P02359 (RS7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S7

Gene names

Name:	rpsG
Ordered Locus Names:	b3341, JW3303

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	179 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 head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA. Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA. Ref.11 Protein S7 is also a translational repressor protein; it regulates the expression of the str operon members to different degrees by binding to its mRNA. Ref.11
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S9 and S11 By similarity. Cross-links to IF3 and the P and E site tRNAs. Ref.11 Ref.18
Miscellaneous	The strain K12 sequence is shown. HAMAP-Rule MF_00480_B Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies (Ref.18); exactly how IF-3 interacts with the 30S subunit is controversial. HAMAP-Rule MF_00480_B
Sequence similarities	Belongs to the ribosomal protein S7P family.
Mass spectrometry	Molecular mass is 19888.7 Da from positions 2 - 179. Determined by MALDI. Ref.17

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of translation Inferred from direct assay PubMed 7016341. Source: EcoCyc ribosomal small subunit assembly Inferred from direct assay Ref.11. Source: EcoCyc translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 16858726. Source: EcoCyc membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	mRNA binding Inferred from direct assay PubMed 17027976PubMed 8289236. Source: EcoCyc rRNA binding Inferred from direct assay PubMed 6338481. Source: EcoCyc structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
infC	P0A707	3	EBI-543074,EBI-546262
tig	P0A850	3	EBI-543074,EBI-544862

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 179

178

30S ribosomal protein S7 HAMAP-Rule MF_00480_B

PRO_0000124259

Natural variations

Natural variant

157 – 179

23

Missing in strain: B and L44.

Experimental info

Mutagenesis

2 – 18

17

Missing: Defective in ribosome assembly; accumulates to abnormally high levels on polysomes; significantly decreases affinity for its own mRNA. Ref.15 Ref.16

Mutagenesis

36

1

K → A or E: Defective in ribosome assembly. Ref.15 Ref.16

Mutagenesis

116

1

M → G: Significantly decreases affinity for its own mRNA. Ref.15 Ref.16

Sequence conflict

92

1

Missing AA sequence Ref.3

Secondary structure

1

.

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179

Helix Strand Turn

Details...

