P0A7R9 (RS11_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S11

Gene names

Name:	rpsK
Ordered Locus Names:	b3297, JW3259

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	129 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	Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome By similarity. HAMAP-Rule MF_01310
Subunit structure	Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18 By similarity. Cross-links to IF-3. Ref.10
Miscellaneous	Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies (Ref.10); exactly how IF-3 interacts with the 30S subunit is controversial. HAMAP-Rule MF_01310
Sequence similarities	Belongs to the ribosomal protein S11P family.
Mass spectrometry	Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. Ref.9

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4897206. Source: EcoliWiki
Molecular_function	SSU rRNA binding Inferred from direct assay PubMed 2505863PubMed 7585249. Source: EcoliWiki structural constituent of ribosome Inferred from direct assay PubMed 4897206. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 129

128

30S ribosomal protein S11 HAMAP-Rule MF_01310

PRO_0000123144

Amino acid modifications

Modified residue

2

1

N-methylalanine HAMAP-Rule MF_01310

Secondary structure

1

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129

Helix Strand Turn

Details...

Beta strand

18 – 25

8

Beta strand

27 – 29

3

Beta strand

30 – 35

6

Turn

37 – 39

3

Beta strand

42 – 46

5

Helix

48 – 50

3

Helix

54 – 57

4

Helix

60 – 74

15

Helix

75 – 77

3

Beta strand

81 – 87

7

Beta strand

89 – 92

4

Helix

95 – 102

8

Beta strand

106 – 112

7

Sequences

	Sequence		Length	Mass (Da)
	P0A7R9 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0C759DDA60E89C0C	FASTA	129	13,845
	10 20 30 40 50 60 MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS GFRGSRKSTP 70 80 90 100 110 120 FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL NAAGFRITNI TDVTPIPHNG CRPPKKRRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli." Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L. Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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.
[3]	"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.
[4]	"Primary structure of protein S11 from Escherichia coli ribosomes." Kamp R., Wittmann-Liebold B. FEBS Lett. 121:117-122(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-129. Strain: K.
[5]	"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 IF-3. Strain: B.
[6]	"IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: identification of 30 S proteins crosslinked to IF-3 -- utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide." Cooperman B.S., Expert-Bezancon A., Kahan L., Dondon J., Grunberg-Manago M. Arch. Biochem. Biophys. 208:554-562(1981) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO IF-3.
[7]	"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 IF-3. Strain: MRE-600.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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

X02543 Genomic DNA. Translation: CAA26393.1.
U18997 Genomic DNA. Translation: AAA58095.1.
U00096 Genomic DNA. Translation: AAC76322.1.
AP009048 Genomic DNA. Translation: BAE77994.1.

PIR

R3EC11. B23807.

