30S ribosomal protein S15 - Escherichia coli (strain K12)

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P0ADZ4 (RS15_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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 S15

Gene names

Name:	rpsO
Synonyms:	secC
Ordered Locus Names:	b3165, JW3134

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	89 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 of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA. HAMAP MF_01343_B In the E.coli 70S ribosome it has been modeled (Ref.11) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (Ref.12) there are minor differences between side-chain conformations. HAMAP MF_01343_B
Subunit structure	Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA. Ref.11 Ref.12
Sequence similarities	Belongs to the ribosomal protein S15P family.
Mass spectrometry	Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. Ref.9

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 direct assay. Source: EcoliWiki
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay. Source: EcoliWiki
Molecular function	rRNA binding Inferred from direct assay. Source: EcoliWiki structural constituent of ribosome Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 89

30S ribosomal protein S15 HAMAP MF_01343_B

PRO_0000115437

Experimental info

Sequence conflict

Missing Ref.3

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ADZ4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AABDDA6674B99B1C
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FASTA

10,269

        10         20         30         40         50         60 
MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH HSRRGLLRMV 

        70         80 
SQRRKLLDYL KRKDVARYTQ LIERLGLRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO)." Takata R., Mukai T., Aoyagi M., Hori K. Mol. Gen. Genet. 197:225-229(1984) [PubMed: 6394953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions." Portier C., Regnier P. Nucleic Acids Res. 12:6091-6102(1984) [PubMed: 6382163] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli." Evans S., Dennis P.P. Gene 40:15-22(1985) [PubMed: 3005122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1." Regnier P., Grunberg-Manago M., Portier C. J. Biol. Chem. 262:63-68(1987) [PubMed: 2432069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	"Primary structure of the 16S rRNA binding protein S15 from Escherichia coli ribosomes." Morinaga T., Funatsu G., Funatsu M., Wittmann H.G. FEBS Lett. 64:307-309(1976) [PubMed: 776686] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-89. Strain: K.
[8]	"The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping." Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B. Nucleic Acids Res. 16:10803-10816(1988) [PubMed: 2849753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[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), INTERSUBUNIT BRIDGE FORMATION. 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 INCLUDING THE INTERSUBUNIT BRIDGE. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01073 Genomic DNA. Translation: CAA25536.1.
X00761 Genomic DNA. Translation: CAA25331.1.
M14425 Genomic DNA. Translation: AAA24595.1.
J02638 Genomic DNA. Translation: AAA83904.1.
U18997 Genomic DNA. Translation: AAA57968.1.
U00096 Genomic DNA. Translation: AAC76199.1.
AP009048 Genomic DNA. Translation: BAE77211.1.
X13775 Genomic DNA. Translation: CAA32022.1.

PIR

R3EC15. B26118.

RefSeq

NP_417634.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P6G	electron microscopy	12.30	O	2-89	[»]
1P87	electron microscopy	11.50	O	2-89	[»]
2AVY	X-ray	3.46	O	1-89	[»]
2AW7	X-ray	3.46	O	1-89	[»]
2GY9	electron microscopy	15.00	O	3-87	[»]
2GYB	electron microscopy	15.00	O	3-87	[»]
2QAL	X-ray	3.21	O	1-89	[»]
2QAN	X-ray	3.21	O	1-89	[»]
2QB9	X-ray	3.54	O	1-89	[»]
2QBB	X-ray	3.54	O	1-89	[»]
2QBD	X-ray	3.30	O	1-89	[»]
2QBF	X-ray	3.30	O	1-89	[»]
2QBH	X-ray	4.00	O	1-89	[»]
2QBJ	X-ray	4.00	O	1-89	[»]
2QOU	X-ray	3.93	O	1-89	[»]
2QOW	X-ray	3.93	O	1-89	[»]
2QOY	X-ray	3.50	O	1-89	[»]
2QP0	X-ray	3.50	O	1-89	[»]
2VAZ	electron microscopy	10.00	F	2-88	[»]
2WWL	electron microscopy	5.80	O	2-89	[»]
2Z4K	X-ray	4.45	O	1-89	[»]
2Z4M	X-ray	4.45	O	1-89	[»]
3DF1	X-ray	3.50	O	1-89	[»]
3DF3	X-ray	3.50	O	1-89	[»]
3FIH	electron microscopy	6.70	O	2-89	[»]
3I1M	X-ray	3.19	O	1-89	[»]
3I1O	X-ray	3.19	O	1-89	[»]
3I1Q	X-ray	3.81	O	1-89	[»]
3I1S	X-ray	3.81	O	1-89	[»]
3I1Z	X-ray	3.71	O	1-89	[»]
3I21	X-ray	3.71	O	1-89	[»]
3IZV	electron microscopy	-	S	1-89	[»]
3IZW	electron microscopy	-	S	1-89	[»]
3J00	electron microscopy	-	O	2-89	[»]
3KC4	electron microscopy	-	O	1-89	[»]
3OAQ	X-ray	3.25	O	2-89	[»]
3OAR	X-ray	3.25	O	2-89	[»]
3OFA	X-ray	3.19	O	2-89	[»]
3OFB	X-ray	3.19	O	2-89	[»]
3OFO	X-ray	3.10	O	2-89	[»]
3OFP	X-ray	3.10	O	2-89	[»]
3OFX	X-ray	3.29	O	2-89	[»]
3OFY	X-ray	3.29	O	2-89	[»]
3OR9	X-ray	3.30	O	1-89	[»]
3ORA	X-ray	3.30	O	1-89	[»]
3R8N	X-ray	3.00	O	2-89	[»]
3R8O	X-ray	3.00	O	2-89	[»]
4A2I	electron microscopy	16.50	O	2-89	[»]

ProteinModelPortal

P0ADZ4.

SMR

P0ADZ4. Positions 3-88.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47909N.

IntAct

P0ADZ4. 28 interactions.

MINT

MINT-1299353.

2D gel databases

ECO2DBASE

I012.0. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001882; EBESCP00000001882; EBESCG00000001548.
EBESCT00000001883; EBESCP00000001883; EBESCG00000001548.
EBESCT00000001884; EBESCP00000001884; EBESCG00000001548.
EBESCT00000001885; EBESCP00000001885; EBESCG00000001548.
EBESCT00000016345; EBESCP00000015636; EBESCG00000015405.

GeneID

947686.

GenomeReviews

Gene locus JW3134 in contig AP009048_GR.
Gene locus b3165 in contig U00096_GR.

KEGG

ecj:JW3134.
eco:b3165.

PATRIC

32121748. VBIEscCol129921_3260.

Organism-specific databases

EchoBASE

EB0907.

EcoGene

EG10914. rpsO.

Phylogenomic databases

eggNOG

COG0184.

GeneTree

EBGT00050000011791.

HOGENOM

HBG500000.

OMA

TYLRNKD.

PhylomeDB

P0ADZ4.

ProtClustDB

PRK05626.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10914-MONOMER.

Gene expression databases

Genevestigator

P0ADZ4.

Family and domain databases

HAMAP

MF_01343_B. Ribosomal_S15_S13e_B.
[Tree]

InterPro

IPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.287.10. S15_NS1_RNA_bd. 1 hit.

K02956.

Pfam

PF00312. Ribosomal_S15. 1 hit.
[Graphical view]

SUPFAM

SSF47060. S15/NS1_bind. 1 hit.

TIGRFAMs

TIGR00952. S15_bact. 1 hit.

PROSITE

PS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RS15_ECOLI

Accession

Primary (citable) accession number: P0ADZ4
Secondary accession number(s): P02371, Q2M945

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 63 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

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents