P80371 (RS2_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S2

Gene names

Name:	rpsB
Synonyms:	rps2
Ordered Locus Names:	TTHA0861

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	256 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	Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit. HAMAP-Rule MF_00291_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts protein S8 and may contact the N-terminus of Era. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13
Sequence similarities	Belongs to the ribosomal protein S2P family.

Ontologies

Keywords
Domain	Coiled coil
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	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 256

255

30S ribosomal protein S2 HAMAP-Rule MF_00291_B

PRO_0000134264

Regions

Coiled coil

104 – 149

46

HAMAP-Rule MF_00291_B

Experimental info

Sequence conflict

19

1

H → N AA sequence Ref.2

Secondary structure

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256

Helix Strand Turn

Details...

Turn

4 – 6

3

Helix

10 – 13

4

Beta strand

15 – 18

4

Beta strand

20 – 23

4

Helix

26 – 28

3

Turn

29 – 31

3

Beta strand

32 – 36

5

Beta strand

39 – 42

4

Helix

44 – 62

19

Turn

63 – 65

3

Beta strand

68 – 71

4

Beta strand

74 – 77

4

Turn

78 – 86

9

Beta strand

87 – 89

3

Beta strand

92 – 95

4

Turn

99 – 104

6

Helix

105 – 121

17

Beta strand

123 – 126

4

Helix

127 – 129

3

Helix

132 – 135

4

Helix

138 – 148

11

Beta strand

149 – 151

3

Helix

152 – 154

3

Beta strand

156 – 158

3

Beta strand

160 – 165

6

Turn

167 – 170

4

Helix

171 – 179

9

Beta strand

184 – 188

5

Beta strand

190 – 192

3

Helix

194 – 196

3

Beta strand

198 – 200

3

Beta strand

205 – 207

3

Helix

208 – 223

16

Turn

224 – 226

3

Turn

234 – 239

6

Sequences

	Sequence		Length	Mass (Da)
	P80371 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 65D7958336911CE5	FASTA	256	29,277
	10 20 30 40 50 60 MPVEITVKEL LEAGVHFGHE RKRWNPKFAR YIYAERNGIH IIDLQKTMEE LERTFRFIED 70 80 90 100 110 120 LAMRGGTILF VGTKKQAQDI VRMEAERAGM PYVNQRWLGG MLTNFKTISQ RVHRLEELEA 130 140 150 160 170 180 LFASPEIEER PKKEQVRLKH ELERLQKYLS GFRLLKRLPD AIFVVDPTKE AIAVREARKL 190 200 210 220 230 240 FIPVIALADT DSDPDLVDYI IPGNDDAIRS IQLILSRAVD LIIQARGGVV EPSPSYALVQ 250 EAEATETPEG ESEVEA

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 2-26.
[3]	"Elongation factor Ts from Thermus thermophilus -- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu." Blank J., Nock S., Kreutzer R., Sprinzl M. Eur. J. Biochem. 236:222-227(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-256.
[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.
[14]	"Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly." Sharma M.R., Barat C., Wilson D.N., Booth T.M., Kawazoe M., Hori-Takemoto C., Shirouzu M., Yokoyama S., Fucini P., Agrawal R.K. Mol. Cell 18:319-329(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (13.50 ANGSTROMS), POSSIBLE INTERACTION WITH ERA.
+	Additional computationally mapped references.

Web resources

T.thermophilus ribosome structure and function

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD70684.1.
X83598 Genomic DNA. Translation: CAA58577.1.

PIR

S51053.

