P02358 (RS6_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S6

Cleaved into the following 2 chains:

1. 30S ribosomal protein S6, fully modified isoform
2. 30S ribosomal protein S6, non-modified isoform

Gene names

Name:	rpsF
Ordered Locus Names:	b4200, JW4158

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	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-Rule MF_00360
Subunit structure	Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (Ref.15).
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-Rule 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.11
Sequence caution	The sequence AAA97096.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally. The sequence AAC77157.5 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally. The sequence BAE78201.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally. The sequence CAA27652.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4587209. Source: EcoliWiki
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-Rule MF_00360

PRO_0000030640

Chain

1 – 131

131

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

PRO_0000030641

Amino acid modifications

Modified residue

93

1

N6-acetyllysine Ref.12

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

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135

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Beta strand

6 – 10

5

Helix

12 – 14

3

Helix

17 – 30

14

Turn

31 – 33

3

Beta strand

35 – 37

3

Beta strand

40 – 45

6

Beta strand

53 – 55

3

Beta strand

57 – 61

5

Beta strand

64 – 66

3

Turn

68 – 71

4

Helix

72 – 80

9

Beta strand

84 – 86

3

Beta strand

88 – 90

3

Sequences

	Sequence		Length	Mass (Da)
	P02358 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[11]	"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.
[12]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]	"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.
[14]	"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.
[15]	"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

X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.

PIR

R3EC6. C65231.

RefSeq

NP_418621.5. NC_000913.2.
YP_492342.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EG0	electron microscopy	11.50	C	1-97	[»]
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	15.00	F	1-95	[»]
2GYB	electron microscopy	15.00	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	[»]
2WWL	electron microscopy	5.80	F	1-100	[»]
2YKR	electron microscopy	9.80	F	1-100	[»]
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	[»]
3E1A	electron microscopy	-	T	1-135	[»]
3E1C	electron microscopy	-	T	1-135	[»]
3FIH	electron microscopy	6.70	F	1-100	[»]
3I1M	X-ray	3.19	F	1-135	[»]
3I1O	X-ray	3.19	F	1-135	[»]
3I1Q	X-ray	3.81	F	1-135	[»]
3I1S	X-ray	3.81	F	1-135	[»]
3I1Z	X-ray	3.71	F	1-135	[»]
3I21	X-ray	3.71	F	1-135	[»]
3IZV	electron microscopy	-	J	1-135	[»]
3IZW	electron microscopy	-	J	1-135	[»]
3J00	electron microscopy	-	F	1-135	[»]
3J0U	electron microscopy	12.10	I	1-135	[»]
3J0V	electron microscopy	14.70	I	1-135	[»]
3J0X	electron microscopy	13.50	I	1-135	[»]
3J0Z	electron microscopy	11.50	I	1-135	[»]
3J10	electron microscopy	11.50	I	1-135	[»]
3J13	electron microscopy	13.10	H	1-135	[»]
3J18	electron microscopy	8.30	F	1-100	[»]
3KC4	electron microscopy	-	F	1-135	[»]
3OAQ	X-ray	3.25	F	1-100	[»]
3OAR	X-ray	3.25	F	1-100	[»]
3OFA	X-ray	3.19	F	1-100	[»]
3OFB	X-ray	3.19	F	1-100	[»]
3OFO	X-ray	3.10	F	1-100	[»]
3OFP	X-ray	3.10	F	1-100	[»]
3OFX	X-ray	3.29	F	1-100	[»]
3OFY	X-ray	3.29	F	1-100	[»]
3OR9	X-ray	3.30	F	1-135	[»]
3ORA	X-ray	3.30	F	1-135	[»]
3SFS	X-ray	3.20	F	1-131	[»]
3UOQ	X-ray	3.70	F	1-135	[»]
4A2I	electron microscopy	16.50	F	1-100	[»]
4ADV	electron microscopy	13.50	F	1-135	[»]
4GAQ	X-ray	3.30	F	1-135	[»]
4GAS	X-ray	3.30	F	1-135	[»]
4GD1	X-ray	3.00	F	1-100	[»]
4GD2	X-ray	3.00	F	1-100	[»]

ProteinModelPortal

P02358.

SMR

P02358. Positions 1-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10782N.

IntAct

P02358. 56 interactions.

MINT

MINT-1279331.

STRING

511145.b4200.

2D gel databases

SWISS-2DPAGE

P02358.

Proteomic databases

PaxDb

P02358.

PRIDE

P02358.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.

GeneID

12930647.
948723.

KEGG

ecj:Y75_p4086.
eco:b4200.

PATRIC

48667972. VBIEscCol107702_4239.

Organism-specific databases

EchoBASE

EB0898.

EcoGene

EG10905. rpsF.

Phylogenomic databases

eggNOG

COG0360.

HOGENOM

HOG000040438.

KO

K02990.

OMA

ITEASPM.

ProtClustDB

PRK00453.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Gene expression databases

Genevestigator

P02358.

Family and domain databases

Gene3D

3.30.70.60. 1 hit.

HAMAP

MF_00360. Ribosomal_S6.

InterPro

IPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]

Pfam

PF01250. Ribosomal_S6. 1 hit.
[Graphical view]

SUPFAM

SSF54995. Ribosomal_S6. 1 hit.

TIGRFAMs

TIGR00166. S6. 1 hit.

PROSITE

PS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02358.

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:	May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program