Reviewed, UniProtKB/Swiss-Prot P0A7J3 (RL10_ECOLI)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L10
Alternative name(s):
    50S ribosomal protein L8

Gene names

Name:	rplJ
Ordered Locus Names:	b3985, JW3948

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	165 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	Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA. HAMAP MF_00362
Subunit structure	Part of the 50S ribosomal subunit. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form a very strong complex (called L8). HAMAP MF_00362
Miscellaneous	Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10. HAMAP MF_00362
Sequence similarities	Belongs to the ribosomal protein L10P family.
Mass spectrometry	Molecular mass is 17581.1 Da from positions 2 - 165. Determined by MALDI. Ref.9

Ontologies

Keywords
Biological process	Translation regulation
Ligand	RNA-binding
Molecular function	Repressor Ribonucleoprotein Ribosomal protein
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW ribosome biogenesis Inferred from electronic annotation. Source: InterPro translation Inferred from electronic annotation. Source: HAMAP
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rpiB	P37351	1	EBI-546827,EBI-557460

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5 Ref.6 Ref.7
	Chain	2 – 165	164	50S ribosomal protein L10 HAMAP MF_00362		PRO_0000154627
Amino acid modifications
	Modified residue	37	1	N6-acetyllysine Ref.10
	Modified residue	105	1	N6-acetyllysine Ref.10
Experimental info
	Sequence conflict	84	1	Y → YR AA sequence Ref.5
	Sequence conflict	84	1	Y → YR AA sequence Ref.6
	Sequence conflict	84	1	Y → YR AA sequence Ref.7
	Sequence conflict	116	1	E → Q AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P0A7J3-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F15822B0EDB6AC02	FASTA	165	17,712
	10 20 30 40 50 60 MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV YMRVVRNTLL 70 80 90 100 110 120 RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA KANAKFEVKA AAFEGELIPA 130 140 150 160 SQIDRLATLP TYEEAIARLM ATMKEASAGK LVRTLAAVRD AKEAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli." Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P. Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed: 377281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"The ribosomal protein L8 is a complex L7/L12 and L10." Pettersson I., Hardy S.J.S., Liljas A. FEBS Lett. 64:135-138(1976) [PubMed: 773698] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-165. Strain: MRE-600.
[6]	"The primary structure of protein L10 from Escherichia coli ribosomes." Dovgas N.V., Vinokurov L.M., Velmoga I.S., Alakhov Y.B., Ovchinnikov Y.A. FEBS Lett. 67:58-61(1976) [PubMed: 782920] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-165, SEQUENCE REVISION. Strain: MRE-600.
[7]	"Primary structure of protein L10 from the large subunit of Escherichia coli ribosomes." Heiland I., Brauer D., Wittmann-Liebold B. Hoppe-Seyler's Z. Physiol. Chem. 357:1751-1770(1976) [PubMed: 797648] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-165. Strain: K12.
[8]	"Feedback regulation of the rplJL-rpoBC ribosomal protein operon of Escherichia coli requires a region of mRNA secondary structure." Climie S.C., Friesen J.D. J. Mol. Biol. 198:371-381(1987) [PubMed: 2448482] [Abstract] Cited for: MECHANISM OF TRANSLATION REGULATION.
[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]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-105, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	V00339 Genomic DNA. Translation: CAA23623.1. U00006 Genomic DNA. Translation: AAC43083.1. U00096 Genomic DNA. Translation: AAC76959.1. AP009048 Genomic DNA. Translation: BAE77335.1.
PIR	R5EC10. S12574.
RefSeq	AP_003834.1. NP_418412.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A7J3. 51 interactions.
STRING	P0A7J3.
Genome annotation databases
GeneID	948490.
GenomeReviews	Gene locus JW3948 in contig AP009048_GR. Gene locus b3985 in contig U00096_GR.
KEGG	ecj:JW3948. eco:b3985.
Organism-specific databases
EchoBASE	EB0864.
EcoGene	EG10871. rplJ.
CMR	Search...
Phylogenomic databases
HOGENOM	P0A7J3.
OMA	EYRGITV.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10871-MON.
Gene expression databases
Genevestigator	P0A7J3.
Family and domain databases
HAMAP	MF_00362. [Tree]
InterPro	IPR001790. Ribosomal_L10. IPR002363. Ribosomal_L10_eubac_CS. [Graphical view]
Pfam	PF00466. Ribosomal_L10. 1 hit. [Graphical view]
PROSITE	PS01109. RIBOSOMAL_L10. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RL10_ECOLI

Accession

Primary (citable) accession number: P0A7J3
Secondary accession number(s): P02408, Q2M8S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 42 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)