RefSeq

YP_144127.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	B	1-256	[»]
1GIX	X-ray	5.50	E	1-256	[»]
1HNW	X-ray	3.40	B	1-256	[»]
1HNX	X-ray	3.40	B	1-256	[»]
1HNZ	X-ray	3.30	B	1-256	[»]
1HR0	X-ray	3.20	B	1-256	[»]
1I94	X-ray	3.20	B	2-256	[»]
1I95	X-ray	4.50	B	2-256	[»]
1I96	X-ray	4.20	B	2-256	[»]
1I97	X-ray	4.50	B	2-256	[»]
1IBK	X-ray	3.31	B	1-256	[»]
1IBL	X-ray	3.11	B	1-256	[»]
1IBM	X-ray	3.31	B	1-256	[»]
1J5E	X-ray	3.05	B	1-256	[»]
1JGO	X-ray	5.60	E	1-256	[»]
1JGP	X-ray	7.00	E	1-256	[»]
1JGQ	X-ray	5.00	E	1-256	[»]
1L1U	model	-	B	7-240	[»]
1N32	X-ray	3.00	B	1-256	[»]
1N33	X-ray	3.35	B	1-256	[»]
1N34	X-ray	3.80	B	1-256	[»]
1N36	X-ray	3.65	B	1-256	[»]
1X18	electron microscopy	13.50	E	7-240	[»]
1XMO	X-ray	3.25	B	1-256	[»]
1XMQ	X-ray	3.00	B	1-256	[»]
1XNQ	X-ray	3.05	B	1-256	[»]
1XNR	X-ray	3.10	B	1-256	[»]
1YL4	X-ray	5.50	E	1-256	[»]
2B64	X-ray	5.90	B	1-256	[»]
2B9M	X-ray	6.76	B	1-256	[»]
2B9O	X-ray	6.46	B	1-256	[»]
2E5L	X-ray	3.30	B	2-228	[»]
2F4V	X-ray	3.80	B	1-256	[»]
2HGI	X-ray	5.00	E	1-256	[»]
2HGP	X-ray	5.50	E	1-256	[»]
2HGR	X-ray	4.51	E	1-256	[»]
2HHH	X-ray	3.35	B	1-256	[»]
2J00	X-ray	2.80	B	2-255	[»]
2J02	X-ray	2.80	B	2-255	[»]
2OM7	electron microscopy	7.30	N	1-256	[»]
2UU9	X-ray	3.10	B	2-255	[»]
2UUA	X-ray	2.90	B	1-256	[»]
2UUB	X-ray	2.90	B	2-255	[»]
2UUC	X-ray	3.10	B	2-255	[»]
2UXB	X-ray	3.10	B	1-256	[»]
2UXC	X-ray	2.90	B	1-256	[»]
2UXD	X-ray	3.20	B	1-256	[»]
2V46	X-ray	3.80	B	2-255	[»]
2V48	X-ray	3.50	B	1-256	[»]
2VQE	X-ray	2.50	B	1-256	[»]
2VQF	X-ray	2.90	B	1-256	[»]
2WDG	X-ray	3.30	B	1-256	[»]
2WDH	X-ray	3.30	B	1-256	[»]
2WDK	X-ray	3.50	B	1-256	[»]
2WDM	X-ray	3.50	B	1-256	[»]
2WH1	X-ray	3.45	B	1-256	[»]
2WH3	X-ray	3.45	B	1-256	[»]
2WRI	X-ray	3.60	B	1-256	[»]
2WRK	X-ray	3.60	B	1-256	[»]
2WRN	X-ray	3.60	B	1-256	[»]
2WRQ	X-ray	3.60	B	1-256	[»]
2X9R	X-ray	3.10	B	1-256	[»]
2X9T	X-ray	3.10	B	1-256	[»]
2XFZ	X-ray	3.20	B	1-256	[»]
2XG1	X-ray	3.20	B	1-256	[»]
2XQD	X-ray	3.10	B	1-256	[»]
2XSY	electron microscopy	7.80	B	1-256	[»]
2XUY	electron microscopy	7.60	B	1-256	[»]
2Y0U	X-ray	3.10	B	1-256	[»]
2Y0W	X-ray	3.10	B	1-256	[»]
2Y0Y	X-ray	3.10	B	1-256	[»]
2Y10	X-ray	3.10	B	1-256	[»]
2Y12	X-ray	3.10	B	1-256	[»]
2Y14	X-ray	3.10	B	1-256	[»]
2Y16	X-ray	3.10	B	1-256	[»]
2Y18	X-ray	3.10	B	1-256	[»]
2ZM6	X-ray	3.30	B	2-256	[»]
3FIC	electron microscopy	6.40	B	7-241	[»]
3HUW	X-ray	3.10	B	1-256	[»]
3HUY	X-ray	3.10	B	1-256	[»]
3I8G	X-ray	3.10	E	1-256	[»]
3I8H	X-ray	3.10	E	1-256	[»]
3I9B	X-ray	3.50	E	1-256	[»]
3I9D	X-ray	3.50	E	1-256	[»]
3KIQ	X-ray	3.30	b	1-256	[»]
3KIS	X-ray	3.30	b	1-256	[»]
3KIU	X-ray	3.60	b	1-256	[»]
3KIX	X-ray	3.60	b	1-256	[»]
3KNH	X-ray	3.00	B	1-256	[»]
3KNJ	X-ray	3.15	B	1-256	[»]
3KNL	X-ray	3.45	B	1-256	[»]
