30S ribosomal protein S9 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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P80374 (RS9_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. 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 S9

Gene names

Name:	rpsI
Synonyms:	rps9
Ordered Locus Names:	TTHA1464

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	128 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of the top of the head of the 30S subunit. The C-terminal region penetrates the head emerging in the P-site where it contacts tRNA. HAMAP-Rule MF_00532_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S7 and S10. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13
Sequence similarities	Belongs to the ribosomal protein S9P family.
Mass spectrometry	Molecular mass is 14384 Da from positions 1 - 128. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-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: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 128

128

30S ribosomal protein S9 HAMAP-Rule MF_00532_B

PRO_0000111431

Secondary structure

128

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P80374 [UniParc].

Last modified May 10, 2005. Version 3.
Checksum: FA9A4ED2CC5D8CC1
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FASTA

128

14,383

        10         20         30         40         50         60 
MEQYYGTGRR KEAVARVFLR PGNGKVTVNG QDFNEYFQGL VRAVAALEPL RAVDALGHFD 

        70         80         90        100        110        120 
AYITVRGGGK SGQIDAIKLG IARALVQYNP DYRAKLKPLG FLTRDARVVE RKKYGKHKAR 


RAPQYSKR

« Hide

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 1-28.
[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: BAD71287.1.

RefSeq

YP_144730.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P80374.

SMR

P80374. Positions 2-128.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1464.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71287; BAD71287; BAD71287.

GeneID

3169752.

KEGG

ttj:TTHA1464.

PATRIC

23957885. VBITheThe93045_1438.

Phylogenomic databases

eggNOG

COG0103.

HOGENOM

HOG000019802.

K02996.

OMA

IKQGAAR.

ProtClustDB

PRK00132.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.

HAMAP

MF_00532_B. Ribosomal_S9_B.

InterPro

IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]

PANTHER

PTHR21569. PTHR21569. 1 hit.

Pfam

PF00380. Ribosomal_S9. 1 hit.
[Graphical view]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

PROSITE

PS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80374.

Entry information

Entry name

RS9_THET8

Accession

Primary (citable) accession number: P80374
Secondary accession number(s): Q5SIB0, Q9ACJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 114 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