50S ribosomal protein L19 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A7K6 (RL19_ECOLI)

Last modified November 3, 2009. Version 50. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · 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 L19

Gene names

Name:	rplS
Ordered Locus Names:	b2606, JW2587

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	115 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (Ref.8) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (Ref.9) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation. HAMAP MF_00402
Subunit structure	Part of the 50S ribosomal subunit. Contacts L14 (Ref.6 and Ref.9). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Ref.8
Sequence similarities	Belongs to the ribosomal protein L19P family.
Mass spectrometry	Molecular mass is 13001.7 Da from positions 2 - 115. Determined by MALDI. Ref.7

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Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
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	protein binding Inferred from physical interaction. Source: IntAct rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
nanE	P0A761	1	EBI-543891,EBI-561432

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 115

114

50S ribosomal protein L19 HAMAP MF_00402

PRO_0000163451

Secondary structure

115

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A7K6-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7BD9F2EFB9DDB06B
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FASTA

115

13,133

        10         20         30         40         50         60 
MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI RNRGLHSAFT 

        70         80         90        100        110 
VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL RERTGKAARI KERLN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"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.
[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]	"Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes." Brosius J., Arfsten U. Biochemistry 17:508-516(1978) [PubMed: 339951] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-115.
[6]	"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli." Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G. Biochemistry 28:4099-4105(1989) [PubMed: 2665813] [Abstract] Cited for: CROSS-LINKING TO L14.
[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: 10094780] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[8]	"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.
[9]	"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

X01818 Genomic DNA. Translation: CAA25960.1.
U00096 Genomic DNA. Translation: AAC75655.1.
AP009048 Genomic DNA. Translation: BAA16491.1.

PIR

R5EC19. S07951.

RefSeq

AP_003187.1.
NP_417097.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	N	2-115	[»]
1P86	electron microscopy	11.50	N	2-115	[»]
1VS6	X-ray	3.46	P	2-114	[»]
1VS8	X-ray	3.46	P	1-115	[»]
2AW4	X-ray	3.46	P	2-115	[»]
2AWB	X-ray	3.46	P	2-115	[»]
2GYA	electron microscopy	15.00	N	2-114	[»]
2GYC	electron microscopy	15.00	N	2-115	[»]
2I2T	X-ray	3.22	P	2-114	[»]
2I2V	X-ray	3.22	P	2-114	[»]
2J28	electron microscopy	8.00	P	2-114	[»]
2QAM	X-ray	3.21	P	2-115	[»]
2QAO	X-ray	3.21	P	2-115	[»]
2QBA	X-ray	3.54	P	2-115	[»]
2QBC	X-ray	3.54	P	2-115	[»]
2QBE	X-ray	3.30	P	2-115	[»]
2QBG	X-ray	3.30	P	2-115	[»]
2QBI	X-ray	4.00	P	2-115	[»]
2QBK	X-ray	4.00	P	2-115	[»]
2QOV	X-ray	3.93	P	2-115	[»]
2QOX	X-ray	3.93	P	2-115	[»]
2QOZ	X-ray	3.50	P	2-115	[»]
2QP1	X-ray	3.50	P	2-115	[»]
2RDO	electron microscopy	9.10	P	2-115	[»]
2VHM	X-ray	3.74	P	2-115	[»]
2VHN	X-ray	3.74	P	2-115	[»]
2Z4L	X-ray	4.45	P	2-115	[»]
2Z4N	X-ray	4.45	P	2-115	[»]
3BBX	electron microscopy	10.00	P	2-115	[»]
3DF2	X-ray	3.50	P	2-114	[»]
3DF4	X-ray	3.50	P	2-114	[»]
3E1B	electron microscopy	-	I	1-115	[»]
3E1D	electron microscopy	-	I	1-115	[»]
3FIK	electron microscopy	6.70	P	2-115	[»]
3I1N	X-ray	3.19	P	1-115	[»]
3I1P	X-ray	3.19	P	1-115	[»]
3I1R	X-ray	3.81	P	1-115	[»]
3I1T	X-ray	3.81	P	1-115	[»]
3I20	X-ray	3.71	P	1-115	[»]
3I22	X-ray	3.71	P	1-115	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7K6. 100 interactions.

STRING

P0A7K6.

PTM databases

PhosSite

P0A7K6.

Proteomic databases

PRIDE

P0A7K6.

Genome annotation databases

GeneID

947096.

GenomeReviews

Gene locus JW2587 in contig AP009048_GR.
Gene locus b2606 in contig U00096_GR.

KEGG

ecj:JW2587.
eco:b2606.

Organism-specific databases

EchoBASE

EB0873.

EcoGene

EG10880. rplS.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A7K6.

OMA

GERTRVQ.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10880-MON.

Gene expression databases

Genevestigator

P0A7K6.

Family and domain databases

HAMAP

MF_00402.
[Tree]

InterPro

IPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
[Graphical view]

PANTHER

PTHR15680. Ribosomal_L19. 1 hit.

Pfam

PF01245. Ribosomal_L19. 1 hit.
[Graphical view]

PRINTS

PR00061. RIBOSOMALL19.

ProDom

PD002979. Ribosomal_L19. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01024. rplS_bact. 1 hit.

PROSITE

PS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

RL19_ECOLI

Accession

Primary (citable) accession number: P0A7K6
Secondary accession number(s): P02420

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 50 of the entry and version 2 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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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents