Q5SHP7 (RS17_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S17

Gene names

Name:	rpsQ
Ordered Locus Names:	TTHA1683

Organism

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

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	105 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 helps nucleate assembly of the platform and body of the 30S subunit by bringing together and stabilizing interactions between several different RNA helices. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. HAMAP-Rule MF_01345 Deletion of the protein leads to an increased generation time and a temperature-sensitive phenotype. HAMAP-Rule MF_01345
Subunit structure	Part of the 30S ribosomal subunit. Contacts protein S12. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16
Sequence similarities	Belongs to the ribosomal protein S17P family.
Mass spectrometry	Molecular mass is 12167 Da from positions 2 - 105. Determined by MALDI. Ref.5

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

1

1

Removed Ref.3

Chain

2 – 105

104

30S ribosomal protein S17 HAMAP-Rule MF_01345

PRO_0000128492

Experimental info

Sequence conflict

50

1

K → R in CAA39893. Ref.1

Sequence conflict

53

1

L → V in CAA39893. Ref.1

Sequence conflict

62

1

S → A in CAA39893. Ref.1

Sequence conflict

79

1

S → E in CAA39893. Ref.1

Sequence conflict

82

1

M → L in CAA39893. Ref.1

Sequence conflict

90

1

I → V in CAA39893. Ref.1

Sequence conflict

96

1

E → A in CAA39893. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

15 – 17

3

Beta strand

18 – 28

11

Turn

30 – 32

3

Beta strand

35 – 45

11

Beta strand

47 – 49

3

Beta strand

56 – 61

6

Beta strand

66 – 68

3

Beta strand

71 – 76

6

Beta strand

77 – 79

3

Helix

82 – 94

13

Turn

95 – 97

3

Beta strand

98 – 101

4

Sequences

	Sequence		Length	Mass (Da)
	Q5SHP7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 60981D6D57478FBD	FASTA	105	12,298
	10 20 30 40 50 60 MPKKVLTGVV VSDKMQKTVT VLVERQFPHP LYGKVIKRSK KYLAHDPEEK YKLGDVVEII 70 80 90 100 ESRPISKRKR FRVLRLVESG RMDLVEKYLI RRQNYESLSK RGGKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the spc ribosomal protein operon of Thermus aquaticus." Jahn O., Hartmann R.K., Erdmann V.A. Eur. J. Biochem. 197:733-740(1991) [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 2-14.
[4]	"Ribosomal gene disruption in the extreme thermophile Thermus thermophilus HB8. Generation of a mutant lacking ribosomal protein S17." Simitsopoulou M., Avila H., Franceschi F. Eur. J. Biochem. 266:524-532(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DELETION OF THE GENE.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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

X56552 Genomic DNA. Translation: CAA39893.1.
AP008226 Genomic DNA. Translation: BAD71506.1.

RefSeq

YP_144949.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FJG	X-ray	3.00	Q	1-105	[»]
1GIX	X-ray	5.50	T	1-105	[»]
1HNW	X-ray	3.40	Q	1-105	[»]
1HNX	X-ray	3.40	Q	1-105	[»]
1HNZ	X-ray	3.30	Q	1-105	[»]
1HR0	X-ray	3.20	Q	1-105	[»]
1I94	X-ray	3.20	Q	2-105	[»]
1I95	X-ray	4.50	Q	2-105	[»]
1I96	X-ray	4.20	Q	2-105	[»]
1I97	X-ray	4.50	Q	2-105	[»]
1IBK	X-ray	3.31	Q	1-105	[»]
1IBL	X-ray	3.11	Q	1-105	[»]
1IBM	X-ray	3.31	Q	1-105	[»]
1J5E	X-ray	3.05	Q	2-105	[»]
1JGO	X-ray	5.60	T	1-105	[»]
1JGP	X-ray	7.00	T	1-105	[»]
1JGQ	X-ray	5.00	T	1-105	[»]
1L1U	model	-	Q	1-105	[»]
1N32	X-ray	3.00	Q	2-105	[»]
1N33	X-ray	3.35	Q	2-105	[»]
1N34	X-ray	3.80	Q	2-105	[»]
1N36	X-ray	3.65	Q	2-105	[»]
1XMO	X-ray	3.25	Q	1-105	[»]
1XMQ	X-ray	3.00	Q	1-105	[»]
1XNQ	X-ray	3.05	Q	1-105	[»]
1XNR	X-ray	3.10	Q	1-105	[»]
1YL4	X-ray	5.50	T	1-105	[»]
2B64	X-ray	5.90	Q	1-105	[»]
2B9M	X-ray	6.76	Q	1-105	[»]
2B9O	X-ray	6.46	Q	1-105	[»]
2E5L	X-ray	3.30	Q	2-105	[»]
2F4V	X-ray	3.80	Q	1-105	[»]
2HGI	X-ray	5.00	T	1-105	[»]
2HGP	X-ray	5.50	T	1-105	[»]
2HGR	X-ray	4.51	T	1-105	[»]
2HHH	X-ray	3.35	Q	1-105	[»]
2J00	X-ray	2.80	Q	2-104	[»]
2J02	X-ray	2.80	Q	2-104	[»]
2OW8	X-ray	3.71	r	1-105	[»]
2UU9	X-ray	3.10	Q	2-104	[»]
2UUA	X-ray	2.90	Q	1-105	[»]
2UUB	X-ray	2.90	Q	2-104	[»]
2UUC	X-ray	3.10	Q	2-104	[»]
2UXB	X-ray	3.10	Q	1-105	[»]
2UXC	X-ray	2.90	Q	1-105	[»]
2UXD	X-ray	3.20	Q	1-105	[»]
2V46	X-ray	3.80	Q	2-104	[»]
2V48	X-ray	3.50	Q	1-105	[»]
2WDG	X-ray	3.30	Q	1-105	[»]
2WDH	X-ray	3.30	Q	1-105	[»]
2WDK	X-ray	3.50	Q	1-105	[»]
2WDM	X-ray	3.50	Q	1-105	[»]
2WH1	X-ray	3.45	Q	1-105	[»]
2WH3	X-ray	3.45	Q	1-105	[»]
2WRI	X-ray	3.60	Q	1-105	[»]
2WRK	X-ray	3.60	Q	1-105	[»]
2WRN	X-ray	3.60	Q	1-105	[»]
2WRQ	X-ray	3.60	Q	1-105	[»]
2X9R	X-ray	3.10	Q	1-105	[»]
2X9T	X-ray	3.10	Q	1-105	[»]
2XFZ	X-ray	3.20	Q	1-105	[»]
2XG1	X-ray	3.20	Q	1-105	[»]
2XQD	X-ray	3.10	Q	1-105	[»]
2XSY	electron microscopy	7.80	Q	1-105	[»]
2XUY	electron microscopy	7.60	Q	1-105	[»]
2Y0U	X-ray	3.10	Q	1-105	[»]
2Y0W	X-ray	3.10	Q	1-105	[»]
2Y0Y	X-ray	3.10	Q	1-105	[»]
2Y10	X-ray	3.10	Q	1-105	[»]
2Y12	X-ray	3.10	Q	1-105	[»]
2Y14	X-ray	3.10	Q	1-105	[»]
2Y16	X-ray	3.10	Q	1-105	[»]
2Y18	X-ray	3.10	Q	1-105	[»]
2ZM6	X-ray	3.30	Q	2-105	[»]
3FIC	electron microscopy	6.40	Q	2-101	[»]
3HUW	X-ray	3.10	Q	1-105	[»]
3HUY	X-ray	3.10	Q	1-105	[»]
3I8G	X-ray	3.10	T	1-105	[»]
3I8H	X-ray	3.10	T	1-105	[»]
3I9B	X-ray	3.50	T	1-105	[»]
3I9D	X-ray	3.50	T	1-105	[»]
3KIQ	X-ray	3.30	q	1-105	[»]
3KIS	X-ray	3.30	q	1-105	[»]
3KIU	X-ray	3.60	q	1-105	[»]
3KIX	X-ray	3.60	q	1-105	[»]
3KNH	X-ray	3.00	Q	1-105	[»]
3KNJ	X-ray	3.15	Q	1-105	[»]
3KNL	X-ray	3.45	Q	1-105	[»]
3KNN	X-ray	3.45	Q	1-105	[»]
3OGE	X-ray	3.00	Q	1-105	[»]
3OGY	X-ray	3.00	Q	1-105	[»]
3OHC	X-ray	3.00	Q	1-105	[»]
3OHD	X-ray	3.00	Q	1-105	[»]
3OHY	X-ray	3.00	Q	1-105	[»]
3OI0	X-ray	3.00	Q	1-105	[»]
3OI2	X-ray	3.10	Q	1-105	[»]
3OI4	X-ray	3.10	Q	1-105	[»]
3OTO	X-ray	3.69	Q	1-105	[»]
3T1H	X-ray	3.11	Q	1-105	[»]
3T1Y	X-ray	2.80	Q	1-105	[»]
3TVF	X-ray	3.10	T	1-105	[»]
3TVG	X-ray	3.10	T	1-105	[»]
3UXS	X-ray	3.20	Q	1-105	[»]
3UXT	X-ray	3.20	Q	1-105	[»]
3UYD	X-ray	3.00	T	1-105	[»]
3UYF	X-ray	3.00	T	1-105	[»]
3UZ3	X-ray	3.30	T	1-105	[»]
3UZ4	X-ray	3.30	T	1-105	[»]
3UZ6	X-ray	3.00	T	1-105	[»]
3UZ7	X-ray	3.00	T	1-105	[»]
3UZG	X-ray	3.30	T	1-105	[»]
3UZI	X-ray	3.30	T	1-105	[»]
3UZL	X-ray	3.30	T	1-105	[»]
3UZM	X-ray	3.30	T	1-105	[»]
3V22	X-ray	3.00	Q	1-105	[»]
3V24	X-ray	3.00	Q	1-105	[»]
3V26	X-ray	3.10	Q	1-105	[»]
3V28	X-ray	3.10	Q	1-105	[»]
3V2C	X-ray	2.70	Q	1-105	[»]
3V2E	X-ray	2.70	Q	1-105	[»]
3ZVO	X-ray	3.80	Q	1-105	[»]
4ABR	X-ray	3.10	Q	1-105	[»]
4AQY	X-ray	3.50	Q	2-105	[»]
4DH9	X-ray	3.20	Q	1-105	[»]
4DHB	X-ray	3.20	Q	1-105	[»]
4DR1	X-ray	3.60	Q	1-105	[»]
4DR2	X-ray	3.25	Q	1-105	[»]
4DR3	X-ray	3.35	Q	1-105	[»]
4DR4	X-ray	3.97	Q	1-105	[»]
4DR5	X-ray	3.45	Q	1-105	[»]
4DR6	X-ray	3.30	Q	1-105	[»]
4DR7	X-ray	3.75	Q	1-105	[»]
4DUY	X-ray	3.39	Q	1-105	[»]
4DUZ	X-ray	3.65	Q	1-105	[»]
4DV0	X-ray	3.85	Q	1-105	[»]
4DV1	X-ray	3.85	Q	1-105	[»]
4DV2	X-ray	3.65	Q	1-105	[»]
4DV3	X-ray	3.55	Q	1-105	[»]
4DV4	X-ray	3.65	Q	1-105	[»]
4DV5	X-ray	3.68	Q	1-105	[»]
4DV6	X-ray	3.30	Q	1-105	[»]
4DV7	X-ray	3.29	Q	1-105	[»]
4G5K	X-ray	3.30	T	1-105	[»]
4G5M	X-ray	3.30	T	1-105	[»]
4G5T	X-ray	3.10	T	1-105	[»]
4G5V	X-ray	3.10	T	1-105	[»]

ProteinModelPortal

Q5SHP7.

SMR

Q5SHP7. Positions 2-105.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1683.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71506; BAD71506; BAD71506.

GeneID

3169831.

KEGG

ttj:TTHA1683.

PATRIC

23958321. VBITheThe93045_1653.

Phylogenomic databases

eggNOG

COG0186.

HOGENOM

HOG000231339.

KO

K02961.

OMA

WIVVKDS.

ProtClustDB

PRK05610.

Family and domain databases

Gene3D

2.40.50.140. 1 hit.

HAMAP

MF_01345_B. Ribosomal_S17_B.

InterPro

IPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]

PANTHER

PTHR10744. PTHR10744. 1 hit.

Pfam

PF00366. Ribosomal_S17. 1 hit.
[Graphical view]

PRINTS

PR00973. RIBOSOMALS17.

ProDom

PD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

TIGRFAMs

TIGR03635. S17_bact. 1 hit.

PROSITE

PS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHP7.

Entry information

Entry name

RS17_THET8

Accession

Primary (citable) accession number: Q5SHP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program