P80372 (RS3_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S3

Gene names

Name:	rpsC
Synonyms:	rps3
Ordered Locus Names:	TTHA1686

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	239 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. HAMAP-Rule MF_01309_B
Subunit structure	Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13
Sequence similarities	Belongs to the ribosomal protein S3P family. Contains 1 KH type-2 domain.
Mass spectrometry	Molecular mass is 26570 Da from positions 2 - 239. Determined by MALDI. Ref.3

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	small ribosomal subunit Inferred from electronic annotation. Source: InterPro
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.2

Chain

2 – 239

238

30S ribosomal protein S3 HAMAP-Rule MF_01309_B

PRO_0000130223

Regions

Domain

39 – 107

69

KH type-2

Secondary structure

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239

Helix Strand Turn

Details...

Turn

7 – 13

7

Beta strand

14 – 16

3

Beta strand

19 – 21

3

Turn

26 – 28

3

Helix

29 – 44

16

Turn

45 – 50

6

Beta strand

52 – 55

4

Beta strand

56 – 58

3

Beta strand

59 – 62

4

Beta strand

64 – 66

3

Beta strand

67 – 71

5

Helix

73 – 75

3

Beta strand

79 – 82

4

Helix

83 – 94

12

Beta strand

97 – 99

3

Beta strand

102 – 105

4

Helix

109 – 111

3

Helix

113 – 125

13

Helix

130 – 143

14

Beta strand

147 – 153

7

Turn

157 – 159

3

Beta strand

166 – 168

3

Beta strand

169 – 171

3

Beta strand

175 – 177

3

Helix

178 – 180

3

Beta strand

182 – 187

6

Beta strand

189 – 191

3

Beta strand

192 – 194

3

Beta strand

195 – 197

3

Beta strand

198 – 203

6

Sequences

	Sequence		Length	Mass (Da)
	P80372 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AD585A1D53AC7F04	FASTA	239	26,701
	10 20 30 40 50 60 MGNKIHPIGF RLGITRDWES RWYAGKKQYR HLLLEDQRIR GLLEKELYSA GLARVDIERA 70 80 90 100 110 120 ADNVAVTVHV AKPGVVIGRG GERIRVLREE LAKLTGKNVA LNVQEVQNPN LSAPLVAQRV 130 140 150 160 170 180 AEQIERRFAV RRAIKQAVQR VMESGAKGAK VIVSGRIGGA EQARTEWAAQ GRVPLHTLRA 190 200 210 220 230 NIDYGFALAR TTYGVLGVKA YIFLGEVIGG QKPKARPELP KAEERPRRRR PAVRVKKEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Purification and characterization of the 30S ribosomal proteins from the bacterium Thermus thermophilus." Tsiboli P., Herfurth E., Choli T. Eur. J. Biochem. 226:169-177(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-37.
[3]	"Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry." Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A. Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[4]	"Structure of the 30S ribosomal subunit." Wimberly B.T., Brodersen D.E., Clemons W.M. Jr., Morgan-Warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V. Nature 407:327-339(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
[5]	"Structure of functionally activated small ribosomal subunit at 3.3 A resolution." Schluenzen F., Tocilj A., Zarivach R., Harms J., Gluehmann M., Janell D., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A. Cell 102:615-623(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[6]	"The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit." Brodersen D.E., Clemons W.M. Jr., Carter A.P., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. Cell 103:1143-1154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[7]	"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics." Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. Nature 407:340-348(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 30S SUBUNIT.
[8]	"The path of messenger RNA through the ribosome." Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F. Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
[9]	"Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3." Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H., Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A., Franceschi F. EMBO J. 20:1829-1839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[10]	"Crystal structure of an initiation factor bound to the 30S ribosomal subunit." Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Hartsch T., Wimberly B.T., Ramakrishnan V. Science 291:498-501(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[11]	"Crystal structure of the ribosome at 5.5 A resolution." Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F. Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
[12]	"Recognition of cognate transfer RNA by the 30S ribosomal subunit." Ogle J.M., Brodersen D.E., Clemons W.M. Jr., Tarry M.J., Carter A.P., Ramakrishnan V. Science 292:897-902(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF THE 30S SUBUNIT.
[13]	"Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA." Brodersen D.E., Clemons W.M. Jr., Carter A.P., Wimberly B.T., Ramakrishnan V. J. Mol. Biol. 316:725-768(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
+	Additional computationally mapped references.

Web resources

T.thermophilus ribosome structure and function

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD71509.1.

RefSeq

YP_144952.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	C	1-239	[»]
1GIX	X-ray	5.50	F	1-239	[»]
1HNW	X-ray	3.40	C	1-239	[»]
1HNX	X-ray	3.40	C	1-239	[»]
1HNZ	X-ray	3.30	C	1-239	[»]
1HR0	X-ray	3.20	C	1-239	[»]
1I94	X-ray	3.20	C	2-239	[»]
1I95	X-ray	4.50	C	2-239	[»]
1I96	X-ray	4.20	C	2-239	[»]
1I97	X-ray	4.50	C	2-239	[»]
1IBK	X-ray	3.31	C	1-239	[»]
1IBL	X-ray	3.11	C	1-239	[»]
1IBM	X-ray	3.31	C	1-239	[»]
1J5E	X-ray	3.05	C	1-239	[»]
1L1U	model	-	C	1-207	[»]
1N32	X-ray	3.00	C	1-239	[»]
1N33	X-ray	3.35	C	1-239	[»]
1N34	X-ray	3.80	C	1-239	[»]
1N36	X-ray	3.65	C	1-239	[»]
1XMO	X-ray	3.25	C	1-239	[»]
1XMQ	X-ray	3.00	C	1-239	[»]
1XNQ	X-ray	3.05	C	1-239	[»]
1XNR	X-ray	3.10	C	1-239	[»]
1YL4	X-ray	5.50	F	1-239	[»]
2B64	X-ray	5.90	C	1-239	[»]
2B9M	X-ray	6.76	C	1-239	[»]
2B9O	X-ray	6.46	C	1-239	[»]
2E5L	X-ray	3.30	C	2-239	[»]
2F4V	X-ray	3.80	C	1-239	[»]
2HGI	X-ray	5.00	F	1-239	[»]
2HGP	X-ray	5.50	F	1-239	[»]
2HGR	X-ray	4.51	F	1-239	[»]
2HHH	X-ray	3.35	C	1-239	[»]
2J00	X-ray	2.80	C	2-238	[»]
2J02	X-ray	2.80	C	2-238	[»]
2UU9	X-ray	3.10	C	2-238	[»]
2UUA	X-ray	2.90	C	1-239	[»]
2UUB	X-ray	2.90	C	2-238	[»]
2UUC	X-ray	3.10	C	2-238	[»]
2UXB	X-ray	3.10	C	1-239	[»]
2UXC	X-ray	2.90	C	1-239	[»]
2UXD	X-ray	3.20	C	1-239	[»]
2V46	X-ray	3.80	C	2-238	[»]
2V48	X-ray	3.50	C	1-239	[»]
2VQE	X-ray	2.50	C	1-239	[»]
2VQF	X-ray	2.90	C	1-239	[»]
2WDG	X-ray	3.30	C	1-239	[»]
2WDH	X-ray	3.30	C	1-239	[»]
2WDK	X-ray	3.50	C	1-239	[»]
2WDM	X-ray	3.50	C	1-239	[»]
2WH1	X-ray	3.45	C	1-239	[»]
2WH3	X-ray	3.45	C	1-239	[»]
2WRI	X-ray	3.60	C	1-239	[»]
2WRK	X-ray	3.60	C	1-239	[»]
2WRN	X-ray	3.60	C	1-239	[»]
2WRQ	X-ray	3.60	C	1-239	[»]
2X9R	X-ray	3.10	C	1-239	[»]
2X9T	X-ray	3.10	C	1-239	[»]
2XFZ	X-ray	3.20	C	1-239	[»]
2XG1	X-ray	3.20	C	1-239	[»]
2XQD	X-ray	3.10	C	1-239	[»]
2XSY	electron microscopy	7.80	C	1-239	[»]
2XUY	electron microscopy	7.60	C	1-239	[»]
2Y0U	X-ray	3.10	C	1-239	[»]
2Y0W	X-ray	3.10	C	1-239	[»]
2Y0Y	X-ray	3.10	C	1-239	[»]
2Y10	X-ray	3.10	C	1-239	[»]
2Y12	X-ray	3.10	C	1-239	[»]
2Y14	X-ray	3.10	C	1-239	[»]
2Y16	X-ray	3.10	C	1-239	[»]
2Y18	X-ray	3.10	C	1-239	[»]
2ZM6	X-ray	3.30	C	2-239	[»]
3FIC	electron microscopy	6.40	C	2-208	[»]
3HUW	X-ray	3.10	C	1-239	[»]
3HUY	X-ray	3.10	C	1-239	[»]
3I8G	X-ray	3.10	F	1-239	[»]
3I8H	X-ray	3.10	F	1-239	[»]
3I9B	X-ray	3.50	F	1-239	[»]
3I9D	X-ray	3.50	F	1-239	[»]
3KIQ	X-ray	3.30	c	1-239	[»]
3KIS	X-ray	3.30	c	1-239	[»]
3KIU	X-ray	3.60	c	1-239	[»]
