P0ADY3 (RL14_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L14

Gene names

Name:	rplN
Ordered Locus Names:	b3310, JW3272

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	123 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (Ref.11) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (Ref.12) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8. Ref.9 Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation. Ref.9
Subunit structure	Part of the 50S ribosomal subunit. Contacts L19 (Ref.7 and Ref.12). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association. Ref.11
Sequence similarities	Belongs to the ribosomal protein L14P family.
Mass spectrometry	Molecular mass is 13540.2 Da from positions 1 - 123. Determined by MALDI. Ref.8

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay PubMed 4922286. Source: EcoCyc
Molecular_function	LSU rRNA binding Inferred from direct assay Ref.6. Source: EcoCyc structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 123

123

50S ribosomal protein L14 HAMAP-Rule MF_01367

PRO_0000128540

Experimental info

Mutagenesis

97

1

T → A: Reduced RsfS binding. Ref.9

Mutagenesis

98

1

R → A: Reduced RsfS binding. Ref.9

Mutagenesis

114

1

K → A: Reduced RsfS binding. Ref.9

Mutagenesis

117

1

S → A: No change in RsfS binding. Ref.9

Sequence conflict

63

1

Missing AA sequence Ref.1

Sequence conflict

84

1

C → S AA sequence Ref.1

Sequence conflict

90 – 91

2

NS → TD AA sequence Ref.1

Sequence conflict

97

1

Missing AA sequence Ref.1

Sequence conflict

115

1

I → L AA sequence Ref.1

Sequence conflict

123

1

Missing AA sequence Ref.1

Secondary structure

1

.

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123

Helix Strand Turn

Details...

Beta strand

7 – 10

4

Beta strand

15 – 24

10

Beta strand

26 – 29

4

Beta strand

38 – 46

9

Beta strand

50 – 52

3

Beta strand

57 – 64

8

Beta strand

69 – 71

3

Beta strand

72 – 74

3

Beta strand

76 – 81

6

Beta strand

83 – 88

6

Turn

89 – 91

3

Beta strand

92 – 95

4

Beta strand

97 – 99

3

Helix

105 – 108

4

Helix

110 – 112

3

Helix

113 – 117

5

Beta strand

118 – 120

3

Sequences

	Sequence		Length	Mass (Da)
	P0ADY3 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 192ACB1623979510	FASTA	123	13,541
	10 20 30 40 50 60 MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG KVKKGDVLKA 70 80 90 100 110 120 VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF GPVTRELRSE KFMKIISLAP EVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of protein L14 isolated from Escherichia coli ribosomes." Morinaga T., Funatsu G., Funatsu M., Wittmann-Liebold B., Wittmann H.G. FEBS Lett. 91:74-77(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene." Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M. Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[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]	"DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli." Post L.E., Arfsten A.E., Reusser F., Nomura M. Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. Strain: K12.
[6]	"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-28, CROSS-LINKING TO RRNA. Strain: MRE-600.
[7]	"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] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO L19.
[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] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[9]	"RsfA (YbeB) proteins are conserved ribosomal silencing factors." Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F., Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T., Diefenbacher M.E., Nierhaus K.H., Uetz P. PLoS Genet. 8:E1002815-E1002815(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RSFS, MUTAGENESIS OF THR-97; ARG-98; LYS-114 AND SER-117. Strain: K12 / MG1655 / ATCC 47076.
[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]	"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), INTERSUBUNIT BRIDGE FORMATION.
[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] [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

X01563 Genomic DNA. Translation: CAA25715.1.
U18997 Genomic DNA. Translation: AAA58107.1.
U00096 Genomic DNA. Translation: AAC76335.1.
AP009048 Genomic DNA. Translation: BAE77981.1.
V00357 Genomic DNA. Translation: CAA23653.1.

PIR

R5EC14. A65124.

RefSeq

NP_417769.1. NC_000913.2.
YP_492122.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ML5	electron microscopy	14.00	n	1-122	[»]
1P85	electron microscopy	12.30	I	1-123	[»]
1P86	electron microscopy	11.50	I	1-123	[»]
1VS6	X-ray	3.46	K	1-123	[»]
1VS8	X-ray	3.46	K	1-123	[»]
1VT2	X-ray	3.30	K	1-123	[»]
2AW4	X-ray	3.46	K	1-123	[»]
2AWB	X-ray	3.46	K	1-123	[»]
2GYA	electron microscopy	15.00	I	2-123	[»]
2GYC	electron microscopy	15.00	I	2-123	[»]
2I2T	X-ray	3.22	K	1-123	[»]
2I2V	X-ray	3.22	K	1-123	[»]
2J28	electron microscopy	8.00	K	2-122	[»]
2QAM	X-ray	3.21	K	1-123	[»]
2QAO	X-ray	3.21	K	1-123	[»]
2QBA	X-ray	3.54	K	1-123	[»]
2QBC	X-ray	3.54	K	1-123	[»]
2QBE	X-ray	3.30	K	1-123	[»]
2QBG	X-ray	3.30	K	1-123	[»]
2QBI	X-ray	4.00	K	1-123	[»]
2QBK	X-ray	4.00	K	1-123	[»]
2QOV	X-ray	3.93	K	1-123	[»]
2QOX	X-ray	3.93	K	1-123	[»]
2QOZ	X-ray	3.50	K	1-123	[»]
2QP1	X-ray	3.50	K	1-123	[»]
2RDO	electron microscopy	9.10	K	1-123	[»]
2WWQ	electron microscopy	5.80	K	1-121	[»]
2Z4L	X-ray	4.45	K	1-123	[»]
2Z4N	X-ray	4.45	K	1-123	[»]
3BBX	electron microscopy	10.00	K	1-123	[»]
3E1B	electron microscopy	-	D	1-123	[»]
3E1D	electron microscopy	-	D	1-123	[»]
3FIK	electron microscopy	6.70	K	2-122	[»]
3I1N	X-ray	3.19	K	1-123	[»]
3I1P	X-ray	3.19	K	1-123	[»]
3I1R	X-ray	3.81	K	1-123	[»]
3I1T	X-ray	3.81	K	1-123	[»]
3I20	X-ray	3.71	K	1-123	[»]
3I22	X-ray	3.71	K	1-123	[»]
3IZT	electron microscopy	-	L	1-123	[»]
3IZU	electron microscopy	-	L	1-123	[»]
3J01	electron microscopy	-	K	1-123	[»]
3J0T	electron microscopy	12.10	M	1-123	[»]
3J0W	electron microscopy	14.70	M	1-123	[»]
3J0Y	electron microscopy	13.50	M	1-123	[»]
3J11	electron microscopy	13.10	M	1-123	[»]
3J12	electron microscopy	11.50	M	1-123	[»]
3J14	electron microscopy	11.50	M	1-123	[»]
3J19	electron microscopy	8.30	K	1-122	[»]
3KCR	electron microscopy	-	K	1-123	[»]
3OAS	X-ray	3.25	K	1-122	[»]
3OAT	X-ray	3.25	K	1-122	[»]
3OFC	X-ray	3.19	K	1-122	[»]
3OFD	X-ray	3.19	K	1-122	[»]
3OFQ	X-ray	3.10	K	1-122	[»]
3OFR	X-ray	3.10	K	1-122	[»]
3OFZ	X-ray	3.29	K	1-122	[»]
3OG0	X-ray	3.29	K	1-122	[»]
3ORB	X-ray	3.30	K	1-123	[»]
3R8S	X-ray	3.00	K	1-122	[»]
3R8T	X-ray	3.00	K	1-122	[»]
3SGF	X-ray	3.20	O	1-123	[»]
3UOS	X-ray	3.70	O	1-123	[»]
487D	electron microscopy	7.50	M	1-122	[»]
4GAR	X-ray	3.30	K	1-123	[»]
4GAU	X-ray	3.30	K	1-123	[»]

ProteinModelPortal

P0ADY3.

SMR

P0ADY3. Positions 2-123.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35798N.

IntAct

P0ADY3. 49 interactions.

MINT

MINT-1304553.

STRING

511145.b3310.

Proteomic databases

PaxDb

P0ADY3.

PRIDE

P0ADY3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76335; AAC76335; b3310.
BAE77981; BAE77981; BAE77981.

GeneID

12934392.
947809.

KEGG

ecj:Y75_p3866.
eco:b3310.

PATRIC

32122052. VBIEscCol129921_3403.

Organism-specific databases

EchoBASE

EB0868.

EcoGene

EG10875. rplN.

Phylogenomic databases

eggNOG

COG0093.

HOGENOM

HOG000183702.

KO

K02874.

OMA

KQFMKIV.

ProtClustDB

PRK05483.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10875-MONOMER.
ECOL316407:JW3272-MONOMER.

Gene expression databases

Genevestigator

P0ADY3.

Family and domain databases

Gene3D

2.40.150.20. 1 hit.

HAMAP

MF_01367_B. Ribosomal_L14_B.

InterPro

IPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]

PANTHER

PTHR11761. PTHR11761. 1 hit.
PTHR11761:SF3. PTHR11761:SF3. 1 hit.

Pfam

PF00238. Ribosomal_L14. 1 hit.
[Graphical view]

SUPFAM

SSF50193. Ribosomal_L14. 1 hit.

TIGRFAMs

TIGR01067. rplN_bact. 1 hit.

PROSITE

PS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ADY3.

Entry information

Entry name

RL14_ECOLI

Accession

Primary (citable) accession number: P0ADY3
Secondary accession number(s): P02411, Q2M6X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program