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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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10878-MONOMER.
ECOL316407:JW3256-MONOMER.
MetaCyc:EG10878-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10878. rplQ.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001755241 – 12750S ribosomal protein L17Add BLAST127

Proteomic databases

EPDiP0AG44.
PaxDbiP0AG44.
PRIDEiP0AG44.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L32.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Helixi14 – 31Combined sources18
Beta strandi32 – 37Combined sources6
Helixi38 – 55Combined sources18
Helixi60 – 68Combined sources9
Helixi73 – 81Combined sources9
Helixi83 – 86Combined sources4
Turni87 – 89Combined sources3
Beta strandi95 – 102Combined sources8
Turni104 – 106Combined sources3
Beta strandi109 – 116Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00N1-127[»]
2RDOelectron microscopy9.10N1-127[»]
3BBXelectron microscopy10.00N1-127[»]
3J5Lelectron microscopy6.60N1-120[»]
3J7Zelectron microscopy3.90N1-127[»]
3J8Gelectron microscopy5.00N1-127[»]
3J9Yelectron microscopy3.90N1-127[»]
3J9Zelectron microscopy3.60LJ1-127[»]
3JA1electron microscopy3.60LP1-127[»]
3JBUelectron microscopy3.64n1-127[»]
3JBVelectron microscopy3.32n1-127[»]
3JCDelectron microscopy3.70N1-127[»]
3JCEelectron microscopy3.20N1-127[»]
3JCJelectron microscopy3.70M1-127[»]
3JCNelectron microscopy4.60N1-127[»]
4CSUelectron microscopy5.50N1-127[»]
4U1UX-ray2.95BN/DN1-120[»]
4U1VX-ray3.00BN/DN1-120[»]
4U20X-ray2.90BN/DN1-120[»]
4U24X-ray2.90BN/DN1-120[»]
4U25X-ray2.90BN/DN1-120[»]
4U26X-ray2.80BN/DN1-120[»]
4U27X-ray2.80BN/DN1-120[»]
4UY8electron microscopy3.80N1-120[»]
4V47electron microscopy12.30AL1-127[»]
4V48electron microscopy11.50AL1-127[»]
4V4HX-ray3.46BN/DN1-127[»]
4V4QX-ray3.46BN/DN1-127[»]
4V4Velectron microscopy15.00BL3-116[»]
4V4Welectron microscopy15.00BL3-116[»]
4V50X-ray3.22BN/DN1-127[»]
4V52X-ray3.21BN/DN1-127[»]
4V53X-ray3.54BN/DN1-127[»]
4V54X-ray3.30BN/DN1-127[»]
4V55X-ray4.00BN/DN1-127[»]
4V56X-ray3.93BN/DN1-127[»]
4V57X-ray3.50BN/DN1-127[»]
4V5BX-ray3.74AN/CN1-127[»]
4V5Helectron microscopy5.80BN1-120[»]
4V5YX-ray4.45BN/DN1-127[»]
4V64X-ray3.50BN/DN1-127[»]
4V65electron microscopy9.00BG1-127[»]
4V66electron microscopy9.00BG1-127[»]
4V69electron microscopy6.70BN1-120[»]
4V6CX-ray3.19BN/DN1-127[»]
4V6DX-ray3.81BN/DN1-127[»]
4V6EX-ray3.71BN/DN1-127[»]
4V6Kelectron microscopy8.25AO1-127[»]
4V6Lelectron microscopy13.20BO1-127[»]
4V6Melectron microscopy7.10BN1-127[»]
4V6Nelectron microscopy12.10AP1-127[»]
4V6Oelectron microscopy14.70BP1-127[»]
4V6Pelectron microscopy13.50BP1-127[»]
4V6Qelectron microscopy11.50BP1-127[»]
4V6Relectron microscopy11.50BP1-127[»]
4V6Selectron microscopy13.10AP1-127[»]
4V6Telectron microscopy8.30BN1-120[»]
4V6Velectron microscopy9.80BR1-127[»]
4V6Yelectron microscopy12.00BN1-120[»]
4V6Zelectron microscopy12.00BN1-120[»]
4V70electron microscopy17.00BN1-120[»]
4V71electron microscopy20.00BN1-120[»]
4V72electron microscopy13.00BN1-120[»]
4V73electron microscopy15.00BN1-120[»]
4V74electron microscopy17.00BN1-120[»]
4V75electron microscopy12.00BN1-120[»]
4V76electron microscopy17.00BN1-120[»]
4V77electron microscopy17.00BN1-120[»]
4V78electron microscopy20.00BN1-120[»]
4V79electron microscopy15.00BN1-120[»]
4V7Aelectron microscopy9.00BN1-120[»]
4V7Belectron microscopy6.80BN1-127[»]
4V7Celectron microscopy7.60BP1-127[»]
4V7Delectron microscopy7.60AQ1-127[»]
4V7Ielectron microscopy9.60AN1-127[»]
4V7SX-ray3.25BN/DN1-120[»]
4V7TX-ray3.19BN/DN1-120[»]
4V7UX-ray3.10BN/DN1-120[»]
4V7VX-ray3.29BN/DN1-120[»]
4V85X-ray3.20R1-127[»]
4V89X-ray3.70BR1-127[»]
4V9CX-ray3.30BN/DN1-127[»]
4V9DX-ray3.00CN/DN1-120[»]
4V9OX-ray2.90AN/CN/EN/GN1-127[»]
4V9PX-ray2.90AN/CN/EN/GN1-127[»]
4WF1X-ray3.09BN/DN1-120[»]
4WOIX-ray3.00BN/CN1-127[»]
4WWWX-ray3.10RN/YN1-120[»]
4YBBX-ray2.10CO/DO1-125[»]
5ADYelectron microscopy4.50N1-127[»]
5AFIelectron microscopy2.90N1-127[»]
5AKAelectron microscopy5.70N1-127[»]
5GADelectron microscopy3.70O1-127[»]
5GAEelectron microscopy3.33O1-127[»]
5GAFelectron microscopy4.30O1-125[»]
5GAGelectron microscopy3.80O1-127[»]
5GAHelectron microscopy3.80O1-127[»]
5IQRelectron microscopy3.00N1-127[»]
5IT8X-ray3.12CO/DO1-125[»]
5J5BX-ray2.80CO/DO1-125[»]
5J7LX-ray3.00CO/DO1-125[»]
5J88X-ray3.32CO/DO1-127[»]
5J8AX-ray3.10CO/DO1-125[»]
5J91X-ray2.96CO/DO1-125[»]
5JC9X-ray3.03CO/DO1-125[»]
5JTEelectron microscopy3.60BN1-127[»]
5JU8electron microscopy3.60BN1-127[»]
5KCRelectron microscopy3.601R1-127[»]
5KCSelectron microscopy3.901R1-127[»]
5KPSelectron microscopy3.90N1-127[»]
5KPVelectron microscopy4.10M1-127[»]
5KPWelectron microscopy3.90M1-127[»]
5KPXelectron microscopy3.90M1-127[»]
5L3Pelectron microscopy3.70R1-127[»]
ProteinModelPortaliP0AG44.
SMRiP0AG44.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG44.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L17P family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108ZT0. Bacteria.
COG0203. LUCA.
HOGENOMiHOG000019780.
InParanoidiP0AG44.
KOiK02879.
OMAiKYERITT.
PhylomeDBiP0AG44.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17. 1 hit.
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.
WP_001216368.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76319; AAC76319; b3294.
BAE77997; BAE77997; BAE77997.
GeneIDi947784.
KEGGiecj:JW3256.
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.
WP_001216368.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00N1-127[»]
2RDOelectron microscopy9.10N1-127[»]
3BBXelectron microscopy10.00N1-127[»]
3J5Lelectron microscopy6.60N1-120[»]
3J7Zelectron microscopy3.90N1-127[»]
3J8Gelectron microscopy5.00N1-127[»]
3J9Yelectron microscopy3.90N1-127[»]
3J9Zelectron microscopy3.60LJ1-127[»]
3JA1electron microscopy3.60LP1-127[»]
3JBUelectron microscopy3.64n1-127[»]
3JBVelectron microscopy3.32n1-127[»]
3JCDelectron microscopy3.70N1-127[»]
3JCEelectron microscopy3.20N1-127[»]
3JCJelectron microscopy3.70M1-127[»]
3JCNelectron microscopy4.60N1-127[»]
4CSUelectron microscopy5.50N1-127[»]
4U1UX-ray2.95BN/DN1-120[»]
4U1VX-ray3.00BN/DN1-120[»]
4U20X-ray2.90BN/DN1-120[»]
4U24X-ray2.90BN/DN1-120[»]
4U25X-ray2.90BN/DN1-120[»]
4U26X-ray2.80BN/DN1-120[»]
4U27X-ray2.80BN/DN1-120[»]
4UY8electron microscopy3.80N1-120[»]
4V47electron microscopy12.30AL1-127[»]
4V48electron microscopy11.50AL1-127[»]
4V4HX-ray3.46BN/DN1-127[»]
4V4QX-ray3.46BN/DN1-127[»]
4V4Velectron microscopy15.00BL3-116[»]
4V4Welectron microscopy15.00BL3-116[»]
4V50X-ray3.22BN/DN1-127[»]
4V52X-ray3.21BN/DN1-127[»]
4V53X-ray3.54BN/DN1-127[»]
4V54X-ray3.30BN/DN1-127[»]
4V55X-ray4.00BN/DN1-127[»]
4V56X-ray3.93BN/DN1-127[»]
4V57X-ray3.50BN/DN1-127[»]
4V5BX-ray3.74AN/CN1-127[»]
4V5Helectron microscopy5.80BN1-120[»]
4V5YX-ray4.45BN/DN1-127[»]
4V64X-ray3.50BN/DN1-127[»]
4V65electron microscopy9.00BG1-127[»]
4V66electron microscopy9.00BG1-127[»]
4V69electron microscopy6.70BN1-120[»]
4V6CX-ray3.19BN/DN1-127[»]
4V6DX-ray3.81BN/DN1-127[»]
4V6EX-ray3.71BN/DN1-127[»]
4V6Kelectron microscopy8.25AO1-127[»]
4V6Lelectron microscopy13.20BO1-127[»]
4V6Melectron microscopy7.10BN1-127[»]
4V6Nelectron microscopy12.10AP1-127[»]
4V6Oelectron microscopy14.70BP1-127[»]
4V6Pelectron microscopy13.50BP1-127[»]
4V6Qelectron microscopy11.50BP1-127[»]
4V6Relectron microscopy11.50BP1-127[»]
4V6Selectron microscopy13.10AP1-127[»]
4V6Telectron microscopy8.30BN1-120[»]
4V6Velectron microscopy9.80BR1-127[»]
4V6Yelectron microscopy12.00BN1-120[»]
4V6Zelectron microscopy12.00BN1-120[»]
4V70electron microscopy17.00BN1-120[»]
4V71electron microscopy20.00BN1-120[»]
4V72electron microscopy13.00BN1-120[»]
4V73electron microscopy15.00BN1-120[»]
4V74electron microscopy17.00BN1-120[»]
4V75electron microscopy12.00BN1-120[»]
4V76electron microscopy17.00BN1-120[»]
4V77electron microscopy17.00BN1-120[»]
4V78electron microscopy20.00BN1-120[»]
4V79electron microscopy15.00BN1-120[»]
4V7Aelectron microscopy9.00BN1-120[»]
4V7Belectron microscopy6.80BN1-127[»]
4V7Celectron microscopy7.60BP1-127[»]
4V7Delectron microscopy7.60AQ1-127[»]
4V7Ielectron microscopy9.60AN1-127[»]
4V7SX-ray3.25BN/DN1-120[»]
4V7TX-ray3.19BN/DN1-120[»]
4V7UX-ray3.10BN/DN1-120[»]
4V7VX-ray3.29BN/DN1-120[»]
4V85X-ray3.20R1-127[»]
4V89X-ray3.70BR1-127[»]
4V9CX-ray3.30BN/DN1-127[»]
4V9DX-ray3.00CN/DN1-120[»]
4V9OX-ray2.90AN/CN/EN/GN1-127[»]
4V9PX-ray2.90AN/CN/EN/GN1-127[»]
4WF1X-ray3.09BN/DN1-120[»]
4WOIX-ray3.00BN/CN1-127[»]
4WWWX-ray3.10RN/YN1-120[»]
4YBBX-ray2.10CO/DO1-125[»]
5ADYelectron microscopy4.50N1-127[»]
5AFIelectron microscopy2.90N1-127[»]
5AKAelectron microscopy5.70N1-127[»]
5GADelectron microscopy3.70O1-127[»]
5GAEelectron microscopy3.33O1-127[»]
5GAFelectron microscopy4.30O1-125[»]
5GAGelectron microscopy3.80O1-127[»]
5GAHelectron microscopy3.80O1-127[»]
5IQRelectron microscopy3.00N1-127[»]
5IT8X-ray3.12CO/DO1-125[»]
5J5BX-ray2.80CO/DO1-125[»]
5J7LX-ray3.00CO/DO1-125[»]
5J88X-ray3.32CO/DO1-127[»]
5J8AX-ray3.10CO/DO1-125[»]
5J91X-ray2.96CO/DO1-125[»]
5JC9X-ray3.03CO/DO1-125[»]
5JTEelectron microscopy3.60BN1-127[»]
5JU8electron microscopy3.60BN1-127[»]
5KCRelectron microscopy3.601R1-127[»]
5KCSelectron microscopy3.901R1-127[»]
5KPSelectron microscopy3.90N1-127[»]
5KPVelectron microscopy4.10M1-127[»]
5KPWelectron microscopy3.90M1-127[»]
5KPXelectron microscopy3.90M1-127[»]
5L3Pelectron microscopy3.70R1-127[»]
ProteinModelPortaliP0AG44.
SMRiP0AG44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP0AG44.
PaxDbiP0AG44.
PRIDEiP0AG44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76319; AAC76319; b3294.
BAE77997; BAE77997; BAE77997.
GeneIDi947784.
KEGGiecj:JW3256.
eco:b3294.
PATRICi32122020. VBIEscCol129921_3387.

Organism-specific databases

EchoBASEiEB0871.
EcoGeneiEG10878. rplQ.

Phylogenomic databases

eggNOGiENOG4108ZT0. Bacteria.
COG0203. LUCA.
HOGENOMiHOG000019780.
InParanoidiP0AG44.
KOiK02879.
OMAiKYERITT.
PhylomeDBiP0AG44.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AG44.
PROiP0AG44.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17. 1 hit.
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...

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: November 30, 2016
This is version 108 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

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 one 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.