RefSeq

NP_417756.1. NC_000913.2.
YP_492135.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	K	13-129	[»]
1P6G	electron microscopy	12.30	K	2-129	[»]
1P87	electron microscopy	11.50	K	2-129	[»]
1VS5	X-ray	3.46	K	1-129	[»]
1VS7	X-ray	3.46	K	1-129	[»]
2AVY	X-ray	3.46	K	2-129	[»]
2AW7	X-ray	3.46	K	2-129	[»]
2GY9	electron microscopy	15.00	K	13-127	[»]
2GYB	electron microscopy	15.00	K	13-127	[»]
2I2P	X-ray	3.22	K	2-128	[»]
2I2U	X-ray	3.22	K	2-128	[»]
2QAL	X-ray	3.21	K	2-129	[»]
2QAN	X-ray	3.21	K	2-129	[»]
2QB9	X-ray	3.54	K	2-129	[»]
2QBB	X-ray	3.54	K	2-129	[»]
2QBD	X-ray	3.30	K	2-129	[»]
2QBF	X-ray	3.30	K	2-129	[»]
2QBH	X-ray	4.00	K	2-129	[»]
2QBJ	X-ray	4.00	K	2-129	[»]
2QOU	X-ray	3.93	K	2-129	[»]
2QOW	X-ray	3.93	K	2-129	[»]
2QOY	X-ray	3.50	K	2-129	[»]
2QP0	X-ray	3.50	K	2-129	[»]
2VHO	X-ray	3.74	K	2-129	[»]
2VHP	X-ray	3.74	K	2-129	[»]
2WWL	electron microscopy	5.80	K	13-129	[»]
2YKR	electron microscopy	9.80	K	13-129	[»]
2Z4K	X-ray	4.45	K	2-129	[»]
2Z4M	X-ray	4.45	K	2-129	[»]
3DF1	X-ray	3.50	K	2-128	[»]
3DF3	X-ray	3.50	K	2-128	[»]
3E1A	electron microscopy	-	C	1-129	[»]
3E1C	electron microscopy	-	C	1-129	[»]
3FIH	electron microscopy	6.70	K	13-129	[»]
3I1M	X-ray	3.19	K	1-129	[»]
3I1O	X-ray	3.19	K	1-129	[»]
3I1Q	X-ray	3.81	K	1-129	[»]
3I1S	X-ray	3.81	K	1-129	[»]
3I1Z	X-ray	3.71	K	1-129	[»]
3I21	X-ray	3.71	K	1-129	[»]
3IZV	electron microscopy	-	O	1-129	[»]
3IZW	electron microscopy	-	O	1-129	[»]
3J00	electron microscopy	-	K	2-129	[»]
3J0U	electron microscopy	12.10	N	2-129	[»]
3J0V	electron microscopy	14.70	N	2-129	[»]
3J0X	electron microscopy	13.50	N	2-129	[»]
3J0Z	electron microscopy	11.50	N	2-129	[»]
3J10	electron microscopy	11.50	N	2-129	[»]
3J13	electron microscopy	13.10	M	2-129	[»]
3J18	electron microscopy	8.30	K	13-129	[»]
3KC4	electron microscopy	-	K	1-129	[»]
3OAQ	X-ray	3.25	K	13-129	[»]
3OAR	X-ray	3.25	K	13-129	[»]
3OFA	X-ray	3.19	K	13-129	[»]
3OFB	X-ray	3.19	K	13-129	[»]
3OFO	X-ray	3.10	K	13-129	[»]
3OFP	X-ray	3.10	K	13-129	[»]
3OFX	X-ray	3.29	K	13-129	[»]
3OFY	X-ray	3.29	K	13-129	[»]
3OR9	X-ray	3.30	K	1-129	[»]
3ORA	X-ray	3.30	K	1-129	[»]
3SFS	X-ray	3.20	K	1-129	[»]
3UOQ	X-ray	3.70	K	1-129	[»]
4A2I	electron microscopy	16.50	K	13-129	[»]
4ADV	electron microscopy	13.50	K	2-129	[»]
4GAQ	X-ray	3.30	K	1-129	[»]
4GAS	X-ray	3.30	K	1-129	[»]
4GD1	X-ray	3.00	K	13-129	[»]
4GD2	X-ray	3.00	K	13-129	[»]

ProteinModelPortal

P0A7R9.

SMR

P0A7R9. Positions 2-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47838N.

IntAct

P0A7R9. 13 interactions.

MINT

MINT-1232137.

STRING

511145.b3297.

Proteomic databases

PaxDb

P0A7R9.

PRIDE

P0A7R9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76322; AAC76322; b3297.
BAE77994; BAE77994; BAE77994.

GeneID

12934439.
947792.

KEGG

ecj:Y75_p3879.
eco:b3297.

PATRIC

32122026. VBIEscCol129921_3390.

Organism-specific databases

EchoBASE

EB0903.

EcoGene

EG10910. rpsK.

Phylogenomic databases

eggNOG

COG0100.

HOGENOM

HOG000111598.

KO

K02948.

OMA

PHNGCRR.

ProtClustDB

PRK05309.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10910-MONOMER.
ECOL316407:JW3259-MONOMER.

Gene expression databases

Genevestigator

P0A7R9.

Family and domain databases

Gene3D

3.30.420.80. 1 hit.

HAMAP

MF_01310. Ribosomal_S11.

InterPro

IPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]

PANTHER

PTHR11759. PTHR11759. 1 hit.

Pfam

PF00411. Ribosomal_S11. 1 hit.
[Graphical view]

PIRSF

PIRSF002131. Ribosomal_S11. 1 hit.

TIGRFAMs

TIGR03632. bact_S11. 1 hit.

PROSITE

PS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7R9.

Entry information

Entry name

RS11_ECOLI

Accession

Primary (citable) accession number: P0A7R9
Secondary accession number(s): P02366, Q2M6W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program