30S ribosomal protein S20 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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P80380 (RS20_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
30S ribosomal protein S20

Gene names

Name:	rpsT
Synonyms:	rps20
Ordered Locus Names:	TTHA1397

Organism

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

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	106 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	One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the bottom of the body of the 30S subunit, by binding to several RNA helices of the 16S rRNA. HAMAP-Rule MF_00500
Subunit structure	Part of the 30S ribosomal subunit. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15
Sequence similarities	Belongs to the ribosomal protein S20P family.
Mass spectrometry	Molecular mass is 11572 Da from positions 2 - 106. Determined by MALDI. Ref.4

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	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	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

Removed Ref.3

Chain

2 – 106

105

30S ribosomal protein S20 HAMAP-Rule MF_00500

PRO_0000168050

Secondary structure

106

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P80380 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BEFD49F34F71F5E8
Show »

FASTA

106

11,703

        10         20         30         40         50         60 
MAQKKPKRNL SALKRHRQSL KRRLRNKAKK SAIKTLSKKA IQLAQEGKAE EALKIMRKAE 

        70         80         90        100 
SLIDKAAKGS TLHKNAAARR KSRLMRKVRQ LLEAAGAPLI GGGLSA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"On the characterization of the putative S20-thx operon of Thermus thermophilus." Leontiadou F., Triantafillidou D., Choli-Papadopoulou T. Biol. Chem. 382:1001-1006(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[3]	"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 2-33.
[4]	"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.
[5]	"Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution." Clemons W.M. Jr., May J.L.C., Wimberly B.T., McCutcheon J.P., Capel M.S., Ramakrishnan V. Nature 400:833-840(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE 30S SUBUNIT.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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

AJ295159 Genomic DNA. Translation: CAC15067.1.
AP008226 Genomic DNA. Translation: BAD71220.1.

