P0A7J7 (RL11_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L11

Gene names

Name:	rplK
Synonyms:	relC
Ordered Locus Names:	b3983, JW3946

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	142 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	This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors. HAMAP-Rule MF_00736_B
Subunit structure	Part of the 50S ribosomal subunit.
Sequence similarities	Belongs to the ribosomal protein L11P family.
Mass spectrometry	Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. Ref.9

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	stringent response Inferred from direct assay PubMed 17095013. Source: EcoCyc translational termination Inferred from mutant phenotype PubMed 16556224. Source: EcoCyc
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay Ref.5. Source: EcoCyc
Molecular_function	rRNA binding Inferred from direct assay PubMed 6271782. Source: EcoCyc structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
prmA	P0A8T1	3	EBI-547288,EBI-556300

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 142

141

50S ribosomal protein L11 HAMAP-Rule MF_00736_B

PRO_0000104283

Amino acid modifications

Modified residue

2

1

N,N,N-trimethylalanine HAMAP-Rule MF_00736_B

Modified residue

4

1

N6,N6,N6-trimethyllysine HAMAP-Rule MF_00736_B

Modified residue

40

1

N6,N6,N6-trimethyllysine HAMAP-Rule MF_00736_B

Modified residue

72

1

N6-succinyllysine Ref.11

Modified residue

81

1

N6-succinyllysine Ref.11

Secondary structure

1

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142

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

9 – 13

5

Beta strand

15 – 19

5

Turn

21 – 24

4

Beta strand

28 – 32

5

Beta strand

35 – 37

3

Turn

38 – 40

3

Turn

42 – 45

4

Helix

46 – 49

4

Beta strand

51 – 53

3

Beta strand

55 – 61

7

Beta strand

62 – 66

5

Beta strand

67 – 71

5

Turn

78 – 81

4

Beta strand

82 – 85

4

Beta strand

87 – 89

3

Turn

93 – 95

3

Beta strand

99 – 101

3

Beta strand

102 – 104

3

Turn

108 – 110

3

Helix

111 – 113

3

Beta strand

114 – 117

4

Turn

122 – 128

7

Turn

130 – 132

3

Beta strand

133 – 136

4

Beta strand

138 – 141

4

Sequences

	Sequence		Length	Mass (Da)
	P0A7J7 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: C49226BB2462BE0F	FASTA	142	14,875
	10 20 30 40 50 60 MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT 70 80 90 100 110 120 VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK ISRAQLQEIA QTKAADMTGA 130 140 DIEAMTRSIE GTARSMGLVV ED

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes." Dognin M.J., Wittmann-Liebold B. Eur. J. Biochem. 112:131-151(1980) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142. Strain: K12.
[6]	"Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon." Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P. J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[7]	"Structural properties of ribosomal protein L11 from Escherichia coli." Choli T. Biochem. Int. 19:1323-1338(1989) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURAL STUDIES.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[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] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[10]	"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution." Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R. J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[11]	"Identification of lysine succinylation as a new post-translational modification." Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y. Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-72 AND LYS-81. Strain: K12.
[12]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[13]	"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] [Europe PMC] [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

V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.

PIR

R5EC11. S12572.

RefSeq

NP_418410.1. NC_000913.2.
YP_491478.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EG0	electron microscopy	11.50	K	1-140	[»]
1MJ1	electron microscopy	13.00	L	1-141	[»]
1ML5	electron microscopy	14.00	l	1-141	[»]
1P85	electron microscopy	12.30	G	2-142	[»]
1P86	electron microscopy	11.50	G	2-142	[»]
1VS6	X-ray	3.46	I	1-142	[»]
1VS8	X-ray	3.46	I	1-142	[»]
1VT2	X-ray	3.30	I	1-142	[»]
2AW4	X-ray	3.46	I	2-142	[»]
2AWB	X-ray	3.46	I	2-142	[»]
2GYA	electron microscopy	15.00	G	3-140	[»]
2GYC	electron microscopy	15.00	G	3-141	[»]
2I2T	X-ray	3.22	I	2-141	[»]
2I2V	X-ray	3.22	I	2-141	[»]
2J28	electron microscopy	8.00	I	2-142	[»]
2QAM	X-ray	3.21	I	2-142	[»]
2QAO	X-ray	3.21	I	2-142	[»]
2QBA	X-ray	3.54	I	2-142	[»]
2QBC	X-ray	3.54	I	2-142	[»]
2QBE	X-ray	3.30	I	2-142	[»]
2QBG	X-ray	3.30	I	2-142	[»]
2QBI	X-ray	4.00	I	2-142	[»]
2QBK	X-ray	4.00	I	2-142	[»]
2QOV	X-ray	3.93	I	2-142	[»]
2QOX	X-ray	3.93	I	2-142	[»]
2QOZ	X-ray	3.50	I	2-142	[»]
2QP1	X-ray	3.50	I	2-142	[»]
2RDO	electron microscopy	9.10	I	2-142	[»]
2VHM	X-ray	3.74	I	2-142	[»]
2VHN	X-ray	3.74	I	2-142	[»]
2WWQ	electron microscopy	5.80	I	2-142	[»]
2Z4L	X-ray	4.45	I	2-142	[»]
2Z4N	X-ray	4.45	I	2-142	[»]
3DEG	electron microscopy	-	H	2-142	[»]
3DF2	X-ray	3.50	I	2-141	[»]
3DF4	X-ray	3.50	I	2-141	[»]
3E1B	electron microscopy	-	5	1-142	[»]
3E1D	electron microscopy	-	5	1-142	[»]
3EP2	electron microscopy	-	I	2-142	[»]
3EQ3	electron microscopy	-	I	2-142	[»]
3EQ4	electron microscopy	-	I	2-142	[»]
3FIK	electron microscopy	6.70	I	2-142	[»]
3I1N	X-ray	3.19	I	1-142	[»]
3I1P	X-ray	3.19	I	1-142	[»]
3I1R	X-ray	3.81	I	1-142	[»]
3I1T	X-ray	3.81	I	1-142	[»]
3I20	X-ray	3.71	I	1-142	[»]
3I22	X-ray	3.71	I	1-142	[»]
3IZT	electron microscopy	-	J	1-142	[»]
3IZU	electron microscopy	-	J	1-142	[»]
3J01	electron microscopy	-	I	2-142	[»]
3J0D	electron microscopy	11.10	G	2-142	[»]
3J0T	electron microscopy	12.10	K	2-141	[»]
3J0W	electron microscopy	14.70	K	2-141	[»]
3J0Y	electron microscopy	13.50	K	2-141	[»]
3J11	electron microscopy	13.10	K	2-141	[»]
3J12	electron microscopy	11.50	K	2-141	[»]
3J14	electron microscopy	11.50	K	2-141	[»]
3J19	electron microscopy	8.30	I	2-142	[»]
3KCR	electron microscopy	-	I	1-142	[»]
3OAS	X-ray	3.25	I	2-142	[»]
3OAT	X-ray	3.25	I	2-142	[»]
3OFC	X-ray	3.19	I	2-142	[»]
3OFD	X-ray	3.19	I	2-142	[»]
3OFQ	X-ray	3.10	I	2-142	[»]
3OFR	X-ray	3.10	I	2-142	[»]
3OFZ	X-ray	3.29	I	2-142	[»]
3OG0	X-ray	3.29	I	2-142	[»]
3ORB	X-ray	3.30	I	1-142	[»]
3R8S	X-ray	3.00	I	2-142	[»]
3R8T	X-ray	3.00	I	2-142	[»]
3SGF	X-ray	3.20	I	1-142	[»]
3UOS	X-ray	3.70	I	1-142	[»]
487D	electron microscopy	7.50	L	10-86	[»]
4GAR	X-ray	3.30	I	1-142	[»]
4GAU	X-ray	3.30	I	1-142	[»]

ProteinModelPortal

P0A7J7.

SMR

P0A7J7. Positions 3-141.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35882N.

IntAct

P0A7J7. 44 interactions.

MINT

MINT-1232893.

STRING

511145.b3983.

Proteomic databases

PaxDb

P0A7J7.

PRIDE

P0A7J7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.

GeneID

12930523.
948484.

KEGG

ecj:Y75_p3214.
eco:b3983.

PATRIC

32123487. VBIEscCol129921_4096.

Organism-specific databases

EchoBASE

EB0865.

EcoGene

EG10872. rplK.

Phylogenomic databases

eggNOG

COG0080.

HOGENOM

HOG000082123.

KO

K02867.

OMA

KQFNAKT.

ProtClustDB

PRK00140.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Gene expression databases

Genevestigator

P0A7J7.

Family and domain databases

Gene3D

1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.

HAMAP

MF_00736_B. Ribosomal_L11_B.

InterPro

IPR000911. Ribosomal_L11.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]

PANTHER

PTHR11661. PTHR11661. 1 hit.

Pfam

PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]

SMART

SM00649. RL11. 1 hit.
[Graphical view]

SUPFAM

SSF46906. Ribosomal_L11. 1 hit.
SSF54747. Ribosomal_L11. 1 hit.

TIGRFAMs

TIGR01632. L11_bact. 1 hit.

PROSITE

PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7J7.

Entry information

Entry name

RL11_ECOLI

Accession

Primary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program