3KNN	X-ray	3.45	B	1-256	[»]
3OGE	X-ray	3.00	B	1-256	[»]
3OGY	X-ray	3.00	B	1-256	[»]
3OHC	X-ray	3.00	B	1-256	[»]
3OHD	X-ray	3.00	B	1-256	[»]
3OHY	X-ray	3.00	B	1-256	[»]
3OI0	X-ray	3.00	B	1-256	[»]
3OI2	X-ray	3.10	B	1-256	[»]
3OI4	X-ray	3.10	B	1-256	[»]
3OTO	X-ray	3.69	B	1-256	[»]
3T1H	X-ray	3.11	B	1-256	[»]
3T1Y	X-ray	2.80	B	1-256	[»]
3TVF	X-ray	3.10	E	1-256	[»]
3TVG	X-ray	3.10	E	1-256	[»]
3UXS	X-ray	3.20	B	1-256	[»]
3UXT	X-ray	3.20	B	1-256	[»]
3UYD	X-ray	3.00	E	1-256	[»]
3UYF	X-ray	3.00	E	1-256	[»]
3UZ3	X-ray	3.30	E	1-256	[»]
3UZ4	X-ray	3.30	E	1-256	[»]
3UZ6	X-ray	3.00	E	1-256	[»]
3UZ7	X-ray	3.00	E	1-256	[»]
3UZG	X-ray	3.30	E	1-256	[»]
3UZI	X-ray	3.30	E	1-256	[»]
3UZL	X-ray	3.30	E	1-256	[»]
3UZM	X-ray	3.30	E	1-256	[»]
3V22	X-ray	3.00	B	1-256	[»]
3V24	X-ray	3.00	B	1-256	[»]
3V26	X-ray	3.10	B	1-256	[»]
3V28	X-ray	3.10	B	1-256	[»]
3V2C	X-ray	2.70	B	1-256	[»]
3V2E	X-ray	2.70	B	1-256	[»]
3ZVO	X-ray	3.80	B	1-256	[»]
4ABR	X-ray	3.10	B	1-256	[»]
4AQY	X-ray	3.50	B	1-256	[»]
4DH9	X-ray	3.20	B	1-256	[»]
4DHB	X-ray	3.20	B	1-256	[»]
4DR1	X-ray	3.60	B	1-256	[»]
4DR2	X-ray	3.25	B	1-256	[»]
4DR3	X-ray	3.35	B	1-256	[»]
4DR4	X-ray	3.97	B	1-256	[»]
4DR5	X-ray	3.45	B	1-256	[»]
4DR6	X-ray	3.30	B	1-256	[»]
4DR7	X-ray	3.75	B	1-256	[»]
4DUY	X-ray	3.39	B	1-256	[»]
4DUZ	X-ray	3.65	B	1-256	[»]
4DV0	X-ray	3.85	B	1-256	[»]
4DV1	X-ray	3.85	B	1-256	[»]
4DV2	X-ray	3.65	B	1-256	[»]
4DV3	X-ray	3.55	B	1-256	[»]
4DV4	X-ray	3.65	B	1-256	[»]
4DV5	X-ray	3.68	B	1-256	[»]
4DV6	X-ray	3.30	B	1-256	[»]
4DV7	X-ray	3.29	B	1-256	[»]
4G5K	X-ray	3.30	E	1-256	[»]
4G5M	X-ray	3.30	E	1-256	[»]
4G5T	X-ray	3.10	E	1-256	[»]
4G5V	X-ray	3.10	E	1-256	[»]

ProteinModelPortal

P80371.

SMR

P80371. Positions 2-250.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA0861.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD70684; BAD70684; BAD70684.

GeneID

3170121.

KEGG

ttj:TTHA0861.

PATRIC

23956704. VBITheThe93045_0855.

Phylogenomic databases

eggNOG

COG0052.

HOGENOM

HOG000071892.

KO

K02967.

OMA

NVAGGTD.

ProtClustDB

PRK05299.

Family and domain databases

HAMAP

MF_00291_B. Ribosomal_S2_B.

InterPro

IPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]

PANTHER

PTHR12534. PTHR12534. 1 hit.

Pfam

PF00318. Ribosomal_S2. 1 hit.
[Graphical view]

PRINTS

PR00395. RIBOSOMALS2.

SUPFAM

SSF52313. Ribosomal_S2. 1 hit.

TIGRFAMs

TIGR01011. rpsB_bact. 1 hit.

PROSITE

PS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80371.

Entry information

Entry name

RS2_THET8

Accession

Primary (citable) accession number: P80371
Secondary accession number(s): Q5SJZ1, Q9ACK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 123 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program