Turn

16 – 18

3

Helix

21 – 30

10

Helix

32 – 34

3

Helix

36 – 51

16

Turn

52 – 54

3

Helix

59 – 69

11

Beta strand

72 – 75

4

Beta strand

78 – 80

3

Beta strand

81 – 83

3

Beta strand

88 – 90

3

Helix

93 – 109

17

Beta strand

113 – 115

3

Helix

116 – 128

13

Helix

134 – 147

14

Helix

148 – 150

3

Sequences

	Sequence		Length	Mass (Da)
	P02359 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8627DB380C4A9C0D	FASTA	179	20,019
	10 20 30 40 50 60 MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE 70 80 90 100 110 120 AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL 130 140 150 160 170 ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"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.
[3]	"The primary structure of ribosomal protein S7 from E. coli strains K and B." Reinbolt J., Tritsch D., Wittmann-Liebold B. Biochimie 61:501-522(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-179. Strain: B and K.
[4]	"DNA sequences from the str operon of Escherichia coli." Post L.E., Nomura M. J. Biol. Chem. 255:4660-4666(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 148-179. Strain: K12.
[5]	"Mutant sequences in the rpsL gene of Escherichia coli B/r: mechanistic implications for spontaneous and ultraviolet light mutagenesis." Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A. Mol. Gen. Genet. 232:89-96(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81. Strain: B/R.
[6]	"Comparison of the complete sequence of the str operon in Salmonella typhimurium and Escherichia coli." Johanson U., Hughes D. Gene 120:93-98(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173. Strain: K12 / MG1655 / ATCC 47076.
[7]	Weigel C.T.O. Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-156. Strain: L44.
[8]	"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 111-131, CROSS-LINKING TO RRNA. Strain: MRE-600.
[9]	"Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits." MacKeen L.A., Kahan L., Wahba A.J., Schwartz I. J. Biol. Chem. 255:10526-10531(1980) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO IF3. Strain: B.
[10]	"Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane." Boileau G., Butler P., Hershey J.W.B., Traut R.R. Biochemistry 22:3162-3170(1983) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO IF3. Strain: MRE-600.
[11]	"Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7." Nowotny V., Nierhaus K.H. Biochemistry 27:7051-7055(1988) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN SUBUNIT ASSEMBLY. Strain: K12 / D10.
[12]	"Post-transcriptional regulation of the str operon in Escherichia coli. Ribosomal protein S7 inhibits coupled translation of S7 but not its independent translation." Saito K., Mattheakis L.C., Nomura M. J. Mol. Biol. 235:111-124(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MECHANISM OF TRANSLATION REGULATION. Strain: K12.
[13]	"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site." Osswald M., Doering T., Brimacombe R. Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD. Strain: MRE-600.
[14]	"The cross-link from the upstream region of mRNA to ribosomal protein S7 is located in the C-terminal peptide: experimental verification of a prediction from modeling studies." Greuer B., Thiede B., Brimacombe R. RNA 5:1521-1525(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO MRNA. Strain: B and K.
[15]	"Tagging ribosomal protein S7 allows rapid identification of mutants defective in assembly and function of 30S subunits." Fredrick K., Dunny G.M., Noller H.F. J. Mol. Biol. 298:379-394(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CONSERVED SURFACE RESIDUES. Strain: K.
[16]	"Ribosomal protein S7 from Escherichia coli uses the same determinants to bind 16S ribosomal RNA and its messenger RNA." Robert F., Brakier-Gingras L. Nucleic Acids Res. 29:677-682(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CONSERVED RESIDUES. Strain: K12.
[17]	"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.
[18]	"Interaction of translation initiation factor 3 with the 30S ribosomal subunit." Dallas A., Noller H.F. Mol. Cell 8:855-864(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MODELING OF IF-3/30S SUBUNIT INTERACTION.
[19]	"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.
[20]	"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.
[21]	"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

U18997 Genomic DNA. Translation: AAA58138.1.
U00096 Genomic DNA. Translation: AAC76366.1.
AP009048 Genomic DNA. Translation: BAE77950.1.
V00355 Genomic DNA. Translation: CAA23649.1.
J01689 Genomic DNA. Translation: AAA50990.1.
X64592 Genomic DNA. Translation: CAA45881.1.
X65735 Genomic DNA. Translation: CAA46644.1.
J01688 Genomic DNA. Translation: AAA50989.1.

PIR

R3EC7K. H65127.

