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Protein

50S ribosomal protein L17

Gene

rplQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Requires L15 for assembly into the 50S subunit.

GO - Molecular functioni

  1. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10878-MONOMER.
ECOL316407:JW3256-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L17UniRule annotation
Gene namesi
Name:rplQUniRule annotation
Ordered Locus Names:b3294, JW3256
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10878. rplQ.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12712750S ribosomal protein L17PRO_0000175524Add
BLAST

Proteomic databases

PaxDbiP0AG44.
PRIDEiP0AG44.

Expressioni

Gene expression databases

GenevestigatoriP0AG44.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L32.

Protein-protein interaction databases

DIPiDIP-35801N.
IntActiP0AG44. 135 interactions.
MINTiMINT-1251899.
STRINGi511145.b3294.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi14 – 3118Combined sources
Beta strandi32 – 376Combined sources
Helixi38 – 5518Combined sources
Helixi60 – 689Combined sources
Helixi73 – 819Combined sources
Helixi83 – 864Combined sources
Turni87 – 893Combined sources
Beta strandi95 – 1028Combined sources
Turni104 – 1063Combined sources
Beta strandi109 – 1168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30L1-127[»]
1P86electron microscopy11.50L1-127[»]
1VS6X-ray3.46N1-127[»]
1VS8X-ray3.46N1-127[»]
1VT2X-ray3.30N1-127[»]
2AW4X-ray3.46N1-127[»]
2AWBX-ray3.46N1-127[»]
2GYAelectron microscopy15.00L3-116[»]
2GYCelectron microscopy15.00L3-116[»]
2I2TX-ray3.22N1-127[»]
2I2VX-ray3.22N1-127[»]
2J28electron microscopy8.00N1-127[»]
2QAMX-ray3.21N1-127[»]
2QAOX-ray3.21N1-127[»]
2QBAX-ray3.54N1-127[»]
2QBCX-ray3.54N1-127[»]
2QBEX-ray3.30N1-127[»]
2QBGX-ray3.30N1-127[»]
2QBIX-ray4.00N1-127[»]
2QBKX-ray4.00N1-127[»]
2QOVX-ray3.93N1-127[»]
2QOXX-ray3.93N1-127[»]
2QOZX-ray3.50N1-127[»]
2QP1X-ray3.50N1-127[»]
2RDOelectron microscopy9.10N1-127[»]
2WWQelectron microscopy5.80N1-120[»]
2Z4LX-ray4.45N1-127[»]
2Z4NX-ray4.45N1-127[»]
3BBXelectron microscopy10.00N1-127[»]
3E1Belectron microscopy-G1-127[»]
3E1Delectron microscopy-G1-127[»]
3FIKelectron microscopy6.70N1-120[»]
3I1NX-ray3.19N1-127[»]
3I1PX-ray3.19N1-127[»]
3I1RX-ray3.81N1-127[»]
3I1TX-ray3.81N1-127[»]
3I20X-ray3.71N1-127[»]
3I22X-ray3.71N1-127[»]
3IZTelectron microscopy-O1-127[»]
3IZUelectron microscopy-O1-127[»]
3J01electron microscopy-N1-127[»]
3J0Telectron microscopy12.10P1-127[»]
3J0Welectron microscopy14.70P1-127[»]
3J0Yelectron microscopy13.50P1-127[»]
3J11electron microscopy13.10P1-127[»]
3J12electron microscopy11.50P1-127[»]
3J14electron microscopy11.50P1-127[»]
3J19electron microscopy8.30N1-120[»]
3J37electron microscopy9.80R1-127[»]
3J4Xelectron microscopy12.00N1-120[»]
3J50electron microscopy20.00N1-120[»]
3J51electron microscopy17.00N1-120[»]
3J52electron microscopy12.00N1-120[»]
3J54electron microscopy13.00N1-120[»]
3J56electron microscopy15.00N1-120[»]
3J58electron microscopy17.00N1-120[»]
3J5Aelectron microscopy12.00N1-120[»]
3J5Celectron microscopy17.00N1-120[»]
3J5Eelectron microscopy17.00N1-120[»]
3J5Gelectron microscopy20.00N1-120[»]
3J5Ielectron microscopy15.00N1-120[»]
3J5Kelectron microscopy9.00N1-120[»]
3J5Lelectron microscopy6.60N1-120[»]
3J5Oelectron microscopy6.80N1-127[»]
3J5Uelectron microscopy7.60P1-127[»]
3J5Welectron microscopy7.60Q1-127[»]
3J7Zelectron microscopy3.90N1-127[»]
3KCRelectron microscopy-N1-127[»]
3OASX-ray3.25N1-120[»]
3OATX-ray3.25N1-120[»]
3OFCX-ray3.19N1-120[»]
3OFDX-ray3.19N1-120[»]
3OFQX-ray3.10N1-120[»]
3OFRX-ray3.10N1-120[»]
3OFZX-ray3.29N1-120[»]
3OG0X-ray3.29N1-120[»]
3ORBX-ray3.30N1-127[»]
3R8SX-ray3.00N1-120[»]
3R8TX-ray3.00N1-120[»]
3SGFX-ray3.20R1-127[»]
3UOSX-ray3.70R1-127[»]
4CSUelectron microscopy5.50N1-127[»]
4GARX-ray3.30N1-127[»]
4GAUX-ray3.30N1-127[»]
4KIXX-ray2.90N1-127[»]
4KIZX-ray2.90N1-127[»]
4KJ1X-ray2.90N1-127[»]
4KJ3X-ray2.90N1-127[»]
4KJ5X-ray2.90N1-127[»]
4KJ7X-ray2.90N1-127[»]
4KJ9X-ray2.90N1-127[»]
4KJBX-ray2.90N1-127[»]
4PEBX-ray2.95N1-120[»]
4PECX-ray2.95N1-120[»]
4TOMX-ray3.00N1-120[»]
4TOOX-ray3.00N1-120[»]
4TOVX-ray2.90N1-120[»]
4TOXX-ray2.90N1-120[»]
4TP1X-ray2.90N1-120[»]
4TP3X-ray2.90N1-120[»]
4TP5X-ray2.90N1-120[»]
4TP7X-ray2.90N1-120[»]
4TP9X-ray2.80N1-120[»]
4TPBX-ray2.80N1-120[»]
4TPDX-ray2.80N1-120[»]
4TPFX-ray2.80N1-120[»]
4WAPX-ray3.09N1-120[»]
4WARX-ray3.09N1-120[»]
ProteinModelPortaliP0AG44.
SMRiP0AG44. Positions 1-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG44.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L17P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0203.
HOGENOMiHOG000019780.
InParanoidiP0AG44.
KOiK02879.
OMAiRVVEPMI.
OrthoDBiEOG6GR3GR.
PhylomeDBiP0AG44.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.
PROSITEiPS01167. RIBOSOMAL_L17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AG44-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRHRKSGRQL NRNSSHRQAM FRNMAGSLVR HEIIKTTLPK AKELRRVVEP
60 70 80 90 100
LITLAKTDSV ANRRLAFART RDNEIVAKLF NELGPRFASR AGGYTRILKC
110 120
GFRAGDNAPM AYIELVDRSE KAEAAAE
Length:127
Mass (Da):14,365
Last modified:July 21, 1986 - v1
Checksum:iD96DF17C07013A11
GO

Mass spectrometryi

Molecular mass is 14364.7 Da from positions 1 - 127. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB22884. R5EC17.
RefSeqiNP_417753.1. NC_000913.3.
YP_492138.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76319; AAC76319; b3294.
BAE77997; BAE77997; BAE77997.
GeneIDi12934436.
947784.
KEGGiecj:Y75_p3882.
eco:b3294.
PATRICi32122020. VBIEscCol129921_3387.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB22884. R5EC17.
RefSeqiNP_417753.1. NC_000913.3.
YP_492138.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30L1-127[»]
1P86electron microscopy11.50L1-127[»]
1VS6X-ray3.46N1-127[»]
1VS8X-ray3.46N1-127[»]
1VT2X-ray3.30N1-127[»]
2AW4X-ray3.46N1-127[»]
2AWBX-ray3.46N1-127[»]
2GYAelectron microscopy15.00L3-116[»]
2GYCelectron microscopy15.00L3-116[»]
2I2TX-ray3.22N1-127[»]
2I2VX-ray3.22N1-127[»]
2J28electron microscopy8.00N1-127[»]
2QAMX-ray3.21N1-127[»]
2QAOX-ray3.21N1-127[»]
2QBAX-ray3.54N1-127[»]
2QBCX-ray3.54N1-127[»]
2QBEX-ray3.30N1-127[»]
2QBGX-ray3.30N1-127[»]
2QBIX-ray4.00N1-127[»]
2QBKX-ray4.00N1-127[»]
2QOVX-ray3.93N1-127[»]
2QOXX-ray3.93N1-127[»]
2QOZX-ray3.50N1-127[»]
2QP1X-ray3.50N1-127[»]
2RDOelectron microscopy9.10N1-127[»]
2WWQelectron microscopy5.80N1-120[»]
2Z4LX-ray4.45N1-127[»]
2Z4NX-ray4.45N1-127[»]
3BBXelectron microscopy10.00N1-127[»]
3E1Belectron microscopy-G1-127[»]
3E1Delectron microscopy-G1-127[»]
3FIKelectron microscopy6.70N1-120[»]
3I1NX-ray3.19N1-127[»]
3I1PX-ray3.19N1-127[»]
3I1RX-ray3.81N1-127[»]
3I1TX-ray3.81N1-127[»]
3I20X-ray3.71N1-127[»]
3I22X-ray3.71N1-127[»]
3IZTelectron microscopy-O1-127[»]
3IZUelectron microscopy-O1-127[»]
3J01electron microscopy-N1-127[»]
3J0Telectron microscopy12.10P1-127[»]
3J0Welectron microscopy14.70P1-127[»]
3J0Yelectron microscopy13.50P1-127[»]
3J11electron microscopy13.10P1-127[»]
3J12electron microscopy11.50P1-127[»]
3J14electron microscopy11.50P1-127[»]
3J19electron microscopy8.30N1-120[»]
3J37electron microscopy9.80R1-127[»]
3J4Xelectron microscopy12.00N1-120[»]
3J50electron microscopy20.00N1-120[»]
3J51electron microscopy17.00N1-120[»]
3J52electron microscopy12.00N1-120[»]
3J54electron microscopy13.00N1-120[»]
3J56electron microscopy15.00N1-120[»]
3J58electron microscopy17.00N1-120[»]
3J5Aelectron microscopy12.00N1-120[»]
3J5Celectron microscopy17.00N1-120[»]
3J5Eelectron microscopy17.00N1-120[»]
3J5Gelectron microscopy20.00N1-120[»]
3J5Ielectron microscopy15.00N1-120[»]
3J5Kelectron microscopy9.00N1-120[»]
3J5Lelectron microscopy6.60N1-120[»]
3J5Oelectron microscopy6.80N1-127[»]
3J5Uelectron microscopy7.60P1-127[»]
3J5Welectron microscopy7.60Q1-127[»]
3J7Zelectron microscopy3.90N1-127[»]
3KCRelectron microscopy-N1-127[»]
3OASX-ray3.25N1-120[»]
3OATX-ray3.25N1-120[»]
3OFCX-ray3.19N1-120[»]
3OFDX-ray3.19N1-120[»]
3OFQX-ray3.10N1-120[»]
3OFRX-ray3.10N1-120[»]
3OFZX-ray3.29N1-120[»]
3OG0X-ray3.29N1-120[»]
3ORBX-ray3.30N1-127[»]
3R8SX-ray3.00N1-120[»]
3R8TX-ray3.00N1-120[»]
3SGFX-ray3.20R1-127[»]
3UOSX-ray3.70R1-127[»]
4CSUelectron microscopy5.50N1-127[»]
4GARX-ray3.30N1-127[»]
4GAUX-ray3.30N1-127[»]
4KIXX-ray2.90N1-127[»]
4KIZX-ray2.90N1-127[»]
4KJ1X-ray2.90N1-127[»]
4KJ3X-ray2.90N1-127[»]
4KJ5X-ray2.90N1-127[»]
4KJ7X-ray2.90N1-127[»]
4KJ9X-ray2.90N1-127[»]
4KJBX-ray2.90N1-127[»]
4PEBX-ray2.95N1-120[»]
4PECX-ray2.95N1-120[»]
4TOMX-ray3.00N1-120[»]
4TOOX-ray3.00N1-120[»]
4TOVX-ray2.90N1-120[»]
4TOXX-ray2.90N1-120[»]
4TP1X-ray2.90N1-120[»]
4TP3X-ray2.90N1-120[»]
4TP5X-ray2.90N1-120[»]
4TP7X-ray2.90N1-120[»]
4TP9X-ray2.80N1-120[»]
4TPBX-ray2.80N1-120[»]
4TPDX-ray2.80N1-120[»]
4TPFX-ray2.80N1-120[»]
4WAPX-ray3.09N1-120[»]
4WARX-ray3.09N1-120[»]
ProteinModelPortaliP0AG44.
SMRiP0AG44. Positions 1-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35801N.
IntActiP0AG44. 135 interactions.
MINTiMINT-1251899.
STRINGi511145.b3294.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0AG44.
PRIDEiP0AG44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76319; AAC76319; b3294.
BAE77997; BAE77997; BAE77997.
GeneIDi12934436.
947784.
KEGGiecj:Y75_p3882.
eco:b3294.
PATRICi32122020. VBIEscCol129921_3387.

Organism-specific databases

EchoBASEiEB0871.
EcoGeneiEG10878. rplQ.

Phylogenomic databases

eggNOGiCOG0203.
HOGENOMiHOG000019780.
InParanoidiP0AG44.
KOiK02879.
OMAiRVVEPMI.
OrthoDBiEOG6GR3GR.
PhylomeDBiP0AG44.

Enzyme and pathway databases

BioCyciEcoCyc:EG10878-MONOMER.
ECOL316407:JW3256-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG44.
PROiP0AG44.

Gene expression databases

GenevestigatoriP0AG44.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.
PROSITEiPS01167. RIBOSOMAL_L17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L32.
  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. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL17_ECOLI
AccessioniPrimary (citable) accession number: P0AG44
Secondary accession number(s): P02416, Q2M6V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.