P0A7V3 (RS3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S3

Gene names

Name:	rpsC
Ordered Locus Names:	b3314, JW3276

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	233 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 the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation By similarity. Ref.7 Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. Ref.7
Subunit structure	Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14 By similarity. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.
Sequence similarities	Belongs to the ribosomal protein S3P family. Contains 1 KH type-2 domain.
Mass spectrometry	Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. Ref.8

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
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	mRNA binding Inferred from electronic annotation. Source: HAMAP 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

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 233

232

30S ribosomal protein S3 HAMAP-Rule MF_01309_B

PRO_0000130113

Regions

Domain

39 – 107

69

KH type-2

Experimental info

Mutagenesis

131 – 135

5

RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

233

Helix Strand Turn

Details...

Helix

9 – 11

3

Beta strand

14 – 16

3

Beta strand

19 – 21

3

Helix

26 – 46

21

Turn

48 – 51

4

Beta strand

52 – 56

5

Beta strand

61 – 64

4

Beta strand

67 – 71

5

Helix

73 – 77

5

Beta strand

79 – 81

3

Helix

82 – 95

14

Beta strand

102 – 105

4

Helix

109 – 111

3

Helix

113 – 126

14

Helix

130 – 142

13

Beta strand

143 – 145

3

Beta strand

147 – 152

6

Beta strand

155 – 157

3

Beta strand

164 – 166

3

Beta strand

169 – 171

3

Beta strand

175 – 177

3

Beta strand

178 – 180

3

Beta strand

182 – 191

10

Beta strand

194 – 203

10

Sequences

	Sequence		Length	Mass (Da)
	P0A7V3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6D0131A285B7AAB3	FASTA	233	25,983
	10 20 30 40 50 60 MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA SVSRIVIERP 70 80 90 100 110 120 AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ INIAEVRKPE LDAKLVADSI 130 140 150 160 170 180 TSQLERRVMF RRAMKRAVQN AMRLGAKGIK VEVSGRLGGA EIARTEWYRE GRVPLHTLRA 190 200 210 220 230 DIDYNTSEAH TTYGVIGVKV WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]	"The primary structure of protein S3 from the small ribosomal subunit of Escherichia coli." Brauer D., Roming R. FEBS Lett. 106:352-357(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-233. Strain: K.
[5]	"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 39-49 AND 87-108, CROSS-LINKING TO RRNA. Strain: MRE-600.
[6]	"Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit." Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R. Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
[7]	"mRNA helicase activity of the ribosome." Takyar S., Hickerson R.P., Noller H.F. Cell 120:49-58(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS. Strain: MRE-600.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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

X02613 Genomic DNA. Translation: CAA26466.1.
U18997 Genomic DNA. Translation: AAA58111.1.
U00096 Genomic DNA. Translation: AAC76339.1.
AP009048 Genomic DNA. Translation: BAE77977.1.

PIR

R3EC3. H23129.

RefSeq

NP_417773.1. NC_000913.2.
YP_492118.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	C	2-207	[»]
1P6G	electron microscopy	12.30	C	2-233	[»]
1P87	electron microscopy	11.50	C	2-233	[»]
1VS5	X-ray	3.46	C	1-233	[»]
1VS7	X-ray	3.46	C	1-233	[»]
2AVY	X-ray	3.46	C	2-233	[»]
2AW7	X-ray	3.46	C	2-233	[»]
2GY9	electron microscopy	15.00	C	2-206	[»]
2GYB	electron microscopy	15.00	C	2-206	[»]
2I2P	X-ray	3.22	C	2-232	[»]
2I2U	X-ray	3.22	C	2-232	[»]
2QAL	X-ray	3.21	C	2-233	[»]
2QAN	X-ray	3.21	C	2-233	[»]
2QB9	X-ray	3.54	C	2-233	[»]
2QBB	X-ray	3.54	C	2-233	[»]
2QBD	X-ray	3.30	C	2-233	[»]
2QBF	X-ray	3.30	C	2-233	[»]
2QBH	X-ray	4.00	C	2-233	[»]
2QBJ	X-ray	4.00	C	2-233	[»]
2QOU	X-ray	3.93	C	2-233	[»]
2QOW	X-ray	3.93	C	2-233	[»]
2QOY	X-ray	3.50	C	2-233	[»]
2QP0	X-ray	3.50	C	2-233	[»]
2VHO	X-ray	3.74	C	2-233	[»]
2VHP	X-ray	3.74	C	2-233	[»]
2WWL	electron microscopy	5.80	C	2-207	[»]
2YKR	electron microscopy	9.80	C	2-207	[»]
2Z4K	X-ray	4.45	C	2-233	[»]
2Z4M	X-ray	4.45	C	2-233	[»]
3DF1	X-ray	3.50	C	2-232	[»]
3DF3	X-ray	3.50	C	2-232	[»]
3E1A	electron microscopy	-	O	1-233	[»]
3E1C	electron microscopy	-	O	1-233	[»]
3FIH	electron microscopy	6.70	C	2-207	[»]
3I1M	X-ray	3.19	C	1-233	[»]
3I1O	X-ray	3.19	C	1-233	[»]
3I1Q	X-ray	3.81	C	1-233	[»]
3I1S	X-ray	3.81	C	1-233	[»]
3I1Z	X-ray	3.71	C	1-233	[»]
3I21	X-ray	3.71	C	1-233	[»]
3IZV	electron microscopy	-	G	1-233	[»]
3IZW	electron microscopy	-	G	1-233	[»]
3J00	electron microscopy	-	C	2-233	[»]
3J0U	electron microscopy	12.10	F	2-233	[»]
3J0V	electron microscopy	14.70	F	2-233	[»]
3J0X	electron microscopy	13.50	F	2-233	[»]
3J0Z	electron microscopy	11.50	F	2-233	[»]
3J10	electron microscopy	11.50	F	2-233	[»]
3J13	electron microscopy	13.10	E	2-233	[»]
3J18	electron microscopy	8.30	C	2-207	[»]
3KC4	electron microscopy	-	C	1-233	[»]
3OAQ	X-ray	3.25	C	2-207	[»]
3OAR	X-ray	3.25	C	2-207	[»]
3OFA	X-ray	3.19	C	2-207	[»]
3OFB	X-ray	3.19	C	2-207	[»]
3OFO	X-ray	3.10	C	2-207	[»]
3OFP	X-ray	3.10	C	2-207	[»]
3OFX	X-ray	3.29	C	2-207	[»]
3OFY	X-ray	3.29	C	2-207	[»]
3OR9	X-ray	3.30	C	1-233	[»]
3ORA	X-ray	3.30	C	1-233	[»]
3SFS	X-ray	3.20	C	1-233	[»]
3UOQ	X-ray	3.70	C	1-233	[»]
4A2I	electron microscopy	16.50	C	2-207	[»]
4ADV	electron microscopy	13.50	C	2-233	[»]
4GAQ	X-ray	3.30	C	1-233	[»]
4GAS	X-ray	3.30	C	1-233	[»]
4GD1	X-ray	3.00	C	2-207	[»]
4GD2	X-ray	3.00	C	2-207	[»]

ProteinModelPortal

P0A7V3.

SMR

P0A7V3. Positions 2-233.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35807N.

IntAct

P0A7V3. 184 interactions.

STRING

511145.b3314.

Proteomic databases

PaxDb

P0A7V3.

PRIDE

P0A7V3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76339; AAC76339; b3314.
BAE77977; BAE77977; BAE77977.

GeneID

12932292.
947814.

KEGG

ecj:Y75_p3862.
eco:b3314.

PATRIC

32122060. VBIEscCol129921_3407.

Organism-specific databases

EchoBASE

EB0895.

EcoGene

EG10902. rpsC.

Phylogenomic databases

eggNOG

COG0092.

HOGENOM

HOG000210610.

KO

K02982.

OMA

MGQKTNP.

ProtClustDB

PRK00310.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Gene expression databases

Genevestigator

P0A7V3.

Family and domain databases

Gene3D

3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.

HAMAP

MF_01309_B. Ribosomal_S3_B.

InterPro

IPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view]

Pfam

PF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]

SMART

SM00322. KH. 1 hit.
[Graphical view]

SUPFAM

SSF54814. KH_prok. 1 hit.
SSF54821. Ribosomal_S3_C. 1 hit.

TIGRFAMs

TIGR01009. rpsC_bact. 1 hit.

PROSITE

PS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7V3.

Entry information

Entry name

RS3_ECOLI

Accession

Primary (citable) accession number: P0A7V3
Secondary accession number(s): P02352, Q2M6X9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program