RefSeq

NP_417800.1. NC_000913.2.
YP_492091.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EG0	electron microscopy	11.50	D	1-146	[»]
1M5G	model	-	G	3-156	[»]
1ML5	electron microscopy	14.00	J	1-156	[»]
1P6G	electron microscopy	12.30	G	2-179	[»]
1P87	electron microscopy	11.50	G	2-179	[»]
1VS5	X-ray	3.46	G	1-179	[»]
1VS7	X-ray	3.46	G	1-179	[»]
2AVY	X-ray	3.46	G	2-179	[»]
2AW7	X-ray	3.46	G	2-179	[»]
2GY9	electron microscopy	15.00	G	20-155	[»]
2GYB	electron microscopy	15.00	G	20-155	[»]
2I2P	X-ray	3.22	G	2-178	[»]
2I2U	X-ray	3.22	G	2-178	[»]
2QAL	X-ray	3.21	G	2-179	[»]
2QAN	X-ray	3.21	G	2-179	[»]
2QB9	X-ray	3.54	G	2-179	[»]
2QBB	X-ray	3.54	G	2-179	[»]
2QBD	X-ray	3.30	G	2-179	[»]
2QBF	X-ray	3.30	G	2-179	[»]
2QBH	X-ray	4.00	G	2-179	[»]
2QBJ	X-ray	4.00	G	2-179	[»]
2QOU	X-ray	3.93	G	2-179	[»]
2QOW	X-ray	3.93	G	2-179	[»]
2QOY	X-ray	3.50	G	2-179	[»]
2QP0	X-ray	3.50	G	2-179	[»]
2VHO	X-ray	3.74	G	2-179	[»]
2VHP	X-ray	3.74	G	2-179	[»]
2WWL	electron microscopy	5.80	G	3-152	[»]
2YKR	electron microscopy	9.80	G	2-152	[»]
2Z4K	X-ray	4.45	G	2-179	[»]
2Z4M	X-ray	4.45	G	2-179	[»]
3DF1	X-ray	3.50	G	2-178	[»]
3DF3	X-ray	3.50	G	2-178	[»]
3E1A	electron microscopy	-	U	1-179	[»]
3E1C	electron microscopy	-	U	1-179	[»]
3FIH	electron microscopy	6.70	G	3-152	[»]
3I1M	X-ray	3.19	G	1-179	[»]
3I1O	X-ray	3.19	G	1-179	[»]
3I1Q	X-ray	3.81	G	1-179	[»]
3I1S	X-ray	3.81	G	1-179	[»]
3I1Z	X-ray	3.71	G	1-179	[»]
3I21	X-ray	3.71	G	1-179	[»]
3IZV	electron microscopy	-	K	1-179	[»]
3IZW	electron microscopy	-	K	1-179	[»]
3J00	electron microscopy	-	G	2-179	[»]
3J0U	electron microscopy	12.10	J	2-179	[»]
3J0V	electron microscopy	14.70	J	2-179	[»]
3J0X	electron microscopy	13.50	J	2-179	[»]
3J0Z	electron microscopy	11.50	J	2-179	[»]
3J10	electron microscopy	11.50	J	2-179	[»]
3J13	electron microscopy	13.10	I	2-179	[»]
3J18	electron microscopy	8.30	G	2-152	[»]
3KC4	electron microscopy	-	G	1-179	[»]
3OAQ	X-ray	3.25	G	2-152	[»]
3OAR	X-ray	3.25	G	3-152	[»]
3OFA	X-ray	3.19	G	2-152	[»]
3OFB	X-ray	3.19	G	3-152	[»]
3OFO	X-ray	3.10	G	2-152	[»]
3OFP	X-ray	3.10	G	3-152	[»]
3OFX	X-ray	3.29	G	2-152	[»]
3OFY	X-ray	3.29	G	3-152	[»]
3OR9	X-ray	3.30	G	1-179	[»]
3ORA	X-ray	3.30	G	1-179	[»]
3SFS	X-ray	3.20	G	1-156	[»]
3UOQ	X-ray	3.70	G	1-179	[»]
4A2I	electron microscopy	16.50	G	3-152	[»]
4ADV	electron microscopy	13.50	G	2-179	[»]
4GAQ	X-ray	3.30	G	1-179	[»]
4GAS	X-ray	3.30	G	1-179	[»]
4GD1	X-ray	3.00	G	2-152	[»]
4GD2	X-ray	3.00	G	2-152	[»]

ProteinModelPortal

P02359.

SMR

P02359. Positions 2-179.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10783N.

IntAct

P02359. 150 interactions.

MINT

MINT-1236482.

STRING

511145.b3341.

PTM databases

PhosSite

P0810434.

Proteomic databases

PaxDb

P02359.

PRIDE

P02359.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76366; AAC76366; b3341.
BAE77950; BAE77950; BAE77950.

GeneID

12933477.
947846.

KEGG

ecj:Y75_p3835.
eco:b3341.

PATRIC

32122114. VBIEscCol129921_3434.

Organism-specific databases

EchoBASE

EB0899.

EcoGene

EG10906. rpsG.

Phylogenomic databases

eggNOG

COG0049.

HOGENOM

HOG000039067.

KO

K02992.

OMA

RREKTMT.

ProtClustDB

PRK05302.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10906-MONOMER.
ECOL316407:JW3303-MONOMER.

Gene expression databases

Genevestigator

P02359.

Family and domain databases

Gene3D

1.10.455.10. 1 hit.

HAMAP

MF_00480_B. Ribosomal_S7_B.

InterPro

IPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]

PANTHER

PTHR11205. PTHR11205. 1 hit.
PTHR11205:SF13. PTHR11205:SF13. 1 hit.

Pfam

PF00177. Ribosomal_S7. 1 hit.
[Graphical view]

PIRSF

PIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.

SUPFAM

SSF47973. Ribosomal_S7. 1 hit.

TIGRFAMs

TIGR01029. rpsG_bact. 1 hit.

PROSITE

PS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02359.

Entry information

Entry name

RS7_ECOLI

Accession

Primary (citable) accession number: P02359
Secondary accession number(s): Q2M706

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program