30S ribosomal protein S16 - Escherichia coli (strain K12)

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P0A7T3 (RS16_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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 S16

Gene names

Name:	rpsP
Ordered Locus Names:	b2609, JW2590

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	82 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. Ref.6 In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes. Ref.6
Induction	Part of the rpsP-rimM-trmD-rplS operon. HAMAP MF_00385
Sequence similarities	Belongs to the ribosomal protein S16P family.
Mass spectrometry	Molecular mass is 9190.5 Da from positions 1 - 82. Determined by MALDI. Ref.9

Ontologies

Keywords
Molecular function	Endonuclease Hydrolase Nuclease Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ribosomal small subunit assembly Inferred from direct assay. Source: EcoCyc translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay. Source: EcoCyc
Molecular function	endodeoxyribonuclease activity Inferred from direct assay Ref.6. Source: EcoCyc structural constituent of ribosome Inferred from direct assay. Source: EcoliWiki structure-specific DNA binding Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 82

30S ribosomal protein S16 HAMAP MF_00385

PRO_0000167184

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7T3 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F94D07049A6D489D
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FASTA

9,191

        10         20         30         40         50         60 
MVTIRLARHG AKKRPFYQVV VADSRNARNG RFIERVGFFN PIASEKEEGT RLDLDRIAHW 

        70         80 
VGQGATISDR VAALIKEVNK AA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence of protein S16 from Escherichia coli." Vandekerckhove J., Rombauts W., Wittmann-Liebold B. Hoppe-Seyler's Z. Physiol. Chem. 358:989-1002(1977) [PubMed: 336510] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide." Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R. EMBO J. 2:899-905(1983) [PubMed: 6357787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE. Strain: K12.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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.
[5]	"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], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The Escherichia coli ribosomal protein S16 is an endonuclease." Oberto J., Bonnefoy E., Mouay E., Pellegrini O., Wilkstroem P.M., Rouviere-Yaniv J. Mol. Microbiol. 19:1319-1330(1996) [PubMed: 8730873] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION AS AN ENDONUCLEASE.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[8]	"Hybrid protein between ribosomal protein S16 and RimM of Escherichia coli retains the ribosome maturation function of both proteins." Loevgren J.M., Wikstroem P.M. J. Bacteriol. 183:5352-5357(2001) [PubMed: 11514519] [Abstract] Cited for: FUSION WITH RIBOSOME MATURATION FACTOR RIMM. Strain: MW100.
[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

X01818 Genomic DNA. Translation: CAA25958.1.
U00096 Genomic DNA. Translation: AAC75658.1.
AP009048 Genomic DNA. Translation: BAA16494.2.

PIR

R3EC16. S07948.

RefSeq

NP_417100.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5G	model	-	P	1-82	[»]
1P6G	electron microscopy	12.30	P	1-82	[»]
1P87	electron microscopy	11.50	P	1-82	[»]
1VS5	X-ray	3.46	P	1-82	[»]
1VS7	X-ray	3.46	P	1-82	[»]
2AVY	X-ray	3.46	P	1-82	[»]
2AW7	X-ray	3.46	P	1-82	[»]
2GY9	electron microscopy	15.00	P	1-78	[»]
2GYB	electron microscopy	15.00	P	1-78	[»]
2I2P	X-ray	3.22	P	1-82	[»]
2I2U	X-ray	3.22	P	1-82	[»]
2QAL	X-ray	3.21	P	1-82	[»]
2QAN	X-ray	3.21	P	1-82	[»]
2QB9	X-ray	3.54	P	1-82	[»]
2QBB	X-ray	3.54	P	1-82	[»]
2QBD	X-ray	3.30	P	1-82	[»]
2QBF	X-ray	3.30	P	1-82	[»]
2QBH	X-ray	4.00	P	1-82	[»]
2QBJ	X-ray	4.00	P	1-82	[»]
2QOU	X-ray	3.93	P	1-82	[»]
2QOW	X-ray	3.93	P	1-82	[»]
2QOY	X-ray	3.50	P	1-82	[»]
2QP0	X-ray	3.50	P	1-82	[»]
2VHO	X-ray	3.74	P	1-82	[»]
2VHP	X-ray	3.74	P	1-82	[»]
2WWL	electron microscopy	5.80	P	1-80	[»]
2YKR	electron microscopy	9.80	P	1-82	[»]
2Z4K	X-ray	4.45	P	1-82	[»]
2Z4M	X-ray	4.45	P	1-82	[»]
3DF1	X-ray	3.50	P	1-82	[»]
3DF3	X-ray	3.50	P	1-82	[»]
3E1A	electron microscopy	-	I	1-82	[»]
3E1C	electron microscopy	-	I	1-82	[»]
3FIH	electron microscopy	6.70	P	1-80	[»]
3I1M	X-ray	3.19	P	1-82	[»]
3I1O	X-ray	3.19	P	1-82	[»]
3I1Q	X-ray	3.81	P	1-82	[»]
3I1S	X-ray	3.81	P	1-82	[»]
3I1Z	X-ray	3.71	P	1-82	[»]
3I21	X-ray	3.71	P	1-82	[»]
3IZV	electron microscopy	-	T	1-82	[»]
3IZW	electron microscopy	-	T	1-82	[»]
3J00	electron microscopy	-	P	1-82	[»]
3KC4	electron microscopy	-	P	1-82	[»]
3OAQ	X-ray	3.25	P	1-82	[»]
3OAR	X-ray	3.25	P	1-80	[»]
3OFA	X-ray	3.19	P	1-82	[»]
3OFB	X-ray	3.19	P	1-80	[»]
3OFO	X-ray	3.10	P	1-82	[»]
3OFP	X-ray	3.10	P	1-80	[»]
3OFX	X-ray	3.29	P	1-82	[»]
3OFY	X-ray	3.29	P	1-80	[»]
3OR9	X-ray	3.30	P	1-82	[»]
3ORA	X-ray	3.30	P	1-82	[»]
3R8N	X-ray	3.00	P	1-82	[»]
3R8O	X-ray	3.00	P	1-82	[»]
4A2I	electron microscopy	16.50	P	1-82	[»]

ProteinModelPortal

P0A7T3.

SMR

P0A7T3. Positions 1-82.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47829N.

IntAct

P0A7T3. 55 interactions.

MINT

MINT-1280042.

2D gel databases

ECO2DBASE

I011.9. 6TH EDITION.

Proteomic databases

PRIDE

P0A7T3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001904; EBESCP00000001904; EBESCG00000001564.
EBESCT00000014322; EBESCP00000013613; EBESCG00000013384.

GeneID

947103.

GenomeReviews

Gene locus JW2590 in contig AP009048_GR.
Gene locus b2609 in contig U00096_GR.

KEGG

ecj:JW2590.
eco:b2609.

PATRIC

32120617. VBIEscCol129921_2707.

Organism-specific databases

EchoBASE

EB0908.

EcoGene

EG10915. rpsP.

Phylogenomic databases

eggNOG

COG0228.

GeneTree

EBGT00050000011206.

HOGENOM

HBG410188.

OMA

SKAGVMK.

PhylomeDB

P0A7T3.

ProtClustDB

PRK00040.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10915-MONOMER.

Gene expression databases

Genevestigator

P0A7T3.

Family and domain databases

HAMAP

MF_00385. Ribosomal_S16.
[Tree]

InterPro

IPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view]

Gene3D

G3DSA:3.30.1320.10. Ribosomal_S16. 1 hit.

K02959.

PANTHER

PTHR12919. Ribosomal_S16. 1 hit.

Pfam

PF00886. Ribosomal_S16. 1 hit.
[Graphical view]

SUPFAM

SSF54565. Ribosomal_S16. 1 hit.

TIGRFAMs

TIGR00002. S16. 1 hit.

PROSITE

PS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RS16_ECOLI

Accession

Primary (citable) accession number: P0A7T3
Secondary accession number(s): P02372, P77006

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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

Entry information

Relevant documents