50S ribosomal protein L16 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0ADY7 (RL16_ECOLI)

Last modified November 3, 2009. Version 42. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
50S ribosomal protein L16

Gene names

Name:	rplP
Ordered Locus Names:	b3313, JW3275

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood. HAMAP MF_01342
Subunit structure	Part of the 50S ribosomal subunit. Cross-links to the A and P site tRNAs. Ref.6
Sequence similarities	Belongs to the ribosomal protein L16P family.
Mass spectrometry	Molecular mass is 15326.2 Da from positions 1 - 136. Determined by MALDI. Ref.8

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Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing
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: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 136

136

50S ribosomal protein L16 HAMAP MF_01342

PRO_0000062101

Amino acid modifications

Modified residue

N-methylmethionine HAMAP MF_01342

Modified residue

Arginine derivative HAMAP MF_01342

Secondary structure

136

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0ADY7-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 445A9B167F7564D1
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FASTA

136

15,281

        10         20         30         40         50         60 
MLQPKRTKFR KMHKGRNRGL AQGTDVSFGS FGLKAVGRGR LTARQIEAAR RAMTRAVKRQ 

        70         80         90        100        110        120 
GKIWIRVFPD KPITEKPLAV RMGKGKGNVE YWVALIQPGK VLYEMDGVPE ELAREAFKLA 

       130 
AAKLPIKTTF VTKTVM

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes." Brosius J., Chen R. FEBS Lett. 68:105-109(1976) [PubMed: 786730] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed: 3892488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli." Post L.E., Arfsten A.E., Davis G.R., Nomura M. J. Biol. Chem. 255:4653-4659(1980) [PubMed: 6154696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-80.
[6]	"Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes." Herold M., Nierhaus K.H. J. Biol. Chem. 262:8826-8833(1987) [PubMed: 3298242] [Abstract] Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT. Strain: K12.
[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]	"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.
[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: 12809609] [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: 16272117] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES. Strain: MRE-600.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X02613 Genomic DNA. Translation: CAA26467.1.
U18997 Genomic DNA. Translation: AAA58110.1.
U00096 Genomic DNA. Translation: AAC76338.1.
AP009048 Genomic DNA. Translation: BAE77978.1.
M12490 Genomic DNA. Translation: AAA83901.1.

PIR

R5EC16. I23129.

RefSeq

AP_004477.1.
NP_417772.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	K	1-136	[»]
1P86	electron microscopy	11.50	K	1-136	[»]
1VS6	X-ray	3.46	M	1-136	[»]
1VS8	X-ray	3.46	M	1-136	[»]
2AW4	X-ray	3.46	M	1-136	[»]
2AWB	X-ray	3.46	M	1-136	[»]
2GYA	electron microscopy	15.00	K	3-133	[»]
2GYC	electron microscopy	15.00	K	3-133	[»]
2I2T	X-ray	3.22	M	1-136	[»]
2I2V	X-ray	3.22	M	1-136	[»]
2J28	electron microscopy	8.00	M	1-136	[»]
2QAM	X-ray	3.21	M	1-136	[»]
2QAO	X-ray	3.21	M	1-136	[»]
2QBA	X-ray	3.54	M	1-136	[»]
2QBC	X-ray	3.54	M	1-136	[»]
2QBE	X-ray	3.30	M	1-136	[»]
2QBG	X-ray	3.30	M	1-136	[»]
2QBI	X-ray	4.00	M	1-136	[»]
2QBK	X-ray	4.00	M	1-136	[»]
2QOV	X-ray	3.93	M	1-136	[»]
2QOX	X-ray	3.93	M	1-136	[»]
2QOZ	X-ray	3.50	M	1-136	[»]
2QP1	X-ray	3.50	M	1-136	[»]
2RDO	electron microscopy	9.10	M	1-136	[»]
2VHM	X-ray	3.74	M	1-136	[»]
2VHN	X-ray	3.74	M	1-136	[»]
2Z4L	X-ray	4.45	M	1-136	[»]
2Z4N	X-ray	4.45	M	1-136	[»]
3BBX	electron microscopy	10.00	M	1-136	[»]
3E1B	electron microscopy	-	F	1-136	[»]
3E1D	electron microscopy	-	F	1-136	[»]
3FIK	electron microscopy	6.70	M	1-136	[»]
3I1N	X-ray	3.19	M	1-136	[»]
3I1P	X-ray	3.19	M	1-136	[»]
3I1R	X-ray	3.81	M	1-136	[»]
3I1T	X-ray	3.81	M	1-136	[»]
3I20	X-ray	3.71	M	1-136	[»]
3I22	X-ray	3.71	M	1-136	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0ADY7.

PTM databases

PhosSite

P0ADY7.

Proteomic databases

PRIDE

P0ADY7.

Genome annotation databases

GeneID

947806.

GenomeReviews

Gene locus JW3275 in contig AP009048_GR.
Gene locus b3313 in contig U00096_GR.

KEGG

ecj:JW3275.
eco:b3313.

Organism-specific databases

EchoBASE

EB0870.

EcoGene

EG10877. rplP.

CMR

Search...

Phylogenomic databases

HOGENOM

P0ADY7.

OMA

KGSPEFW.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10877-MON.

Gene expression databases

Genevestigator

P0ADY7.

Family and domain databases

HAMAP

MF_01342.
[Tree]

InterPro

IPR016180. Ribosomal_L10e/L16.
IPR000114. Ribosomal_L16.
[Graphical view]

PANTHER

PTHR12220. Ribosomal_L16. 1 hit.

Pfam

PF00252. Ribosomal_L16. 1 hit.
[Graphical view]

PRINTS

PR00060. RIBOSOMALL16.

TIGRFAMs

TIGR01164. rplP_bact. 1 hit.

PROSITE

PS00586. RIBOSOMAL_L16_1. 1 hit.
PS00701. RIBOSOMAL_L16_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

RL16_ECOLI

Accession

Primary (citable) accession number: P0ADY7
Secondary accession number(s): P02414, Q2M6X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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