3KIX	X-ray	3.60	c	1-239	[»]
3KNH	X-ray	3.00	C	1-239	[»]
3KNJ	X-ray	3.15	C	1-239	[»]
3KNL	X-ray	3.45	C	1-239	[»]
3KNN	X-ray	3.45	C	1-239	[»]
3OGE	X-ray	3.00	C	1-239	[»]
3OGY	X-ray	3.00	C	1-239	[»]
3OHC	X-ray	3.00	C	1-239	[»]
3OHD	X-ray	3.00	C	1-239	[»]
3OHY	X-ray	3.00	C	1-239	[»]
3OI0	X-ray	3.00	C	1-239	[»]
3OI2	X-ray	3.10	C	1-239	[»]
3OI4	X-ray	3.10	C	1-239	[»]
3OTO	X-ray	3.69	C	1-239	[»]
3T1H	X-ray	3.11	C	1-239	[»]
3T1Y	X-ray	2.80	C	1-239	[»]
3TVF	X-ray	3.10	F	1-239	[»]
3TVG	X-ray	3.10	F	1-239	[»]
3UXS	X-ray	3.20	C	1-239	[»]
3UXT	X-ray	3.20	C	1-239	[»]
3UYD	X-ray	3.00	F	1-239	[»]
3UYF	X-ray	3.00	F	1-239	[»]
3UZ3	X-ray	3.30	F	1-239	[»]
3UZ4	X-ray	3.30	F	1-239	[»]
3UZ6	X-ray	3.00	F	1-239	[»]
3UZ7	X-ray	3.00	F	1-239	[»]
3UZG	X-ray	3.30	F	1-239	[»]
3UZI	X-ray	3.30	F	1-239	[»]
3UZL	X-ray	3.30	F	1-239	[»]
3UZM	X-ray	3.30	F	1-239	[»]
3V22	X-ray	3.00	C	1-239	[»]
3V24	X-ray	3.00	C	1-239	[»]
3V26	X-ray	3.10	C	1-239	[»]
3V28	X-ray	3.10	C	1-239	[»]
3V2C	X-ray	2.70	C	1-239	[»]
3V2E	X-ray	2.70	C	1-239	[»]
3ZVO	X-ray	3.80	C	1-239	[»]
4ABR	X-ray	3.10	C	1-239	[»]
4AQY	X-ray	3.50	C	1-239	[»]
4DH9	X-ray	3.20	C	1-239	[»]
4DHB	X-ray	3.20	C	1-239	[»]
4DR1	X-ray	3.60	C	1-239	[»]
4DR2	X-ray	3.25	C	1-239	[»]
4DR3	X-ray	3.35	C	1-239	[»]
4DR4	X-ray	3.97	C	1-239	[»]
4DR5	X-ray	3.45	C	1-239	[»]
4DR6	X-ray	3.30	C	1-239	[»]
4DR7	X-ray	3.75	C	1-239	[»]
4DUY	X-ray	3.39	C	1-239	[»]
4DUZ	X-ray	3.65	C	1-239	[»]
4DV0	X-ray	3.85	C	1-239	[»]
4DV1	X-ray	3.85	C	1-239	[»]
4DV2	X-ray	3.65	C	1-239	[»]
4DV3	X-ray	3.55	C	1-239	[»]
4DV4	X-ray	3.65	C	1-239	[»]
4DV5	X-ray	3.68	C	1-239	[»]
4DV6	X-ray	3.30	C	1-239	[»]
4DV7	X-ray	3.29	C	1-239	[»]
4G5K	X-ray	3.30	F	1-239	[»]
4G5M	X-ray	3.30	F	1-239	[»]
4G5T	X-ray	3.10	F	1-239	[»]
4G5V	X-ray	3.10	F	1-239	[»]

ProteinModelPortal

P80372.

SMR

P80372. Positions 2-207.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1686.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71509; BAD71509; BAD71509.

GeneID

3168725.

KEGG

ttj:TTHA1686.

PATRIC

23958327. VBITheThe93045_1656.

Phylogenomic databases

eggNOG

COG0092.

HOGENOM

HOG000210610.

KO

K02982.

OMA

MGQKTNP.

ProtClustDB

PRK00310.

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

P80372.

Entry information

Entry name

RS3_THET8

Accession

Primary (citable) accession number: P80372
Secondary accession number(s): Q5SHP4, Q9ACK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program