Reviewed, UniProtKB/Swiss-Prot P80371 (RS2_THET8)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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 MF_00291
Subunit structure	Part of the 30S ribosomal subunit. Contacts protein S8. 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.
Caution	The sequence shown here has been extracted from PDB entry 1FJG.

Ontologies

Keywords
Domain	Coiled coil
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing
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 MF_00291

PRO_0000134264

Regions

Coiled coil

104 – 149

46

HAMAP MF_00291

Experimental info

Sequence conflict

19

1

H → N AA sequence Ref.2

Secondary structure

1

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256

Helix Strand Turn

Details...

Turn

13 – 15

3

Helix

26 – 31

6

Helix

44 – 64

21

Beta strand

68 – 71

4

Helix

75 – 77

3

Helix

78 – 87

10

Turn

99 – 104

6

Helix

105 – 121

17

Turn

125 – 128

4

Helix

132 – 148

17

Turn

150 – 153

4

Beta strand

160 – 165

6

Turn

167 – 170

4

Helix

171 – 179

9

Beta strand

184 – 188

5

Helix

194 – 196

3

Beta strand

198 – 203

6

Helix

208 – 223

16

Turn

224 – 227

4

Helix

236 – 242

7

Sequences

	Sequence		Length	Mass (Da)
	P80371-1 [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].
[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: 7957245] [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: 8617268] [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: 11014182] [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: 11007480] [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: 11163189] [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: 11014183] [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: 11511350] [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: 11296217] [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: 11228145] [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: 11283358] [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: 11340196] [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: 11866529] [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

EMBLGenBankDDBJ

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

PIR

S51053.

RefSeq

YP_144127.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	B	1-256	[»]
1GIX	X-ray	5.50	E	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	[»]
1PNS	X-ray	8.70	B	7-240	[»]
1PNX	X-ray	9.50	B	7-240	[»]
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	[»]
2OW8	X-ray	3.71	c	-	[»]
2UU9	X-ray	3.10	B	2-255	[»]
2UUA	X-ray	2.90	B	2-255	[»]
2UUB	X-ray	2.90	B	2-255	[»]
2UUC	X-ray	3.10	B	2-255	[»]
2UXB	X-ray	3.10	B	2-255	[»]
2UXC	X-ray	2.90	B	2-255	[»]
2UXD	X-ray	3.20	B	2-255	[»]
2V46	X-ray	3.80	B	2-255	[»]
2V48	X-ray	3.80	B	2-255	[»]
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	[»]
2ZM6	X-ray	3.30	B	2-256	[»]
3FIC	electron microscopy	6.40	B	7-241	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P80371.

Genome annotation databases

GeneID

3170121.

GenomeReviews

Gene locus TTHA0861 in contig AP008226_GR.

KEGG

ttj:TTHA0861.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P80371.

OMA

LTNFQTV.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0861-MON.

Family and domain databases

HAMAP

MF_00291.
[Tree]

InterPro

IPR001865. Ribosomal_S2.
IPR020589. Ribosomal_S2_bac/chp.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
[Graphical view]

PANTHER

PTHR12534. Ribosom_S2_bac. 1 hit.

Pfam

PF00318. Ribosomal_S2. 1 hit.
[Graphical view]

PRINTS

PR00395. RIBOSOMALS2.

TIGRFAMs

TIGR01011. rpsB_bact. 1 hit.

PROSITE

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

ProtoNet

Search...

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:	November 3, 2009
This is version 90 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)