P0AG44 (RL17_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L17

Gene names

Name:	rplQ
Ordered Locus Names:	b3294, JW3256

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	127 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Requires L15 for assembly into the 50S subunit. HAMAP MF_01368
Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L32. Ref.6
Sequence similarities	Belongs to the ribosomal protein L17P family.
Mass spectrometry	Molecular mass is 14364.7 Da from positions 1 - 127. Determined by MALDI. Ref.8

Ontologies

Keywords
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: InterPro
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 127

127

50S ribosomal protein L17 HAMAP MF_01368

PRO_0000175524

Secondary structure

1

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127

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Turn

14 – 16

3

Helix

17 – 30

14

Helix

38 – 52

15

Helix

62 – 64

3

Turn

67 – 69

3

Beta strand

70 – 73

4

Helix

74 – 81

8

Helix

83 – 86

4

Beta strand

104 – 106

3

Beta strand

116 – 118

3

Sequences

	Sequence		Length	Mass (Da)
	P0AG44 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D96DF17C07013A11	FASTA	127	14,365
	10 20 30 40 50 60 MRHRKSGRQL NRNSSHRQAM FRNMAGSLVR HEIIKTTLPK AKELRRVVEP LITLAKTDSV 70 80 90 100 110 120 ANRRLAFART RDNEIVAKLF NELGPRFASR AGGYTRILKC GFRAGDNAPM AYIELVDRSE KAEAAAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of protein L17 from the Escherichia coli ribosome." Rombauts W., Feytons V., Wittmann-Liebold B. FEBS Lett. 149:320-327(1982) Cited for: PROTEIN SEQUENCE.
[2]	"Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?" Meek D.W., Hayward R.S. Nucleic Acids Res. 12:5813-5821(1984) [PubMed: 6379605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli." Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L. Nucleic Acids Res. 13:3891-3903(1985) [PubMed: 2989779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"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.
[5]	"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.
[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]	"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 L32.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02543 Genomic DNA. Translation: CAA26396.1.
J01685 Genomic DNA. Translation: AAA24578.1.
X00766 Genomic DNA. Translation: CAA25338.1.
U18997 Genomic DNA. Translation: AAA58091.1.
U00096 Genomic DNA. Translation: AAC76319.1.
AP009048 Genomic DNA. Translation: BAE77997.1.

PIR

R5EC17. B22884.

RefSeq

NP_417753.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	L	1-127	[»]
1P86	electron microscopy	11.50	L	1-127	[»]
1VS6	X-ray	3.46	N	1-127	[»]
1VS8	X-ray	3.46	N	1-127	[»]
1VT2	X-ray	3.30	N	1-127	[»]
2AW4	X-ray	3.46	N	1-127	[»]
2AWB	X-ray	3.46	N	1-127	[»]
2GYA	electron microscopy	15.00	L	3-116	[»]
2GYC	electron microscopy	15.00	L	3-116	[»]
2I2T	X-ray	3.22	N	1-127	[»]
2I2V	X-ray	3.22	N	1-127	[»]
2J28	electron microscopy	8.00	N	1-127	[»]
2QAM	X-ray	3.21	N	1-127	[»]
2QAO	X-ray	3.21	N	1-127	[»]
2QBA	X-ray	3.54	N	1-127	[»]
2QBC	X-ray	3.54	N	1-127	[»]
2QBE	X-ray	3.30	N	1-127	[»]
2QBG	X-ray	3.30	N	1-127	[»]
2QBI	X-ray	4.00	N	1-127	[»]
2QBK	X-ray	4.00	N	1-127	[»]
2QOV	X-ray	3.93	N	1-127	[»]
2QOX	X-ray	3.93	N	1-127	[»]
2QOZ	X-ray	3.50	N	1-127	[»]
2QP1	X-ray	3.50	N	1-127	[»]
2RDO	electron microscopy	9.10	N	1-127	[»]
2WWQ	electron microscopy	5.80	N	1-120	[»]
2Z4L	X-ray	4.45	N	1-127	[»]
2Z4N	X-ray	4.45	N	1-127	[»]
3BBX	electron microscopy	10.00	N	1-127	[»]
3E1B	electron microscopy	-	G	1-127	[»]
3E1D	electron microscopy	-	G	1-127	[»]
3FIK	electron microscopy	6.70	N	1-120	[»]
3I1N	X-ray	3.19	N	1-127	[»]
3I1P	X-ray	3.19	N	1-127	[»]
3I1R	X-ray	3.81	N	1-127	[»]
3I1T	X-ray	3.81	N	1-127	[»]
3I20	X-ray	3.71	N	1-127	[»]
3I22	X-ray	3.71	N	1-127	[»]
3IZT	electron microscopy	-	O	1-127	[»]
3IZU	electron microscopy	-	O	1-127	[»]
3J01	electron microscopy	-	N	1-127	[»]
3KCR	electron microscopy	-	N	1-127	[»]
3OAS	X-ray	3.25	N	1-120	[»]
3OAT	X-ray	3.25	N	1-120	[»]
3OFC	X-ray	3.19	N	1-120	[»]
3OFD	X-ray	3.19	N	1-120	[»]
3OFQ	X-ray	3.10	N	1-120	[»]
3OFR	X-ray	3.10	N	1-120	[»]
3OFZ	X-ray	3.29	N	1-120	[»]
3OG0	X-ray	3.29	N	1-120	[»]
3ORB	X-ray	3.30	N	1-127	[»]
3R8S	X-ray	3.00	N	1-120	[»]
3R8T	X-ray	3.00	N	1-120	[»]

ProteinModelPortal

P0AG44.

SMR

P0AG44. Positions 1-127.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35801N.

IntAct

P0AG44. 135 interactions.

MINT

MINT-1251899.

2D gel databases

ECO2DBASE

I014.9. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001152; EBESCP00000001152; EBESCG00000000949.
EBESCT00000015807; EBESCP00000015098; EBESCG00000014867.

GeneID

947784.

GenomeReviews

Gene locus JW3256 in contig AP009048_GR.
Gene locus b3294 in contig U00096_GR.

KEGG

ecj:JW3256.
eco:b3294.

PATRIC

32122020. VBIEscCol129921_3387.

Organism-specific databases

EchoBASE

EB0871.

EcoGene

EG10878. rplQ.

Phylogenomic databases

eggNOG

COG0203.

GeneTree

EBGT00050000009822.

HOGENOM

HBG704211.

OMA

FSELGPR.

PhylomeDB

P0AG44.

ProtClustDB

PRK05591.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10878-MONOMER.

Gene expression databases

Genevestigator

P0AG44.

Family and domain databases

HAMAP

MF_01368. Ribosomal_L17.
[Tree]

InterPro

IPR000456. Ribosomal_L17.
[Graphical view]

Gene3D

G3DSA:3.90.1030.10. Ribosomal_L17. 1 hit.

KO

K02879.

PANTHER

PTHR14413. Ribosomal_L17. 1 hit.

Pfam

PF01196. Ribosomal_L17. 1 hit.
[Graphical view]

SUPFAM

SSF64263. Ribosomal_L17. 1 hit.

TIGRFAMs

TIGR00059. L17. 1 hit.

PROSITE

PS01167. RIBOSOMAL_L17. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL17_ECOLI

Accession

Primary (citable) accession number: P0AG44
Secondary accession number(s): P02416, Q2M6V9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program