30S ribosomal protein S17 - Escherichia coli (strain K12)

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P0AG63 (RS17_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
30S ribosomal protein S17

Gene names

Name:	rpsQ
Synonyms:	neaA
Ordered Locus Names:	b3311, JW3273

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	84 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 specifically to the 5'-end of 16S ribosomal RNA. Also plays a role in translational accuracy; neamine-resistant ribosomes show reduced neamine-induced misreading in vitro. HAMAP-Rule MF_01345
Subunit structure	Part of the 30S ribosomal subunit. Ref.8
Miscellaneous	The strain missing both S17 and L29 grows very slowly and has a rather unstable temperature-sensitive phenotype. HAMAP-Rule MF_01345
Sequence similarities	Belongs to the ribosomal protein S17P family.
Mass spectrometry	Molecular mass is 9573.0 Da from positions 2 - 84. Determined by MALDI. Ref.12

Ontologies

Keywords
Biological process	Antibiotic resistance
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	response to antibiotic Inferred from mutant phenotype Ref.13. Source: EcoliWiki translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosolic small ribosomal subunit Inferred from direct assay PubMed 4587209. Source: EcoliWiki
Molecular_function	SSU rRNA binding Inferred from direct assay Ref.8. Source: EcoliWiki 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.4 Ref.6

Chain

2 – 84

30S ribosomal protein S17 HAMAP-Rule MF_01345

PRO_0000128456

Natural variations

Natural variant

H → P in neamine-resistant mutant nea301.

Natural variant

S → F Prevents 30S subunit assembly at 42 degrees Celsius. Ref.10

Experimental info

Sequence conflict

53 – 59

CGIGDVV → GIGDVVC AA sequence Ref.4

Sequence conflict

64 – 66

CRP → RPC Ref.5

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AG63 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FC64AF04841842F6
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FASTA

9,704

        10         20         30         40         50         60 
MTDKIRTLQG RVVSDKMEKS IVVAIERFVK HPIYGKFIKR TTKLHVHDEN NECGIGDVVE 

        70         80 
IRECRPLSKT KSWTLVRVVE KAVL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The primary structure of protein S17 from the small ribosomal subunit of Escherichia coli." Yaguchi M., Wittmann H.G. FEBS Lett. 87:37-40(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-84. Strain: K.
[5]	"DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli." Post L.E., Arfsten A.E., Reusser F., Nomura M. Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-84. Strain: K12.
[6]	"Small genes/gene-products in Escherichia coli K-12." Wasinger V.C., Humphery-Smith I. FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Strain: K12.
[7]	"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-36, CROSS-LINKING TO RRNA. Strain: MRE-600.
[8]	"Assembly mapping of 30 S ribosomal proteins from Escherichia coli. Further studies." Held W.A., Ballou B., Mizushima S., Nomura M. J. Biol. Chem. 249:3103-3111(1974) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A PRIMARY 16S RRNA-BINDING PROTEIN, ASSEMBLY MAP OF THE 30S SUBUNIT. Strain: Q13.
[9]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[10]	"A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli." Herzog A., Yaguchi M., Cabezon T., Corchuelo M.C., Petre J., Bollen A. Mol. Gen. Genet. 171:15-22(1979) [PubMed] [Europe PMC] [Abstract] Cited for: THERMOSENSITIVE VARIANT PHE-68 AFFECTS ASSEMBLY.
[11]	"A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surface." Stoeffler-Meilicke M., Dabbs E.R., Albrecht-Ehrlich R., Stoeffler G. Eur. J. Biochem. 150:485-490(1985) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF A STRAIN MISSING S17 AND L29. Strain: AM111.
[12]	"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Arnold R.J., Reilly J.P. Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[13]	"Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. I. General properties of neaA mutants." Bollen A., Cabezon T., de Wilde M., Villarroel R., Herzog A. J. Mol. Biol. 99:795-806(1975) [PubMed] [Europe PMC] [Abstract] Cited for: ISOLATION, CHARACTERIZATION OF NEAMINE-RESISTANT VARIANT NEA301. Strain: K12S.
[14]	"Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant." Yaguchi M., Wittmann H.G., Cabezon T., DeWilde M., Villarroel R., Herzog A., Bollen A. J. Mol. Biol. 104:617-620(1976) [PubMed] [Europe PMC] [Abstract] Cited for: NEAMINE-RESISTANT VARIANT NEA301. Strain: K12S.
[15]	"All-atom homology model of the Escherichia coli 30S ribosomal subunit." Tung C.-S., Joseph S., Sanbonmatsu K.Y. Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[16]	"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement." Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J. Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[17]	"Structures of the bacterial ribosome at 3.5 A resolution." Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D. Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02613 Genomic DNA. Translation: CAA26469.1.
U18997 Genomic DNA. Translation: AAA58108.1.
U00096 Genomic DNA. Translation: AAC76336.1.
AP009048 Genomic DNA. Translation: BAE77980.1.
V00357 Genomic DNA. Translation: CAA23652.1.
X01563 Genomic DNA. Translation: CAA25714.1.

PIR

R3EC17. A37519.

RefSeq

NP_417770.1. NC_000913.2.
YP_492121.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EG0	electron microscopy	11.50	G	2-84	[»]
1M5G	model	-	Q	4-84	[»]
1P6G	electron microscopy	12.30	Q	2-84	[»]
1P87	electron microscopy	11.50	Q	2-84	[»]
1VS5	X-ray	3.46	Q	1-84	[»]
1VS7	X-ray	3.46	Q	1-84	[»]
2AVY	X-ray	3.46	Q	2-84	[»]
2AW7	X-ray	3.46	Q	2-84	[»]
2GY9	electron microscopy	15.00	Q	6-83	[»]
2GYB	electron microscopy	15.00	Q	6-83	[»]
2I2P	X-ray	3.22	Q	2-83	[»]
2I2U	X-ray	3.22	Q	2-83	[»]
2QAL	X-ray	3.21	Q	2-84	[»]
2QAN	X-ray	3.21	Q	2-84	[»]
2QB9	X-ray	3.54	Q	2-84	[»]
2QBB	X-ray	3.54	Q	2-84	[»]
2QBD	X-ray	3.30	Q	2-84	[»]
2QBF	X-ray	3.30	Q	2-84	[»]
2QBH	X-ray	4.00	Q	2-84	[»]
2QBJ	X-ray	4.00	Q	2-84	[»]
2QOU	X-ray	3.93	Q	2-84	[»]
2QOW	X-ray	3.93	Q	2-84	[»]
2QOY	X-ray	3.50	Q	2-84	[»]
2QP0	X-ray	3.50	Q	2-84	[»]
2WWL	electron microscopy	5.80	Q	4-83	[»]
2YKR	electron microscopy	9.80	Q	4-83	[»]
2Z4K	X-ray	4.45	Q	2-84	[»]
2Z4M	X-ray	4.45	Q	2-84	[»]
3E1A	electron microscopy	-	J	1-84	[»]
3E1C	electron microscopy	-	J	1-84	[»]
3FIH	electron microscopy	6.70	Q	4-83	[»]
3I1M	X-ray	3.19	Q	1-84	[»]
3I1O	X-ray	3.19	Q	1-84	[»]
3I1Q	X-ray	3.81	Q	1-84	[»]
3I1S	X-ray	3.81	Q	1-84	[»]
3I1Z	X-ray	3.71	Q	1-84	[»]
3I21	X-ray	3.71	Q	1-84	[»]
3IZV	electron microscopy	-	U	1-84	[»]
3IZW	electron microscopy	-	U	1-84	[»]
3J00	electron microscopy	-	Q	2-84	[»]
3J0U	electron microscopy	12.10	T	2-84	[»]
3J0V	electron microscopy	14.70	T	2-84	[»]
3J0X	electron microscopy	13.50	T	2-84	[»]
3J0Z	electron microscopy	11.50	T	2-84	[»]
3J10	electron microscopy	11.50	T	2-84	[»]
3J13	electron microscopy	13.10	S	2-84	[»]
3J18	electron microscopy	8.30	Q	4-83	[»]
3J36	electron microscopy	9.80	Q	2-84	[»]
3KC4	electron microscopy	-	Q	1-84	[»]
3OAQ	X-ray	3.25	Q	4-83	[»]
3OAR	X-ray	3.25	Q	4-83	[»]
3OFA	X-ray	3.19	Q	4-83	[»]
3OFB	X-ray	3.19	Q	4-83	[»]
3OFO	X-ray	3.10	Q	4-83	[»]
3OFP	X-ray	3.10	Q	4-83	[»]
3OFX	X-ray	3.29	Q	4-83	[»]
3OFY	X-ray	3.29	Q	4-83	[»]
3OR9	X-ray	3.30	Q	1-84	[»]
3ORA	X-ray	3.30	Q	1-84	[»]
3SFS	X-ray	3.20	Q	1-84	[»]
3UOQ	X-ray	3.70	Q	1-84	[»]
4A2I	electron microscopy	16.50	Q	4-83	[»]
4ADV	electron microscopy	13.50	Q	2-84	[»]
4GAQ	X-ray	3.30	Q	1-84	[»]
4GAS	X-ray	3.30	Q	1-84	[»]
4GD1	X-ray	3.00	Q	4-83	[»]
4GD2	X-ray	3.00	Q	4-83	[»]

ProteinModelPortal

P0AG63.

SMR

P0AG63. Positions 6-84.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47952N.

IntAct

P0AG63. 1 interaction.

STRING

511145.b3311.

Proteomic databases

PaxDb

P0AG63.

PRIDE

P0AG63.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.

GeneID

12934391.
947808.

KEGG

ecj:Y75_p3865.
eco:b3311.

PATRIC

32122054. VBIEscCol129921_3404.

Organism-specific databases

EchoBASE

EB0909.

EcoGene

EG10916. rpsQ.

Phylogenomic databases

eggNOG

COG0186.

HOGENOM

HOG000231339.

K02961.

OMA

TIRECRP.

ProtClustDB

PRK05610.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10916-MONOMER.
ECOL316407:JW3273-MONOMER.

Gene expression databases

Genevestigator

P0AG63.

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

P0AG63.

Entry information

Entry name

RS17_ECOLI

Accession

Primary (citable) accession number: P0AG63
Secondary accession number(s): P02373, Q2M6X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 78 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents