30S ribosomal protein S8 - Escherichia coli (strain K12)

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P0A7W7 (RS8_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
30S ribosomal protein S8

Gene names

Name:	rpsH
Ordered Locus Names:	b3306, JW3268

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit By similarity. HAMAP MF_01302_B Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA. HAMAP MF_01302_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S5 and S12 By similarity.
Sequence similarities	Belongs to the ribosomal protein S8P family.
Mass spectrometry	Molecular mass is 13993.2 Da from positions 2 - 130. Determined by MALDI. Ref.7

Ontologies

Keywords
Biological process	Translation regulation
Ligand	RNA-binding rRNA-binding
Molecular function	Repressor Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of mRNA stability Inferred from mutant phenotype. Source: EcoliWiki translation Inferred from direct assay. Source: EcoliWiki
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay. Source: EcoliWiki
Molecular function	rRNA binding Inferred from direct assay. Source: EcoliWiki structural constituent of ribosome Inferred from electronic annotation. Source: InterPro translation repressor activity Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 130

129

30S ribosomal protein S8 HAMAP MF_01302_B

PRO_0000126405

Experimental info

Sequence conflict

E → Q in CAA25719. Ref.1

Secondary structure

130

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7W7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 74641BC5021DA651
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FASTA

130

14,127

        10         20         30         40         50         60 
MSMQDPIADM LTRIRNGQAA NKAAVTMPSS KLKVAIANVL KEEGFIEDFK VEGDTKPELE 

        70         80         90        100        110        120 
LTLKYFQGKA VVESIQRVSR PGLRIYKRKD ELPKVMAGLG IAVVSTSKGV MTDRAARQAG 

       130 
LGGEIICYVA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene." Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M. Nucleic Acids Res. 11:2599-2616(1983) [PubMed: 6222285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The amino acid sequence of the ribosomal protein S8 of Escherichia coli." Allen G., Wittmann-Liebold B. Hoppe-Seyler's Z. Physiol. Chem. 359:1509-1525(1978) [PubMed: 365698] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-130. Strain: K.
[5]	"Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA." Olins P.O., Nomura M. Nucleic Acids Res. 9:1757-1764(1981) [PubMed: 6262737] [Abstract] Cited for: MECHANISM OF TRANSLATION REGULATION.
[6]	"Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operon." Wower I., Kowaleski M.P., Sears L.E., Zimmermann R.A. J. Bacteriol. 174:1213-1221(1992) [PubMed: 1735715] [Abstract] Cited for: MUTAGENESIS.
[7]	"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: 10094780] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[8]	"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: 12244297] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[9]	"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: 12809609] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[10]	"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: 16272117] [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

X01563 Genomic DNA. Translation: CAA25719.1.
U18997 Genomic DNA. Translation: AAA58103.1.
U00096 Genomic DNA. Translation: AAC76331.1.
AP009048 Genomic DNA. Translation: BAE77985.1.

PIR

R3EC8. E65123.

RefSeq

NP_417765.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	H	2-130	[»]
1P6G	electron microscopy	12.30	H	2-130	[»]
1P87	electron microscopy	11.50	H	2-130	[»]
1S03	X-ray	2.70	G/H	2-129	[»]
1VS5	X-ray	3.46	H	1-130	[»]
1VS7	X-ray	3.46	H	1-130	[»]
2AVY	X-ray	3.46	H	2-130	[»]
2AW7	X-ray	3.46	H	2-130	[»]
2GY9	electron microscopy	15.00	H	3-128	[»]
2GYB	electron microscopy	15.00	H	3-128	[»]
2I2P	X-ray	3.22	H	2-129	[»]
2I2U	X-ray	3.22	H	2-129	[»]
2QAL	X-ray	3.21	H	2-130	[»]
2QAN	X-ray	3.21	H	2-130	[»]
2QB9	X-ray	3.54	H	2-130	[»]
2QBB	X-ray	3.54	H	2-130	[»]
2QBD	X-ray	3.30	H	2-130	[»]
2QBF	X-ray	3.30	H	2-130	[»]
2QBH	X-ray	4.00	H	2-130	[»]
2QBJ	X-ray	4.00	H	2-130	[»]
2QOU	X-ray	3.93	H	2-130	[»]
2QOW	X-ray	3.93	H	2-130	[»]
2QOY	X-ray	3.50	H	2-130	[»]
2QP0	X-ray	3.50	H	2-130	[»]
2VHO	X-ray	3.74	H	2-130	[»]
2VHP	X-ray	3.74	H	2-130	[»]
2WWL	electron microscopy	5.80	H	2-130	[»]
2YKR	electron microscopy	9.80	H	2-130	[»]
2Z4K	X-ray	4.45	H	2-130	[»]
2Z4M	X-ray	4.45	H	2-130	[»]
3DF1	X-ray	3.50	H	2-129	[»]
3DF3	X-ray	3.50	H	2-129	[»]
3FIH	electron microscopy	6.70	H	2-130	[»]
3I1M	X-ray	3.19	H	1-130	[»]
3I1O	X-ray	3.19	H	1-130	[»]
3I1Q	X-ray	3.81	H	1-130	[»]
3I1S	X-ray	3.81	H	1-130	[»]
3I1Z	X-ray	3.71	H	1-130	[»]
3I21	X-ray	3.71	H	1-130	[»]
3IZV	electron microscopy	-	L	1-130	[»]
3IZW	electron microscopy	-	L	1-130	[»]
3J00	electron microscopy	-	H	2-130	[»]
3KC4	electron microscopy	-	H	1-130	[»]
3OAQ	X-ray	3.25	H	2-130	[»]
3OAR	X-ray	3.25	H	2-130	[»]
3OFA	X-ray	3.19	H	2-130	[»]
3OFB	X-ray	3.19	H	2-130	[»]
3OFO	X-ray	3.10	H	2-130	[»]
3OFP	X-ray	3.10	H	2-130	[»]
3OFX	X-ray	3.29	H	2-130	[»]
3OFY	X-ray	3.29	H	2-130	[»]
3OR9	X-ray	3.30	H	1-130	[»]
3ORA	X-ray	3.30	H	1-130	[»]
3R8N	X-ray	3.00	H	2-130	[»]
3R8O	X-ray	3.00	H	2-130	[»]
4A2I	electron microscopy	16.50	H	2-130	[»]

ProteinModelPortal

P0A7W7.

SMR

P0A7W7. Positions 3-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47901N.

IntAct

P0A7W7. 23 interactions.

MINT

MINT-1318565.

2D gel databases

ECO2DBASE

I013.5. 6TH EDITION.

Proteomic databases

PRIDE

P0A7W7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001349; EBESCP00000001349; EBESCG00000001121.
EBESCT00000016714; EBESCP00000016005; EBESCG00000015773.

GeneID

947802.

GenomeReviews

Gene locus JW3268 in contig AP009048_GR.
Gene locus b3306 in contig U00096_GR.

KEGG

ecj:JW3268.
eco:b3306.

PATRIC

32122044. VBIEscCol129921_3399.

Organism-specific databases

EchoBASE

EB0900.

EcoGene

EG10907. rpsH.

Phylogenomic databases

eggNOG

COG0096.

GeneTree

EBGT00050000011452.

HOGENOM

HBG735443.

OMA

QRVSKPG.

PhylomeDB

P0A7W7.

ProtClustDB

PRK00136.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10907-MONOMER.

Gene expression databases

Genevestigator

P0A7W7.

Family and domain databases

HAMAP

MF_01302_B. Ribosomal_S8_B.
[Tree]

InterPro

IPR000630. Ribosomal_S8.
[Graphical view]

K02994.

PANTHER

PTHR11758. Ribosomal_S8. 1 hit.

Pfam

PF00410. Ribosomal_S8. 1 hit.
[Graphical view]

SUPFAM

SSF56047. Ribosomal_S8. 1 hit.

PROSITE

PS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RS8_ECOLI

Accession

Primary (citable) accession number: P0A7W7
Secondary accession number(s): P02361, Q2M6X1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents