30S ribosomal protein S11 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Contribute

Send feedback

Read comments (?) or add your own

P80376 (RS11_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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 S11

Gene names

Name:	rpsK
Synonyms:	rps11
Ordered Locus Names:	TTHA1666

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	129 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	Located on the upper part of the platform of the 30S subunit, where it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it interacts both with the Shine-Dalgarno helix and mRNA. HAMAP-Rule MF_01310
Subunit structure	Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to the C-terminus of IF-3; however exactly how IF-3 interacts with the 30S subunit is unclear. May contact the C-terminus of Era. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the ribosomal protein S11P family.
Mass spectrometry	Molecular mass is 13583 Da from positions 2 - 129. 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: InterPro
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
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

Removed Ref.3

Chain

2 – 129

128

30S ribosomal protein S11 HAMAP-Rule MF_01310

PRO_0000123246

Secondary structure

129

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P80376 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 028E047E6DCE3CA2
Show »

FASTA

129

13,713

        10         20         30         40         50         60 
MAKKPSKKKV KRQVASGRAY IHASYNNTIV TITDPDGNPI TWSSGGVIGY KGSRKGTPYA 

        70         80         90        100        110        120 
AQLAALDAAK KAMAYGMQSV DVIVRGTGAG REQAIRALQA SGLQVKSIVD DTPVPHNGCR 


PKKKFRKAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the RNA polymerase alpha subunit gene from Thermus thermophilus HB8 and characterization of the protein." Wada T., Yamazaki T., Kuramitsu S., Kyogoku Y. J. Biochem. 125:143-150(1999) [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 2-26.
[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 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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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

AB024328 Genomic DNA. Translation: BAA75547.1.
AP008226 Genomic DNA. Translation: BAD71489.1.