RefSeq

YP_144663.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	T	1-106	[»]
1GIX	X-ray	5.50	W	1-106	[»]
1HNW	X-ray	3.40	T	1-106	[»]
1HNX	X-ray	3.40	T	1-106	[»]
1HNZ	X-ray	3.30	T	1-106	[»]
1HR0	X-ray	3.20	T	1-106	[»]
1I94	X-ray	3.20	T	2-106	[»]
1I95	X-ray	4.50	T	2-106	[»]
1I96	X-ray	4.20	T	2-106	[»]
1I97	X-ray	4.50	T	2-106	[»]
1IBK	X-ray	3.31	T	1-106	[»]
1IBL	X-ray	3.11	T	1-106	[»]
1IBM	X-ray	3.31	T	1-106	[»]
1J5E	X-ray	3.05	T	1-106	[»]
1JGO	X-ray	5.60	W	1-106	[»]
1JGP	X-ray	7.00	W	1-106	[»]
1JGQ	X-ray	5.00	W	1-106	[»]
1L1U	model	-	T	8-106	[»]
1N32	X-ray	3.00	T	1-106	[»]
1N33	X-ray	3.35	T	1-106	[»]
1N34	X-ray	3.80	T	1-106	[»]
1N36	X-ray	3.65	T	1-106	[»]
1XMO	X-ray	3.25	T	1-106	[»]
1XMQ	X-ray	3.00	T	1-106	[»]
1XNQ	X-ray	3.05	T	1-106	[»]
1XNR	X-ray	3.10	T	1-106	[»]
1YL4	X-ray	5.50	W	1-106	[»]
2B64	X-ray	5.90	T	1-106	[»]
2B9M	X-ray	6.76	T	1-106	[»]
2B9O	X-ray	6.46	T	1-106	[»]
2E5L	X-ray	3.30	T	2-106	[»]
2F4V	X-ray	3.80	T	1-106	[»]
2HGI	X-ray	5.00	W	1-106	[»]
2HGP	X-ray	5.50	W	1-106	[»]
2HGR	X-ray	4.51	W	1-106	[»]
2HHH	X-ray	3.35	T	1-106	[»]
2J00	X-ray	2.80	T	2-105	[»]
2J02	X-ray	2.80	T	2-105	[»]
2OW8	X-ray	3.71	u	1-106	[»]
2UU9	X-ray	3.10	T	2-105	[»]
2UUA	X-ray	2.90	T	1-106	[»]
2UUB	X-ray	2.90	T	2-105	[»]
2UUC	X-ray	3.10	T	2-105	[»]
2V46	X-ray	3.80	T	2-105	[»]
2V48	X-ray	3.50	T	1-106	[»]
2WDG	X-ray	3.30	T	1-106	[»]
2WDH	X-ray	3.30	T	1-106	[»]
2WDK	X-ray	3.50	T	1-106	[»]
2WDM	X-ray	3.50	T	1-106	[»]
2WH1	X-ray	3.45	T	1-106	[»]
2WH3	X-ray	3.45	T	1-106	[»]
2WRI	X-ray	3.60	T	1-106	[»]
2WRK	X-ray	3.60	T	1-106	[»]
2WRN	X-ray	3.60	T	1-106	[»]
2WRQ	X-ray	3.60	T	1-106	[»]
2X9R	X-ray	3.10	T	1-106	[»]
2X9T	X-ray	3.10	T	1-106	[»]
2XFZ	X-ray	3.20	T	1-106	[»]
2XG1	X-ray	3.20	T	1-106	[»]
2XQD	X-ray	3.10	T	1-106	[»]
2XSY	electron microscopy	7.80	T	1-106	[»]
2XUY	electron microscopy	7.60	T	1-106	[»]
2Y0U	X-ray	3.10	T	1-106	[»]
2Y0W	X-ray	3.10	T	1-106	[»]
2Y0Y	X-ray	3.10	T	1-106	[»]
2Y10	X-ray	3.10	T	1-106	[»]
2Y12	X-ray	3.10	T	1-106	[»]
2Y14	X-ray	3.10	T	1-106	[»]
2Y16	X-ray	3.10	T	1-106	[»]
2Y18	X-ray	3.10	T	1-106	[»]
2ZM6	X-ray	3.30	T	2-106	[»]
3FIC	electron microscopy	6.40	T	8-106	[»]
3HUW	X-ray	3.10	T	1-106	[»]
3HUY	X-ray	3.10	T	1-106	[»]
3I8G	X-ray	3.10	W	1-106	[»]
3I8H	X-ray	3.10	W	1-106	[»]
3I9B	X-ray	3.50	W	1-106	[»]
3I9D	X-ray	3.50	W	1-106	[»]
3KIQ	X-ray	3.30	t	1-106	[»]
3KIS	X-ray	3.30	t	1-106	[»]
3KIU	X-ray	3.60	t	1-106	[»]
3KIX	X-ray	3.60	t	1-106	[»]
3KNH	X-ray	3.00	T	1-106	[»]
3KNJ	X-ray	3.15	T	1-106	[»]
3KNL	X-ray	3.45	T	1-106	[»]
3KNN	X-ray	3.45	T	1-106	[»]
3OGE	X-ray	3.00	T	1-106	[»]
3OGY	X-ray	3.00	T	1-106	[»]
3OHC	X-ray	3.00	T	1-106	[»]
3OHD	X-ray	3.00	T	1-106	[»]
3OHY	X-ray	3.00	T	1-106	[»]
3OI0	X-ray	3.00	T	1-106	[»]
3OI2	X-ray	3.10	T	1-106	[»]
3OI4	X-ray	3.10	T	1-106	[»]
3OTO	X-ray	3.69	T	1-106	[»]
3TVF	X-ray	3.10	W	1-106	[»]
3TVG	X-ray	3.10	W	1-106	[»]
3UXS	X-ray	3.20	T	1-106	[»]
3UXT	X-ray	3.20	T	1-106	[»]
3UYD	X-ray	3.00	W	1-106	[»]
3UYF	X-ray	3.00	W	1-106	[»]
3UZ3	X-ray	3.30	W	1-106	[»]
3UZ4	X-ray	3.30	W	1-106	[»]
3UZ6	X-ray	3.00	W	1-106	[»]
3UZ7	X-ray	3.00	W	1-106	[»]
3UZG	X-ray	3.30	W	1-106	[»]
3UZI	X-ray	3.30	W	1-106	[»]
3UZL	X-ray	3.30	W	1-106	[»]
3UZM	X-ray	3.30	W	1-106	[»]
3V22	X-ray	3.00	T	1-106	[»]
3V24	X-ray	3.00	T	1-106	[»]
3V26	X-ray	3.10	T	1-106	[»]
3V28	X-ray	3.10	T	1-106	[»]
3V2C	X-ray	2.70	T	1-106	[»]
3V2E	X-ray	2.70	T	1-106	[»]
3ZVO	X-ray	3.80	T	1-106	[»]
4ABR	X-ray	3.10	T	1-106	[»]
4AQY	X-ray	3.50	T	1-106	[»]
4DH9	X-ray	3.20	T	1-106	[»]
4DHB	X-ray	3.20	T	1-106	[»]
4DR1	X-ray	3.60	T	1-106	[»]
4DR2	X-ray	3.25	T	1-106	[»]
4DR3	X-ray	3.35	T	1-106	[»]
4DR4	X-ray	3.97	T	1-106	[»]
4DR5	X-ray	3.45	T	1-106	[»]
4DR6	X-ray	3.30	T	1-106	[»]
4DR7	X-ray	3.75	T	1-106	[»]
4DUY	X-ray	3.39	T	1-106	[»]
4DUZ	X-ray	3.65	T	1-106	[»]
4DV0	X-ray	3.85	T	1-106	[»]
4DV1	X-ray	3.85	T	1-106	[»]
4DV2	X-ray	3.65	T	1-106	[»]
4DV3	X-ray	3.55	T	1-106	[»]
4DV4	X-ray	3.65	T	1-106	[»]
4DV5	X-ray	3.68	T	1-106	[»]
4DV6	X-ray	3.30	T	1-106	[»]
4DV7	X-ray	3.29	T	1-106	[»]
4G5K	X-ray	3.30	W	1-106	[»]
4G5M	X-ray	3.30	W	1-106	[»]
4G5T	X-ray	3.10	W	1-106	[»]
4G5V	X-ray	3.10	W	1-106	[»]

ProteinModelPortal

P80380.

SMR

P80380. Positions 8-106.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1397.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71220; BAD71220; BAD71220.

GeneID

3168087.

KEGG

ttj:TTHA1397.

PATRIC

23957751. VBITheThe93045_1371.

Phylogenomic databases

eggNOG

COG0268.

HOGENOM

HOG000097049.

K02968.

OMA

MRTAIKQ.

ProtClustDB

PRK00239.

Family and domain databases

Gene3D

1.20.58.110. 1 hit.

HAMAP

MF_00500. Ribosomal_S20.

InterPro

IPR002583. Ribosomal_S20.
[Graphical view]

Pfam

PF01649. Ribosomal_S20p. 1 hit.
[Graphical view]

ProDom

PD004231. Ribosomal_S20. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF46992. Ribosomal_S20p. 1 hit.

TIGRFAMs

TIGR00029. S20. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P80380.

Entry information

Entry name

RS20_THET8

Accession

Primary (citable) accession number: P80380
Secondary accession number(s): Q5SIH2, Q9F2A9

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

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents