30S ribosomal protein S5 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Contribute

Send feedback

Read comments (?) or add your own

Q5SHQ5 (RS5_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. 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 S5

Gene names

Name:	rpsE
Ordered Locus Names:	TTHA1675

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	162 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	With S4 and S12 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_01307_B Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Binds mRNA in the 70S ribosome, positioning it for translation. HAMAP-Rule MF_01307_B
Subunit structure	Part of the 30S ribosomal subunit. Contacts proteins S4 and S8. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15
Domain	The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity. HAMAP-Rule MF_01307_B
Miscellaneous	Is positioned such that it could physically interact with spectinomycin. HAMAP-Rule MF_01307_B
Sequence similarities	Belongs to the ribosomal protein S5P family. Contains 1 S5 DRBM domain.
Mass spectrometry	Molecular mass is 17428 Da from positions 2 - 162. Determined by MALDI. Ref.3

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	small ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 162

161

30S ribosomal protein S5 HAMAP-Rule MF_01307_B

PRO_0000131621

Regions

Domain

6 – 69

S5 DRBM

Secondary structure

162

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SHQ5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BE3367CB619E68D2
Show »

FASTA

162

17,557

        10         20         30         40         50         60 
MPETDFEEKM ILIRRTARMQ AGGRRFRFGA LVVVGDRQGR VGLGFGKAPE VPLAVQKAGY 

        70         80         90        100        110        120 
YARRNMVEVP LQNGTIPHEI EVEFGASKIV LKPAAPGTGV IAGAVPRAIL ELAGVTDILT 

       130        140        150        160 
KELGSRNPIN IAYATMEALR QLRTKADVER LRKGEAHAQA QG

« 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 2-44.
[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 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.
[5]	"The small ribosomal subunit from Thermus thermophilus at 4.5 A resolution: pattern fittings and the identification of a functional site." Tocilj A., Schluenzen F., Janell D., Gluehmann M., Hansen H.A., Harms J., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A. Proc. Natl. Acad. Sci. U.S.A. 96:14252-14257(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
[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

AP008226 Genomic DNA. Translation: BAD71498.1.

RefSeq

YP_144941.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	E	1-162	[»]
1FKA	X-ray	3.30	E	1-162	[»]
1GIX	X-ray	5.50	H	1-162	[»]
1HNW	X-ray	3.40	E	1-162	[»]
1HNX	X-ray	3.40	E	1-162	[»]
1HNZ	X-ray	3.30	E	1-162	[»]
1HR0	X-ray	3.20	E	1-162	[»]
1I94	X-ray	3.20	E	2-162	[»]
1I95	X-ray	4.50	E	2-162	[»]
1I96	X-ray	4.20	E	2-162	[»]
1I97	X-ray	4.50	E	2-162	[»]
1IBK	X-ray	3.31	E	1-162	[»]
1IBL	X-ray	3.11	E	1-162	[»]
1IBM	X-ray	3.31	E	1-162	[»]
1J5E	X-ray	3.05	E	2-162	[»]
1JGO	X-ray	5.60	H	1-162	[»]
1JGP	X-ray	7.00	H	1-162	[»]
1JGQ	X-ray	5.00	H	1-162	[»]
1L1U	model	-	E	5-154	[»]
1N32	X-ray	3.00	E	2-162	[»]
1N33	X-ray	3.35	E	2-162	[»]
1N34	X-ray	3.80	E	2-162	[»]
1N36	X-ray	3.65	E	2-162	[»]
1QD7	X-ray	5.50	D	22-130	[»]
1XMO	X-ray	3.25	E	1-162	[»]
1XMQ	X-ray	3.00	E	1-162	[»]
1XNQ	X-ray	3.05	E	1-162	[»]
1XNR	X-ray	3.10	E	1-162	[»]
1YL4	X-ray	5.50	H	1-162	[»]
2B64	X-ray	5.90	E	1-162	[»]
2B9M	X-ray	6.76	E	1-162	[»]
2B9O	X-ray	6.46	E	1-162	[»]
2E5L	X-ray	3.30	E	2-162	[»]
2F4V	X-ray	3.80	E	1-162	[»]
2HGI	X-ray	5.00	H	1-162	[»]
2HGP	X-ray	5.50	H	1-162	[»]
2HGR	X-ray	4.51	H	1-162	[»]
2HHH	X-ray	3.35	E	1-162	[»]
2J00	X-ray	2.80	E	2-161	[»]
2J02	X-ray	2.80	E	2-161	[»]
2OW8	X-ray	3.71	f	-	[»]
2UU9	X-ray	3.10	E	2-161	[»]
2UUA	X-ray	2.90	E	1-162	[»]
2UUB	X-ray	2.90	E	2-161	[»]
2UUC	X-ray	3.10	E	2-161	[»]
2UXB	X-ray	3.10	E	1-162	[»]
2UXC	X-ray	2.90	E	1-162	[»]
2UXD	X-ray	3.20	E	1-162	[»]
2V46	X-ray	3.80	E	2-161	[»]
2V48	X-ray	3.50	E	1-162	[»]
2VQE	X-ray	2.50	E	1-162	[»]
2VQF	X-ray	2.90	E	1-162	[»]
2WDG	X-ray	3.30	E	1-162	[»]
2WDH	X-ray	3.30	E	1-162	[»]
2WDK	X-ray	3.50	E	1-162	[»]
2WDM	X-ray	3.50	E	1-162	[»]
2WH1	X-ray	3.45	E	1-162	[»]
2WH3	X-ray	3.45	E	1-162	[»]
2WRI	X-ray	3.60	E	1-162	[»]
2WRK	X-ray	3.60	E	1-162	[»]
2WRN	X-ray	3.60	E	1-162	[»]
2WRQ	X-ray	3.60	E	1-162	[»]
2X9R	X-ray	3.10	E	1-162	[»]
2X9T	X-ray	3.10	E	1-162	[»]
2XFZ	X-ray	3.20	E	1-162	[»]
2XG1	X-ray	3.20	E	1-162	[»]
2XQD	X-ray	3.10	E	1-162	[»]
2XSY	electron microscopy	7.80	E	1-162	[»]
2XUY	electron microscopy	7.60	E	1-162	[»]
2Y0U	X-ray	3.10	E	1-162	[»]
2Y0W	X-ray	3.10	E	1-162	[»]
2Y0Y	X-ray	3.10	E	1-162	[»]
2Y10	X-ray	3.10	E	1-162	[»]
2Y12	X-ray	3.10	E	1-162	[»]
2Y14	X-ray	3.10	E	1-162	[»]
2Y16	X-ray	3.10	E	1-162	[»]
2Y18	X-ray	3.10	E	1-162	[»]
2ZM6	X-ray	3.30	E	2-162	[»]
3FIC	electron microscopy	6.40	E	5-155	[»]
3HUW	X-ray	3.10	E	1-162	[»]
3HUY	X-ray	3.10	E	1-162	[»]
3I8G	X-ray	3.10	H	1-162	[»]
3I8H	X-ray	3.10	H	1-162	[»]
3I9B	X-ray	3.50	H	1-162	[»]
3I9D	X-ray	3.50	H	1-162	[»]
3KIQ	X-ray	3.30	e	1-162	[»]
3KIS	X-ray	3.30	e	1-162	[»]
3KIU	X-ray	3.60	e	1-162	[»]
3KIX	X-ray	3.60	e	1-162	[»]
3KNH	X-ray	3.00	E	1-162	[»]
3KNJ	X-ray	3.15	E	1-162	[»]
3KNL	X-ray	3.45	E	1-162	[»]
3KNN	X-ray	3.45	E	1-162	[»]
3OGE	X-ray	3.00	E	1-162	[»]
3OGY	X-ray	3.00	E	1-162	[»]
3OHC	X-ray	3.00	E	1-160	[»]
3OHD	X-ray	3.00	E	1-160	[»]
3OHY	X-ray	3.00	E	1-162	[»]
3OI0	X-ray	3.00	E	1-162	[»]
3OI2	X-ray	3.10	E	1-162	[»]
3OI4	X-ray	3.10	E	1-162	[»]
3OTO	X-ray	3.69	E	1-162	[»]
3T1H	X-ray	3.11	E	1-162	[»]
3T1Y	X-ray	2.80	E	1-162	[»]
3TVF	X-ray	3.10	H	1-162	[»]
3TVG	X-ray	3.10	H	1-162	[»]
3UXS	X-ray	3.20	E	1-162	[»]
3UXT	X-ray	3.20	E	1-162	[»]
3UYD	X-ray	3.00	H	1-162	[»]
3UYF	X-ray	3.00	H	1-162	[»]
3UZ3	X-ray	3.30	H	1-162	[»]
3UZ4	X-ray	3.30	H	1-162	[»]
3UZ6	X-ray	3.00	H	1-162	[»]
3UZ7	X-ray	3.00	H	1-162	[»]
3UZG	X-ray	3.30	H	1-162	[»]
3UZI	X-ray	3.30	H	1-162	[»]
3UZL	X-ray	3.30	H	1-162	[»]
3UZM	X-ray	3.30	H	1-162	[»]
3V22	X-ray	3.00	E	1-162	[»]
3V24	X-ray	3.00	E	1-162	[»]
3V26	X-ray	3.10	E	1-162	[»]
3V28	X-ray	3.10	E	1-162	[»]
3V2C	X-ray	2.70	E	1-162	[»]
3V2E	X-ray	2.70	E	1-162	[»]
3ZVO	X-ray	3.80	E	1-162	[»]
4ABR	X-ray	3.10	E	1-162	[»]
4AQY	X-ray	3.50	E	2-162	[»]
4DH9	X-ray	3.20	E	1-162	[»]
4DHB	X-ray	3.20	E	1-162	[»]
4DR1	X-ray	3.60	E	1-162	[»]
4DR2	X-ray	3.25	E	1-162	[»]
4DR3	X-ray	3.35	E	1-162	[»]
4DR4	X-ray	3.97	E	1-162	[»]
4DR5	X-ray	3.45	E	1-162	[»]
4DR6	X-ray	3.30	E	1-162	[»]
4DR7	X-ray	3.75	E	1-162	[»]
4DUY	X-ray	3.39	E	1-162	[»]
4DUZ	X-ray	3.65	E	1-162	[»]
4DV0	X-ray	3.85	E	1-162	[»]
4DV1	X-ray	3.85	E	1-162	[»]
4DV2	X-ray	3.65	E	1-162	[»]
4DV3	X-ray	3.55	E	1-162	[»]
4DV4	X-ray	3.65	E	1-162	[»]
4DV5	X-ray	3.68	E	1-162	[»]
4DV6	X-ray	3.30	E	1-162	[»]
4DV7	X-ray	3.29	E	1-162	[»]
4G5K	X-ray	3.30	H	1-162	[»]
4G5M	X-ray	3.30	H	1-162	[»]
4G5T	X-ray	3.10	H	1-162	[»]
4G5V	X-ray	3.10	H	1-162	[»]

ProteinModelPortal

Q5SHQ5.

SMR

Q5SHQ5. Positions 1-157.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1675.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71498; BAD71498; BAD71498.

GeneID

3169827.

KEGG

ttj:TTHA1675.

PATRIC

23958305. VBITheThe93045_1645.

Phylogenomic databases

eggNOG

COG0098.

HOGENOM

HOG000072595.

K02988.

OMA

YNASKIL.

ProtClustDB

PRK00550.

Family and domain databases

Gene3D

3.30.160.20. 1 hit.
3.30.230.10. 1 hit.

HAMAP

MF_01307_B. Ribosomal_S5_B.

InterPro

IPR014720. dsRNA-bd-like_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]

PANTHER

PTHR13718. PTHR13718. 1 hit.

Pfam

PF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR01021. rpsE_bact. 1 hit.

PROSITE

PS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHQ5.

Entry information

Entry name

RS5_THET8

Accession

Primary (citable) accession number: Q5SHQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 80 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

Regions

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