B2-241[»]
2AW7X-ray3.46B2-241[»]
2GY9electron microscopy15.00B6-241[»]
2GYBelectron microscopy15.00B6-241[»]
2I2PX-ray3.22B2-241[»]
2I2UX-ray3.22B2-241[»]
2QALX-ray3.21B2-241[»]
2QANX-ray3.21B2-241[»]
2QB9X-ray3.54B2-241[»]
2QBBX-ray3.54B2-241[»]
2QBDX-ray3.30B2-241[»]
2QBFX-ray3.30B2-241[»]
2QBHX-ray4.00B2-241[»]
2QBJX-ray4.00B2-241[»]
2QOUX-ray3.93B2-241[»]
2QOWX-ray3.93B2-241[»]
2QOYX-ray3.50B2-241[»]
2QP0X-ray3.50B2-241[»]
2VHOX-ray3.74B2-241[»]
2VHPX-ray3.74B2-241[»]
2WWLelectron microscopy5.80B9-226[»]
2YKRelectron microscopy9.80B9-226[»]
2Z4KX-ray4.45B2-241[»]
2Z4MX-ray4.45B2-241[»]
3DF1X-ray3.50B2-241[»]
3DF3X-ray3.50B2-240[»]
3E1Aelectron microscopy-B1-241[»]
3E1Celectron microscopy-B1-241[»]
3FIHelectron microscopy6.70B9-226[»]
3I1MX-ray3.19B1-241[»]
3I1OX-ray3.19B1-241[»]
3I1QX-ray3.81B1-241[»]
3I1SX-ray3.81B1-241[»]
3I1ZX-ray3.71B1-241[»]
3I21X-ray3.71B1-241[»]
3IZVelectron microscopy-F1-241[»]
3IZWelectron microscopy-F1-241[»]
3J00electron microscopy-B2-241[»]
3J0Uelectron microscopy12.10E2-241[»]
3J0Velectron microscopy14.70E2-241[»]
3J0Xelectron microscopy13.50E2-241[»]
3J0Zelectron microscopy11.50E2-241[»]
3J10electron microscopy11.50E2-241[»]
3J13electron microscopy13.10D2-241[»]
3J18electron microscopy8.30B9-226[»]
3J36electron microscopy9.80B2-241[»]
3J4Velectron microscopy12.00B9-226[»]
3J4Welectron microscopy12.00B9-226[»]
3J4Yelectron microscopy17.00B9-226[»]
3J4Zelectron microscopy20.00B9-226[»]
3J53electron microscopy13.00B9-226[»]
3J55electron microscopy15.00B9-226[»]
3J57electron microscopy17.00B9-226[»]
3J59electron microscopy12.00B9-226[»]
3J5Belectron microscopy17.00B9-226[»]
3J5Delectron microscopy17.00B9-226[»]
3J5Felectron microscopy20.00B9-226[»]
3J5Helectron microscopy15.00B9-226[»]
3J5Jelectron microscopy9.00B9-226[»]
3J5Nelectron microscopy6.80B1-241[»]
3J5Telectron microscopy7.60B2-241[»]
3J5Xelectron microscopy7.60B2-241[»]
3KC4electron microscopy-B1-241[»]
3OAQX-ray3.25B9-226[»]
3OARX-ray3.25B9-226[»]
3OFAX-ray3.19B9-226[»]
3OFBX-ray3.19B9-226[»]
3OFOX-ray3.10B9-226[»]
3OFPX-ray3.10B9-226[»]
3OFXX-ray3.29B9-226[»]
3OFYX-ray3.29B9-226[»]
3OR9X-ray3.30B1-241[»]
3ORAX-ray3.30B1-241[»]
3SFSX-ray3.20B1-241[»]
3UOQX-ray3.70B1-241[»]
4A2Ielectron microscopy16.50B9-226[»]
4ADVelectron microscopy13.50B2-241[»]
4GAQX-ray3.30B1-241[»]
4GASX-ray3.30B1-241[»]
4GD1X-ray3.00B9-226[»]
4GD2X-ray3.00B9-226[»]
4KIYX-ray2.90B1-241[»]
4KJ0X-ray2.90B1-241[»]
4KJ2X-ray2.90B1-241[»]
4KJ4X-ray2.90B1-241[»]
4KJ6X-ray2.90B1-241[»]
4KJ8X-ray2.90B1-241[»]
4KJAX-ray2.90B1-241[»]
4KJCX-ray2.90B1-241[»]
ProteinModelPortalP0A7V0.
SMRP0A7V0. Positions 2-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852185. 1 interaction.
DIPDIP-6877N.
IntActP0A7V0. 206 interactions.
STRING511145.b0169.

Chemistry

ChEMBLCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0A7V0.

Proteomic databases

PaxDbP0A7V0.
PRIDEP0A7V0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.
GeneID12931818.
947874.
KEGGecj:Y75_p0165.
eco:b0169.
PATRIC32115445. VBIEscCol129921_0174.

Organism-specific databases

EchoBASEEB0894.
EcoGeneEG10901. rpsB.

Phylogenomic databases

eggNOGCOG0052.
HOGENOMHOG000071892.
KOK02967.
OMAFVNYRWL.
OrthoDBEOG6XWV6P.
PhylomeDBP0A7V0.

Enzyme and pathway databases

BioCycEcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.

Gene expression databases

GenevestigatorP0A7V0.

Family and domain databases

HAMAPMF_00291_B. Ribosomal_S2_B.
InterProIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERPTHR12534. PTHR12534. 1 hit.
PfamPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSPR00395. RIBOSOMALS2.
SUPFAMSSF52313. SSF52313. 1 hit.
TIGRFAMsTIGR01011. rpsB_bact. 1 hit.
PROSITEPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7V0.
PROP0A7V0.

Entry information

Entry nameRS2_ECOLI
AccessionPrimary (citable) accession number: P0A7V0
Secondary accession number(s): P02351, Q9R2E5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 2 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