RefSeq

YP_144932.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	K	1-129	[»]
1GIX	X-ray	5.50	N	1-129	[»]
1HNW	X-ray	3.40	K	1-129	[»]
1HNX	X-ray	3.40	K	1-129	[»]
1HNZ	X-ray	3.30	K	1-129	[»]
1HR0	X-ray	3.20	K	1-129	[»]
1I94	X-ray	3.20	K	2-129	[»]
1I95	X-ray	4.50	K	2-129	[»]
1I96	X-ray	4.20	K	2-129	[»]
1I97	X-ray	4.50	K	2-129	[»]
1IBK	X-ray	3.31	K	1-129	[»]
1IBL	X-ray	3.11	K	1-129	[»]
1IBM	X-ray	3.31	K	1-129	[»]
1J5E	X-ray	3.05	K	1-129	[»]
1JGO	X-ray	5.60	N	1-129	[»]
1JGP	X-ray	7.00	N	1-129	[»]
1JGQ	X-ray	5.00	N	1-129	[»]
1L1U	model	-	K	11-129	[»]
1N32	X-ray	3.00	K	1-129	[»]
1N33	X-ray	3.35	K	1-129	[»]
1N34	X-ray	3.80	K	1-129	[»]
1N36	X-ray	3.65	K	1-129	[»]
1X18	electron microscopy	13.50	G	11-129	[»]
1XMO	X-ray	3.25	K	1-129	[»]
1XMQ	X-ray	3.00	K	1-129	[»]
1XNQ	X-ray	3.05	K	1-129	[»]
1XNR	X-ray	3.10	K	1-129	[»]
1YL4	X-ray	5.50	N	1-129	[»]
2B64	X-ray	5.90	K	1-129	[»]
2B9M	X-ray	6.76	K	1-129	[»]
2B9O	X-ray	6.46	K	1-129	[»]
2E5L	X-ray	3.30	K	2-129	[»]
2F4V	X-ray	3.80	K	1-129	[»]
2HGI	X-ray	5.00	N	1-129	[»]
2HGP	X-ray	5.50	N	1-129	[»]
2HGR	X-ray	4.51	N	1-129	[»]
2HHH	X-ray	3.35	K	1-129	[»]
2J00	X-ray	2.80	K	2-129	[»]
2J02	X-ray	2.80	K	2-129	[»]
2OW8	X-ray	3.71	l	-	[»]
2UU9	X-ray	3.10	K	2-129	[»]
2UUA	X-ray	2.90	K	1-129	[»]
2UUB	X-ray	2.90	K	2-129	[»]
2UUC	X-ray	3.10	K	2-128	[»]
2UXB	X-ray	3.10	K	1-129	[»]
2UXC	X-ray	2.90	K	1-129	[»]
2UXD	X-ray	3.20	K	1-129	[»]
2V46	X-ray	3.80	K	2-128	[»]
2V48	X-ray	3.50	K	1-129	[»]
2VQE	X-ray	2.50	K	1-129	[»]
2VQF	X-ray	2.90	K	1-129	[»]
2WDG	X-ray	3.30	K	1-129	[»]
2WDH	X-ray	3.30	K	1-129	[»]
2WDK	X-ray	3.50	K	1-129	[»]
2WDM	X-ray	3.50	K	1-129	[»]
2WH1	X-ray	3.45	K	1-129	[»]
2WH3	X-ray	3.45	K	1-129	[»]
2WRI	X-ray	3.60	K	1-129	[»]
2WRK	X-ray	3.60	K	1-129	[»]
2WRN	X-ray	3.60	K	1-129	[»]
2WRQ	X-ray	3.60	K	1-129	[»]
2X9R	X-ray	3.10	K	1-129	[»]
2X9T	X-ray	3.10	K	1-129	[»]
2XFZ	X-ray	3.20	K	1-129	[»]
2XG1	X-ray	3.20	K	1-129	[»]
2XQD	X-ray	3.10	K	1-129	[»]
2XSY	electron microscopy	7.80	K	1-129	[»]
2XUY	electron microscopy	7.60	K	1-129	[»]
2Y0U	X-ray	3.10	K	1-129	[»]
2Y0W	X-ray	3.10	K	1-129	[»]
2Y0Y	X-ray	3.10	K	1-129	[»]
2Y10	X-ray	3.10	K	1-129	[»]
2Y12	X-ray	3.10	K	1-129	[»]
2Y14	X-ray	3.10	K	1-129	[»]
2Y16	X-ray	3.10	K	1-129	[»]
2Y18	X-ray	3.10	K	1-129	[»]
2ZM6	X-ray	3.30	K	2-129	[»]
3FIC	electron microscopy	6.40	K	11-129	[»]
3HUW	X-ray	3.10	K	1-129	[»]
3HUY	X-ray	3.10	K	1-129	[»]
3I8G	X-ray	3.10	N	1-129	[»]
3I8H	X-ray	3.10	N	1-129	[»]
3I9B	X-ray	3.50	N	1-129	[»]
3I9D	X-ray	3.50	N	1-129	[»]
3KIQ	X-ray	3.30	k	1-129	[»]
3KIS	X-ray	3.30	k	1-129	[»]
3KIU	X-ray	3.60	k	1-129	[»]
3KIX	X-ray	3.60	k	1-129	[»]
3KNH	X-ray	3.00	K	1-129	[»]
3KNJ	X-ray	3.15	K	1-129	[»]
3KNL	X-ray	3.45	K	1-129	[»]
3KNN	X-ray	3.45	K	1-129	[»]
3OGE	X-ray	3.00	K	1-129	[»]
3OGY	X-ray	3.00	K	1-129	[»]
3OHC	X-ray	3.00	K	1-129	[»]
3OHD	X-ray	3.00	K	1-129	[»]
3OHY	X-ray	3.00	K	1-129	[»]
3OI0	X-ray	3.00	K	1-129	[»]
3OI2	X-ray	3.10	K	1-129	[»]
3OI4	X-ray	3.10	K	1-129	[»]
3OTO	X-ray	3.69	K	1-129	[»]
3T1H	X-ray	3.11	K	1-129	[»]
3T1Y	X-ray	2.80	K	1-129	[»]
3TVF	X-ray	3.10	N	1-129	[»]
3TVG	X-ray	3.10	N	1-129	[»]
3UXS	X-ray	3.20	K	1-129	[»]
3UXT	X-ray	3.20	K	1-129	[»]
3UYD	X-ray	3.00	N	1-129	[»]
3UYF	X-ray	3.00	N	1-129	[»]
3UZ3	X-ray	3.30	N	1-129	[»]
3UZ4	X-ray	3.30	N	1-129	[»]
3UZ6	X-ray	3.00	N	1-129	[»]
3UZ7	X-ray	3.00	N	1-129	[»]
3UZG	X-ray	3.30	N	1-129	[»]
3UZI	X-ray	3.30	N	1-129	[»]
3UZL	X-ray	3.30	N	1-129	[»]
3UZM	X-ray	3.30	N	1-129	[»]
3V22	X-ray	3.00	K	1-129	[»]
3V24	X-ray	3.00	K	1-129	[»]
3V26	X-ray	3.10	K	1-129	[»]
3V28	X-ray	3.10	K	1-129	[»]
3V2C	X-ray	2.70	K	1-129	[»]
3V2E	X-ray	2.70	K	1-129	[»]
3ZVO	X-ray	3.80	K	1-129	[»]
4ABR	X-ray	3.10	K	1-129	[»]
4AQY	X-ray	3.50	K	1-129	[»]
4DH9	X-ray	3.20	K	1-129	[»]
4DHB	X-ray	3.20	K	1-129	[»]
4DR1	X-ray	3.60	K	1-129	[»]
4DR2	X-ray	3.25	K	1-129	[»]
4DR3	X-ray	3.35	K	1-129	[»]
4DR4	X-ray	3.97	K	1-129	[»]
4DR5	X-ray	3.45	K	1-129	[»]
4DR6	X-ray	3.30	K	1-129	[»]
4DR7	X-ray	3.75	K	1-129	[»]
4DUY	X-ray	3.39	K	1-129	[»]
4DUZ	X-ray	3.65	K	1-129	[»]
4DV0	X-ray	3.85	K	1-129	[»]
4DV1	X-ray	3.85	K	1-129	[»]
4DV2	X-ray	3.65	K	1-129	[»]
4DV3	X-ray	3.55	K	1-129	[»]
4DV4	X-ray	3.65	K	1-129	[»]
4DV5	X-ray	3.68	K	1-129	[»]
4DV6	X-ray	3.30	K	1-129	[»]
4DV7	X-ray	3.29	K	1-129	[»]
4G5K	X-ray	3.30	N	1-129	[»]
4G5M	X-ray	3.30	N	1-129	[»]
4G5T	X-ray	3.10	N	1-129	[»]
4G5V	X-ray	3.10	N	1-129	[»]

ProteinModelPortal

P80376.

SMR

P80376. Positions 7-129.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1666.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71489; BAD71489; BAD71489.

GeneID

3168024.

KEGG

ttj:TTHA1666.

PATRIC

23958287. VBITheThe93045_1636.

Phylogenomic databases

eggNOG

COG0100.

HOGENOM

HOG000111597.

K02948.

OMA

PHNGCRR.

ProtClustDB

PRK05309.

Family and domain databases

Gene3D

3.30.420.80. 1 hit.

HAMAP

MF_01310. Ribosomal_S11.

InterPro

IPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]

PANTHER

PTHR11759. PTHR11759. 1 hit.

Pfam

PF00411. Ribosomal_S11. 1 hit.
[Graphical view]

PIRSF

PIRSF002131. Ribosomal_S11. 1 hit.

TIGRFAMs

TIGR03632. bact_S11. 1 hit.

PROSITE

PS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80376.

Entry information

Entry name

RS11_THET8

Accession

Primary (citable) accession number: P80376
Secondary accession number(s): Q5SHR4, Q9RA66

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 109 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

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

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