P0A7X3 (RS9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
30S ribosomal protein S9

Gene names

Name:	rpsI
Ordered Locus Names:	b3230, JW3199

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	130 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	The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome. Ref.8
Subunit structure	Part of the 30S ribosomal subunit. Cross-links to the P site tRNA and weakly to the A site tRNA.
Sequence similarities	Belongs to the ribosomal protein S9P family.
Mass spectrometry	Molecular mass is 14723.3 Da from positions 2 - 130. Determined by MALDI. Ref.9

Ontologies

Keywords
Ligand	RNA-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 direct assay. Source: EcoliWiki
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	structural constituent of ribosome Inferred from direct assay. Source: EcoliWiki 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

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 130

129

30S ribosomal protein S9 HAMAP MF_00532_B

PRO_0000111354

Experimental info

Mutagenesis

105 – 130

26

Missing: Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro.

Mutagenesis

128 – 130

3

Missing: Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro.

Sequence conflict

56

1

D → N AA sequence Ref.4

Sequence conflict

124

1

Missing AA sequence Ref.4

Sequence conflict

126

1

Q → E AA sequence Ref.4

Secondary structure

1

.

.

.

.

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.

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.

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.

.

130

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

19 – 24

6

Beta strand

28 – 34

7

Helix

35 – 39

5

Beta strand

40 – 44

5

Helix

50 – 54

5

Beta strand

58 – 65

8

Helix

72 – 90

19

Helix

95 – 101

7

Beta strand

118 – 120

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7X3 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 757D599168812806	FASTA	130	14,856
	10 20 30 40 50 60 MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ PLELVDMVEK 70 80 90 100 110 120 LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK AGFVTRDARQ VERKKVGLRK 130 ARRRPQFSKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli." Isono S., Thamm S., Kitakawa M., Isono K. Mol. Gen. Genet. 198:279-282(1985) [PubMed: 3884974] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The primary structure of protein S9 from the 30S subunit of Escherichia coli ribosomes." Chen R., Wittmann-Liebold B. FEBS Lett. 52:139-140(1975) [PubMed: 1091515] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-130. Strain: K.
[5]	"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: 7556101] [Abstract] Cited for: PROTEIN SEQUENCE OF 121-130, CROSS-LINKING TO RRNA. Strain: MRE-600.
[6]	"Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G." Marsh R.C., Parmeggiani A. Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973) [PubMed: 4346030] [Abstract] Cited for: INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX. Strain: B/2.
[7]	"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site." Osswald M., Doering T., Brimacombe R. Nucleic Acids Res. 23:4635-4641(1995) [PubMed: 8524654] [Abstract] Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD. Strain: MRE-600.
[8]	"Creating ribosomes with an all-RNA 30S subunit P site." Hoang L., Fredrick K., Noller H.F. Proc. Natl. Acad. Sci. U.S.A. 101:12439-12443(2004) [PubMed: 15308780] [Abstract] Cited for: ROLE IN P SITE TRNA BINDING, MUTAGENESIS. Strain: CSH142.
[9]	"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: 10094780] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[10]	"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: 12244297] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[11]	"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: 12809609] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[12]	"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: 16272117] [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

X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.

PIR

R3EC9. H65114.

RefSeq

NP_417697.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	I	4-130	[»]
1P6G	electron microscopy	12.30	I	2-130	[»]
1P87	electron microscopy	11.50	I	2-130	[»]
1VS5	X-ray	3.46	I	1-130	[»]
1VS7	X-ray	3.46	I	1-130	[»]
2AVY	X-ray	3.46	I	2-130	[»]
2AW7	X-ray	3.46	I	2-130	[»]
2GY9	electron microscopy	15.00	I	5-129	[»]
2GYB	electron microscopy	15.00	I	5-129	[»]
2I2P	X-ray	3.22	I	2-129	[»]
2I2U	X-ray	3.22	I	2-129	[»]
2QAL	X-ray	3.21	I	2-130	[»]
2QAN	X-ray	3.21	I	2-130	[»]
2QB9	X-ray	3.54	I	2-130	[»]
2QBB	X-ray	3.54	I	2-130	[»]
2QBD	X-ray	3.30	I	2-130	[»]
2QBF	X-ray	3.30	I	2-130	[»]
2QBH	X-ray	4.00	I	2-130	[»]
2QBJ	X-ray	4.00	I	2-130	[»]
2QOU	X-ray	3.93	I	2-130	[»]
2QOW	X-ray	3.93	I	2-130	[»]
2QOY	X-ray	3.50	I	2-130	[»]
2QP0	X-ray	3.50	I	2-130	[»]
2VHO	X-ray	3.74	I	2-130	[»]
2VHP	X-ray	3.74	I	2-130	[»]
2WWL	electron microscopy	5.80	I	4-130	[»]
2YKR	electron microscopy	9.80	I	4-130	[»]
2Z4K	X-ray	4.45	I	2-130	[»]
2Z4M	X-ray	4.45	I	2-130	[»]
3DF1	X-ray	3.50	I	2-129	[»]
3DF3	X-ray	3.50	I	2-129	[»]
3E1A	electron microscopy	-	W	1-130	[»]
3E1C	electron microscopy	-	W	1-130	[»]
3FIH	electron microscopy	6.70	I	4-130	[»]
3I1M	X-ray	3.19	I	1-130	[»]
3I1O	X-ray	3.19	I	1-130	[»]
3I1Q	X-ray	3.81	I	1-130	[»]
3I1S	X-ray	3.81	I	1-130	[»]
3I1Z	X-ray	3.71	I	1-130	[»]
3I21	X-ray	3.71	I	1-130	[»]
3IZV	electron microscopy	-	M	1-130	[»]
3IZW	electron microscopy	-	M	1-130	[»]
3J00	electron microscopy	-	I	2-130	[»]
3KC4	electron microscopy	-	I	1-130	[»]
3OAQ	X-ray	3.25	I	4-130	[»]
3OAR	X-ray	3.25	I	4-130	[»]
3OFA	X-ray	3.19	I	4-130	[»]
3OFB	X-ray	3.19	I	4-130	[»]
3OFO	X-ray	3.10	I	4-130	[»]
3OFP	X-ray	3.10	I	4-130	[»]
3OFX	X-ray	3.29	I	4-130	[»]
3OFY	X-ray	3.29	I	4-130	[»]
3OR9	X-ray	3.30	I	1-130	[»]
3ORA	X-ray	3.30	I	1-130	[»]
3R8N	X-ray	3.00	I	4-130	[»]
3R8O	X-ray	3.00	I	4-130	[»]
4A2I	electron microscopy	16.50	I	4-130	[»]

ProteinModelPortal

P0A7X3.

SMR

P0A7X3. Positions 4-130.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35799N.

IntAct

P0A7X3. 147 interactions.

MINT

MINT-1290939.

2D gel databases

ECO2DBASE

I014.6. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000423; EBESCP00000000423; EBESCG00000000350.
EBESCT00000018245; EBESCP00000017536; EBESCG00000017300.

GeneID

949000.

GenomeReviews

Gene locus JW3199 in contig AP009048_GR.
Gene locus b3230 in contig U00096_GR.

KEGG

ecj:JW3199.
eco:b3230.

PATRIC

32121886. VBIEscCol129921_3327.

Organism-specific databases

EchoBASE

EB0901.

EcoGene

EG10908. rpsI.

Phylogenomic databases

eggNOG

COG0103.

GeneTree

EBGT00050000011362.

HOGENOM

HBG518785.

OMA

IKQGAAR.

PhylomeDB

P0A7X3.

ProtClustDB

PRK00132.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10908-MONOMER.

Gene expression databases

Genevestigator

P0A7X3.

Family and domain databases

HAMAP

MF_00532_B. Ribosomal_S9_B.
[Tree]

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]

Gene3D

G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

KO

K02996.

PANTHER

PTHR21569. Ribosomal_S9. 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

DrugBank

DB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.
DB00759. Tetracycline.
DB00560. Tigecycline.

Entry information

Entry name

RS9_ECOLI

Accession

Primary (citable) accession number: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program