P81288 (RS4_GEOSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 30S ribosomal protein S4 Alternative name(s): BS5 | ||
| Gene names |
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| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) | ||
| Taxonomic identifier | 1422 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus![]() |
Protein attributes
| Sequence length | 200 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 where it nucleates assembly of the body of the 30S subunit By similarity. HAMAP-Rule MF_01306_B With S5 and S12 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_01306_B |
| Subunit structure | Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity By similarity. |
| Sequence similarities | Belongs to the ribosomal protein S4P family. Contains 1 S4 RNA-binding domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Ligand | RNA-binding rRNA-binding |
| Molecular function | Ribonucleoprotein Ribosomal protein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW translationInferred from electronic annotation. Source: HAMAP |
| Cellular_component | small ribosomal subunit Inferred from electronic annotation. Source: InterPro |
| Molecular_function | rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosomeInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 Ref.3 | ||||||||||||||||||||||||||||||||||||
| Chain | 2 – 200 | 199 | 30S ribosomal protein S4 HAMAP-Rule MF_01306_B | PRO_0000132338 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| Domain | 92 – 152 | 61 | S4 RNA-binding | ||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 41 | 1 | Missing AA sequence Ref.2 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 59 | 14 | |||||||||||||||||||||||||||||||||||||
| Turn | 60 – 62 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 65 – 75 | 11 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 80 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 82 – 92 | 11 | |||||||||||||||||||||||||||||||||||||
| Helix | 94 – 100 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 106 | 4 | |||||||||||||||||||||||||||||||||||||
| Helix | 107 – 115 | 9 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 121 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 138 – 141 | 4 | |||||||||||||||||||||||||||||||||||||
| Helix | 143 – 145 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 149 – 156 | 8 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 163 – 168 | 6 | |||||||||||||||||||||||||||||||||||||
| Turn | 169 – 172 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 173 – 176 | 4 | |||||||||||||||||||||||||||||||||||||
| Turn | 182 – 184 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 192 – 199 | 8 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif." Davies C., Gerstner R.B., Draper D.E., Ramakrishnan V., White S.W. EMBO J. 17:4545-4558(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-200. |
| [2] | "Primary structures of ribosomal proteins from the archaebacterium Halobacterium marismortui and the eubacterium Bacillus stearothermophilus." Arndt E., Scholzen T., Kromer W., Hatakeyama T., Kimura M. Biochimie 73:657-668(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-200. |
| [3] | "Procaryotic ribosomal proteins: N-terminal sequence homologies and structural correspondence of 30 S ribosomal proteins from Escherichia coli and Bacillus stearothermophilus." Yaguchi M., Matheson A.T., Visentin L.P. FEBS Lett. 46:296-300(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Strain: DSM 13240 / CIP 106956 / 10. |
| [4] | "Isolation and characterization of Bacillus stearothermophilus 30S and 50S ribosomal protein mutations." Schnier J., Gewitz H.S., Behrens S.E., Lee A., Ginther C., Leighton T. J. Bacteriol. 172:7306-7309(1990) [PubMed] [Europe PMC] [Abstract] Cited for: ISOLATION OF STREPTOMYCIN INDEPENDENT STRAINS. Strain: 799. |
| [5] | "Recognition of 16S rRNA by ribosomal protein S4 from Bacillus stearothermophilus." Gerstner R.B., Pak Y., Draper D.E. Biochemistry 40:7165-7173(2001) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO RRNA. |
| [6] | "Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases." Markus M.A., Gerstner R.B., Draper D.E., Torchia D.A. J. Mol. Biol. 292:375-387(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 42-199. |
| [7] | "Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy." Sayers E.W., Gerstner R.B., Draper D.E., Torchia D.A. Biochemistry 39:13602-13613(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR. |
Cross-references
3D structure databases | |||||||||||||||||||
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| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P81288. | ||||||||||||||||||
| SMR | P81288. Positions 43-200. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 1.10.1050.10. 1 hit. 3.10.290.10. 1 hit. | ||||||||||||||||||
| HAMAP | MF_01306_B. Ribosomal_S4_B. | ||||||||||||||||||
| InterPro | IPR022801. Ribosomal_S4/S9. IPR001912. Ribosomal_S4/S9_N. IPR005709. Ribosomal_S4_bac-type. IPR018079. Ribosomal_S4_CS. IPR002942. S4_RNA-bd. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11831. PTHR11831. 1 hit. | ||||||||||||||||||
| Pfam | PF00163. Ribosomal_S4. 1 hit. PF01479. S4. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00363. S4. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR01017. rpsD_bact. 1 hit. | ||||||||||||||||||
| PROSITE | PS00632. RIBOSOMAL_S4. 1 hit. PS50889. S4. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P81288. | ||||||||||||||||||
Entry information
| Entry name | RS4_GEOSE | ||||||||
| Accession | Primary (citable) accession number: P81288 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Ribosomal proteins Ribosomal proteins families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
