Reviewed, UniProtKB/Swiss-Prot P02357 (RS5_BACST)

Names and origin

Protein names

Recommended name:
    30S ribosomal protein S5
      Short name=BS5
Alternative name(s):
    BS6

Gene names

Name:

rpsE

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	With S4 and S12 plays an important role in translational accuracy By similarity. Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body By similarity.
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.
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: InterPro
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

PRO_0000131469

Regions

Domain

11 – 74

64

S5 DRBM

Secondary structure

1

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166

Helix Strand Turn

Details...

Helix

6 – 8

3

Beta strand

12 – 19

8

Beta strand

21 – 24

4

Beta strand

33 – 40

8

Beta strand

42 – 55

14

Helix

56 – 67

12

Beta strand

85 – 89

5

Beta strand

92 – 98

7

Beta strand

105 – 107

3

Helix

109 – 118

10

Beta strand

122 – 127

6

Helix

133 – 146

14

Sequences

	Sequence		Length	Mass (Da)
	P02357-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 774E82A2ED1D8EC5	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

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: 6363400] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 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: 1985969] [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: 4607606] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: 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: 2254291] [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: 1508272] [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: 9642068] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M57621 Genomic DNA. Translation: AAA22699.1.

PIR

R3BS5F. A02708.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DV4	X-ray	4.50	E	4-148	[»]
1EG0	electron microscopy	11.50	B	1-148	[»]
1PKP	X-ray	2.80	A	1-150	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_01307.
[Tree]

InterPro

IPR014720. dsRNA-bd-like.
IPR002197. HTH_Fis.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR014721. Ribosomal_S5_D2-type_fold.
IPR013810. Ribosomal_S5_N.
[Graphical view]

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

PANTHER

PTHR13718. Ribosomal_S5. 1 hit.

Pfam

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

PRINTS

PR01590. HTHFIS.

TIGRFAMs

TIGR01021. rpsE_bact. 1 hit.

PROSITE

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

ProtoNet

Search...

Other Resources

LinkHub

P02357.

Entry information

Entry name

RS5_BACST

Accession

Primary (citable) accession number: P02357

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 25, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)