30S ribosomal protein S18 - Escherichia coli (strain K12)

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P0A7T7 (RS18_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. 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 S18

Gene names

Name:	rpsR
Ordered Locus Names:	b4202, JW4160

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	75 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	Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. HAMAP-Rule MF_00270
Subunit structure	Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6.
Sequence similarities	Belongs to the ribosomal protein S18P family.
Mass spectrometry	Molecular mass is 8897.0 Da from positions 2 - 75. Determined by MALDI. Ref.7

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
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

Removed Ref.5

Chain

2 – 75

30S ribosomal protein S18 HAMAP-Rule MF_00270

PRO_0000111153

Amino acid modifications

Modified residue

N-acetylalanine HAMAP-Rule MF_00270

Experimental info

Sequence conflict

K → E AA sequence Ref.5

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7T7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AB2E8288901B73B8
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FASTA

8,986

        10         20         30         40         50         60 
MARYFRRRKF CRFTAEGVQE IDYKDIATLK NYITESGKIV PSRITGTRAK YQRQLARAIK 

        70 
RARYLSLLPY TDRHQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame." Schnier J., Kitakawa M., Isono K. Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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.
[5]	"Primary structure of protein S18 from the small Escherichia coli ribosomal subunit." Yaguchi M. FEBS Lett. 59:217-220(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-75. Strain: K.
[6]	"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 31-38, CROSS-LINKING TO RRNA. Strain: MRE-600.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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

X04022 Genomic DNA. Translation: CAA27654.1.
U14003 Genomic DNA. Translation: AAA97098.1.
U00096 Genomic DNA. Translation: AAC77159.1.
AP009048 Genomic DNA. Translation: BAE78203.1.

PIR

R3EC18. S56427.

RefSeq

NP_418623.1. NC_000913.2.
YP_492344.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	R	5-75	[»]
1P6G	electron microscopy	12.30	R	2-75	[»]
1P87	electron microscopy	11.50	R	2-75	[»]
1VS5	X-ray	3.46	R	1-75	[»]
1VS7	X-ray	3.46	R	1-75	[»]
2AVY	X-ray	3.46	R	2-75	[»]
2AW7	X-ray	3.46	R	2-75	[»]
2GY9	electron microscopy	15.00	R	7-74	[»]
2GYB	electron microscopy	15.00	R	7-74	[»]
2I2P	X-ray	3.22	R	2-74	[»]
2I2U	X-ray	3.22	R	2-74	[»]
2QAL	X-ray	3.21	R	2-75	[»]
2QAN	X-ray	3.21	R	2-75	[»]
2QB9	X-ray	3.54	R	2-75	[»]
2QBB	X-ray	3.54	R	2-75	[»]
2QBD	X-ray	3.30	R	2-75	[»]
2QBF	X-ray	3.30	R	2-75	[»]
2QBH	X-ray	4.00	R	2-75	[»]
2QBJ	X-ray	4.00	R	2-75	[»]
2QOU	X-ray	3.93	R	2-75	[»]
2QOW	X-ray	3.93	R	2-75	[»]
2QOY	X-ray	3.50	R	2-75	[»]
2QP0	X-ray	3.50	R	2-75	[»]
2VHO	X-ray	3.74	R	2-75	[»]
2VHP	X-ray	3.74	R	2-75	[»]
2WWL	electron microscopy	5.80	R	20-74	[»]
2YKR	electron microscopy	9.80	R	20-74	[»]
2Z4K	X-ray	4.45	R	2-75	[»]
2Z4M	X-ray	4.45	R	2-75	[»]
3DF1	X-ray	3.50	R	2-74	[»]
3DF3	X-ray	3.50	R	2-74	[»]
3E1A	electron microscopy	-	K	1-75	[»]
3E1C	electron microscopy	-	K	1-75	[»]
3FIH	electron microscopy	6.70	R	20-74	[»]
3I1M	X-ray	3.19	R	1-75	[»]
3I1O	X-ray	3.19	R	1-75	[»]
3I1Q	X-ray	3.81	R	1-75	[»]
3I1S	X-ray	3.81	R	1-75	[»]
3I1Z	X-ray	3.71	R	1-75	[»]
3I21	X-ray	3.71	R	1-75	[»]
3IZV	electron microscopy	-	V	1-75	[»]
3IZW	electron microscopy	-	V	1-75	[»]
3J00	electron microscopy	-	R	2-75	[»]
3J0U	electron microscopy	12.10	U	2-75	[»]
3J0V	electron microscopy	14.70	U	2-75	[»]
3J0X	electron microscopy	13.50	U	2-75	[»]
3J0Z	electron microscopy	11.50	U	2-75	[»]
3J10	electron microscopy	11.50	U	2-75	[»]
3J13	electron microscopy	13.10	T	2-75	[»]
3J18	electron microscopy	8.30	R	20-74	[»]
3KC4	electron microscopy	-	R	1-75	[»]
3OAQ	X-ray	3.25	R	20-74	[»]
3OAR	X-ray	3.25	R	20-74	[»]
3OFA	X-ray	3.19	R	20-74	[»]
3OFB	X-ray	3.19	R	20-74	[»]
3OFO	X-ray	3.10	R	20-74	[»]
3OFP	X-ray	3.10	R	20-74	[»]
3OFX	X-ray	3.29	R	20-74	[»]
3OFY	X-ray	3.29	R	20-74	[»]
3OR9	X-ray	3.30	R	1-75	[»]
3ORA	X-ray	3.30	R	1-75	[»]
3SFS	X-ray	3.20	R	1-75	[»]
3UOQ	X-ray	3.70	R	1-75	[»]
4A2I	electron microscopy	16.50	R	20-74	[»]
4ADV	electron microscopy	13.50	R	2-75	[»]
4GAQ	X-ray	3.30	R	1-75	[»]
4GAS	X-ray	3.30	R	1-75	[»]
4GD1	X-ray	3.00	R	20-74	[»]
4GD2	X-ray	3.00	R	20-74	[»]

ProteinModelPortal

P0A7T7.

SMR

P0A7T7. Positions 2-75.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47889N.

IntAct

P0A7T7. 24 interactions.

MINT

MINT-1247424.

STRING

511145.b4202.

Proteomic databases

PaxDb

P0A7T7.

PRIDE

P0A7T7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77159; AAC77159; b4202.
BAE78203; BAE78203; BAE78203.

GeneID

12930640.
948721.

KEGG

ecj:Y75_p4088.
eco:b4202.

PATRIC

32123979. VBIEscCol129921_4334.

Organism-specific databases

EchoBASE

EB0910.

EcoGene

EG10917. rpsR.

Phylogenomic databases

eggNOG

COG0238.

HOGENOM

HOG000218466.

K02963.

OMA

RRRYCRF.

ProtClustDB

PRK00391.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10917-MONOMER.
ECOL316407:JW4160-MONOMER.

Gene expression databases

Genevestigator

P0A7T7.

Family and domain databases

Gene3D

4.10.640.10. 1 hit.

HAMAP

MF_00270. Ribosomal_S18.

InterPro

IPR001648. Ribosomal_S18.
IPR018275. Ribosomal_S18_CS.
[Graphical view]

PANTHER

PTHR13479. PTHR13479. 1 hit.

Pfam

PF01084. Ribosomal_S18. 1 hit.
[Graphical view]

PRINTS

PR00974. RIBOSOMALS18.

ProDom

PD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF46911. Ribosomal_S18. 1 hit.

TIGRFAMs

TIGR00165. S18. 1 hit.

PROSITE

PS00057. RIBOSOMAL_S18. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7T7.

Entry information

Entry name

RS18_ECOLI

Accession

Primary (citable) accession number: P0A7T7
Secondary accession number(s): P02374, Q2M6A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 86 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

Amino acid modifications

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