Reviewed, UniProtKB/Swiss-Prot P02358 (RS6_ECOLI)

Names and origin

Protein names

Recommended name:
    30S ribosomal protein S6
Cleaved into the following 2 chains:
    1- Recommended name:
            30S ribosomal protein S6, fully modified isoform
    2- Recommended name:
            30S ribosomal protein S6, non-modified isoform

Gene names

Name:	rpsF
Ordered Locus Names:	b4200, JW4158

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	135 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	Binds together with S18 to 16S ribosomal RNA. HAMAP MF_00360
Subunit structure	Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (Ref.14). HAMAP MF_00360
Post-translational modification	5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the rimK enzyme. HAMAP MF_00360
Sequence similarities	Belongs to the ribosomal protein S6P family.
Mass spectrometry	Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. Ref.10

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
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 – 135

135

30S ribosomal protein S6, fully modified isoform HAMAP MF_00360

PRO_0000030640

Chain

1 – 131

131

30S ribosomal protein S6, non-modified isoform HAMAP MF_00360

PRO_0000030641

Amino acid modifications

Modified residue

93

1

N6-acetyllysine Ref.11

Experimental info

Sequence conflict

14

1

Q → T AA sequence Ref.6

Sequence conflict

20

1

G → A AA sequence Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

135

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Helix

12 – 17

6

Helix

18 – 31

14

Beta strand

41 – 46

6

Beta strand

53 – 60

8

Helix

68 – 79

12

Beta strand

84 – 91

8

Sequences

	Sequence		Length	Mass (Da)
	P02358-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: F4CC629711C1FD0E	FASTA	135	15,703
	10 20 30 40 50 60 MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP INKLHKAHYV 70 80 90 100 110 120 LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS PMVKAKDERR ERRDDFANET 130 ADDAEAGDSE EEEEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Determination of the complete amino-acid sequence of protein S6 from the wild-type and a mutant of Escherichia coli." Hitz H., Schaefer D., Wittmann-Liebold B. Eur. J. Biochem. 75:497-512(1977) [PubMed: 328274] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame." Schnier J., Kitakawa M., Isono K. Mol. Gen. Genet. 204:126-132(1986) [PubMed: 3528756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
[3]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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] OF 1-131. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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] OF 1-131. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Small genes/gene-products in Escherichia coli K-12." Wasinger V.C., Humphery-Smith I. FEMS Microbiol. Lett. 169:375-382(1998) [PubMed: 9868784] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: K12.
[7]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-11. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[9]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"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.
[11]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, MASS SPECTROMETRY.
[12]	"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.
[13]	"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.
[14]	"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

EMBLGenBankDDBJ

X04022 Genomic DNA. Translation: CAA27652.1.
U14003 Genomic DNA. Translation: AAA97096.1.
U00096 Genomic DNA. Translation: AAC77157.2.
AP009048 Genomic DNA. Translation: BAE78201.1.

PIR

R3EC6. C65231.

RefSeq

AP_004700.1.
NP_418621.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	F	1-100	[»]
1P6G	electron microscopy	12.30	F	1-135	[»]
1P87	electron microscopy	11.50	F	1-135	[»]
1VS5	X-ray	3.46	F	1-135	[»]
1VS7	X-ray	3.46	F	1-135	[»]
2AVY	X-ray	3.46	F	1-135	[»]
2AW7	X-ray	3.46	F	1-135	[»]
2GY9	electron microscopy	2.00	F	1-95	[»]
2GYB	electron microscopy	2.00	F	1-95	[»]
2I2P	X-ray	3.22	F	1-135	[»]
2I2U	X-ray	3.22	F	1-135	[»]
2QAL	X-ray	3.21	F	1-135	[»]
2QAN	X-ray	3.21	F	1-135	[»]
2QB9	X-ray	3.54	F	1-135	[»]
2QBB	X-ray	3.54	F	1-135	[»]
2QBD	X-ray	3.30	F	1-135	[»]
2QBF	X-ray	3.30	F	1-135	[»]
2QBH	X-ray	4.00	F	1-135	[»]
2QBJ	X-ray	4.00	F	1-135	[»]
2QOU	X-ray	3.93	F	1-135	[»]
2QOW	X-ray	3.93	F	1-135	[»]
2QOY	X-ray	3.50	F	1-135	[»]
2QP0	X-ray	3.50	F	1-135	[»]
2VHO	X-ray	3.74	F	1-135	[»]
2VHP	X-ray	3.74	F	1-135	[»]
2Z4K	X-ray	4.45	F	1-135	[»]
2Z4M	X-ray	4.45	F	1-135	[»]
3DF1	X-ray	3.50	F	1-135	[»]
3DF3	X-ray	3.50	F	1-135	[»]
3FIH	electron microscopy	-	F	1-100	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10782N.

2-D gel databases

SWISS-2DPAGE

P02358.

ECO2DBASE

C014.8. 6TH EDITION.
C015.3. 6TH EDITION.
D014.7. 6TH EDITION.

Genome annotation databases

GeneID

948723.

GenomeReviews

Gene locus JW4158 in contig AP009048_GR.
Gene locus b4200 in contig U00096_GR.

KEGG

ecj:JW4158.
eco:b4200.

Organism-specific databases

EchoBASE

EB0898.

EcoGene

EG10905. rpsF.

CMR

Search...

Phylogenomic databases

HOGENOM

P02358.

OMA

P02358. MSFYESV.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10905-MON.

Family and domain databases

HAMAP

MF_00360.
[Tree]

InterPro

IPR000529. Ribosomal_S6.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]

Gene3D

G3DSA:3.30.70.60. Transl_elong_EF1B/rib_con. 1 hit.

Pfam

PF01250. Ribosomal_S6. 1 hit.
[Graphical view]

ProDom

PD003809. Ribosomal_S6. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00166. S6. 1 hit.

PROSITE

PS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RS6_ECOLI

Accession

Primary (citable) accession number: P02358
Secondary accession number(s): Q2M6A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 109 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)