30S ribosomal protein S5 - Geobacillus stearothermophilus

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P02357 (RS5_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. History...

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

Documents (3) |

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 S5
Short name=BS5

Alternative name(s):
BS6

Gene names

Name:

rpsE

Organism

Geobacillus stearothermophilus (Bacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	With S4 and S12 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_01307_B Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body By similarity. HAMAP-Rule MF_01307_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S4 and S8 By similarity.
Domain	The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity. HAMAP-Rule MF_01307_B
Sequence similarities	Belongs to the ribosomal protein S5P family. Contains 1 S5 DRBM 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 translation Inferred 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 ribosome Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 166

166

30S ribosomal protein S5 HAMAP-Rule MF_01307_B

PRO_0000131469

Regions

Domain

11 – 74

S5 DRBM

Secondary structure

166

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02357 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 774E82A2ED1D8EC5
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FASTA

166

17,628

        10         20         30         40         50         60 
MRRINPNKLE LEERVVAVNR VAKVVKGGRR LRFSALVVVG DKNGHVGFGT GKAQEVPEAI 

        70         80         90        100        110        120 
RKAIEDAKKN LIEVPIVGTT IPHEVIGHFG AGEIILKPAS EGTGVIAGGP ARAVLELAGI 

       130        140        150        160 
SDILSKSIGS NTPINMVRAT FDGLKQLKRA EDVAKLRGKT VEELLG

« Hide

References

[1]	"Proteins of the Bacillus stearothermophilus ribosome. The amino acid sequences of proteins S5 and L30." Kimura M. J. Biol. Chem. 259:1051-1055(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]	"Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus." Ramakrishnan V., Gerchman S.E. J. Biol. Chem. 266:880-885(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 1-15. 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]	"The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA." Ramakrishnan V., White S.W. Nature 358:768-771(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[6]	"Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance." Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W. J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57621 Genomic DNA. Translation: AAA22699.1.

PIR

R3BS5F. A02708.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DV4	X-ray	4.50	E	4-148	[»]
1PKP	X-ray	2.80	A	1-150	[»]

ProteinModelPortal

P02357.

SMR

P02357. Positions 4-148.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-112114.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.160.20. 1 hit.
3.30.230.10. 1 hit.

HAMAP

MF_01307_B. Ribosomal_S5_B.

InterPro

IPR014720. dsRNA-bd-like_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]

PANTHER

PTHR13718. PTHR13718. 1 hit.

Pfam

PF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR01021. rpsE_bact. 1 hit.

PROSITE

PS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02357.

Entry information

Entry name

RS5_GEOSE

Accession

Primary (citable) accession number: P02357

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 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

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

Regions

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents