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Protein

50S ribosomal protein L9

Gene

rplI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.
MetaCyc:EG10870-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L9
Gene namesi
Name:rplI
Ordered Locus Names:b4203, JW4161
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10870. rplI.

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_00001766361 – 14950S ribosomal protein L9Add BLAST149

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei71N6-succinyllysine1 Publication1
Modified residuei83N6-succinyllysine1 Publication1
Modified residuei89N6-acetyllysine1 Publication1
Modified residuei112N6-succinyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7R1.
PaxDbiP0A7R1.
PRIDEiP0A7R1.

2D gel databases

SWISS-2DPAGEP0A7R1.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

BioGridi4259635. 31 interactors.
DIPiDIP-35748N.
IntActiP0A7R1. 59 interactors.
MINTiMINT-1228834.
STRINGi511145.b4203.

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Turni10 – 12Combined sources3
Beta strandi14 – 16Combined sources3
Helixi23 – 26Combined sources4
Turni27 – 34Combined sources8
Beta strandi35 – 37Combined sources3
Helixi42 – 46Combined sources5
Helixi49 – 51Combined sources3
Helixi53 – 57Combined sources5
Turni58 – 60Combined sources3
Turni62 – 64Combined sources3
Helixi65 – 68Combined sources4
Helixi69 – 71Combined sources3
Beta strandi73 – 75Combined sources3
Beta strandi78 – 81Combined sources4
Beta strandi84 – 88Combined sources5
Beta strandi90 – 92Combined sources3
Helixi96 – 99Combined sources4
Helixi101 – 104Combined sources4
Turni105 – 107Combined sources3
Helixi112 – 114Combined sources3
Turni118 – 120Combined sources3
Beta strandi124 – 128Combined sources5
Beta strandi129 – 132Combined sources4
Beta strandi134 – 137Combined sources4
Beta strandi141 – 143Combined sources3
Beta strandi144 – 147Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00H1-149[»]
2RDOelectron microscopy9.10H1-149[»]
3BBXelectron microscopy10.00H1-149[»]
3J5Lelectron microscopy6.60H1-56[»]
3J7Zelectron microscopy3.90H1-149[»]
3J8Gelectron microscopy5.00H1-149[»]
3J9Yelectron microscopy3.90H1-149[»]
3J9Zelectron microscopy3.60L91-149[»]
3JA1electron microscopy3.60LI1-149[»]
3JBUelectron microscopy3.64h1-149[»]
3JBVelectron microscopy3.32h1-149[»]
3JCDelectron microscopy3.70H1-149[»]
3JCEelectron microscopy3.20H1-149[»]
3JCJelectron microscopy3.70G1-149[»]
3JCNelectron microscopy4.60H1-149[»]
487Delectron microscopy7.50K24-123[»]
4CSUelectron microscopy5.50H1-149[»]
4U1UX-ray2.95BH/DH1-149[»]
4U1VX-ray3.00BH/DH1-149[»]
4U20X-ray2.90BH/DH1-149[»]
4U24X-ray2.90BH/DH1-149[»]
4U25X-ray2.90BH/DH1-149[»]
4U26X-ray2.80BH/DH1-149[»]
4U27X-ray2.80BH/DH1-149[»]
4UY8electron microscopy3.80H1-50[»]
4V47electron microscopy12.30AF1-149[»]
4V48electron microscopy11.50AF1-149[»]
4V4HX-ray3.46BH/DH1-149[»]
4V4QX-ray3.46BH/DH1-149[»]
4V4Velectron microscopy15.00BF1-149[»]
4V4Welectron microscopy15.00BF1-149[»]
4V50X-ray3.22BH/DH1-149[»]
4V52X-ray3.21BH/DH1-149[»]
4V53X-ray3.54BH/DH1-149[»]
4V54X-ray3.30BH/DH1-149[»]
4V55X-ray4.00BH/DH1-149[»]
4V56X-ray3.93BH/DH1-149[»]
4V57X-ray3.50BH/DH1-149[»]
4V5BX-ray3.74AH/CH1-149[»]
4V5Helectron microscopy5.80BH1-149[»]
4V5YX-ray4.45BH/DH1-149[»]
4V64X-ray3.50BH/DH1-149[»]
4V65electron microscopy9.00B41-149[»]
4V66electron microscopy9.00B41-149[»]
4V69electron microscopy6.70BH1-149[»]
4V6CX-ray3.19BH/DH1-149[»]
4V6DX-ray3.81BH/DH1-149[»]
4V6EX-ray3.71BH/DH1-149[»]
4V6Kelectron microscopy8.25AI1-149[»]
4V6Lelectron microscopy13.20BI1-149[»]
4V6Melectron microscopy7.10BH1-149[»]
4V6Nelectron microscopy12.10AI1-149[»]
4V6Oelectron microscopy14.70BI1-149[»]
4V6Pelectron microscopy13.50BI1-149[»]
4V6Qelectron microscopy11.50BI1-149[»]
4V6Relectron microscopy11.50BI1-149[»]
4V6Selectron microscopy13.10AI1-149[»]
4V6Telectron microscopy8.30BH1-149[»]
4V6Velectron microscopy9.80BL1-149[»]
4V6Yelectron microscopy12.00BH1-149[»]
4V6Zelectron microscopy12.00BH1-149[»]
4V70electron microscopy17.00BH1-149[»]
4V71electron microscopy20.00BH1-149[»]
4V72electron microscopy13.00BH1-149[»]
4V73electron microscopy15.00BH1-149[»]
4V74electron microscopy17.00BH1-149[»]
4V75electron microscopy12.00BH1-149[»]
4V76electron microscopy17.00BH1-149[»]
4V77electron microscopy17.00BH1-149[»]
4V78electron microscopy20.00BH1-149[»]
4V79electron microscopy15.00BH1-149[»]
4V7Aelectron microscopy9.00BH1-149[»]
4V7Belectron microscopy6.80BH1-50[»]
4V7Celectron microscopy7.60BI1-149[»]
4V7Delectron microscopy7.60AI1-149[»]
4V7Ielectron microscopy9.60AH1-149[»]
4V7SX-ray3.25BH/DH1-149[»]
4V7TX-ray3.19BH/DH1-149[»]
4V7UX-ray3.10BH/DH1-149[»]
4V7VX-ray3.29BH/DH1-149[»]
4V9CX-ray3.30BH/DH1-149[»]
4V9DX-ray3.00CH/DH1-149[»]
4V9OX-ray2.90AH/CH/EH/GH1-50[»]
4V9PX-ray2.90AH/CH/EH/GH1-50[»]
4WF1X-ray3.09BH/DH1-149[»]
4WOIX-ray3.00BH/CH1-149[»]
4WWWX-ray3.10RH/YH1-149[»]
4YBBX-ray2.10CH/DH1-149[»]
5ADYelectron microscopy4.50H1-149[»]
5AFIelectron microscopy2.90H1-149[»]
5AKAelectron microscopy5.70H1-149[»]
5GADelectron microscopy3.70H1-149[»]
5GAEelectron microscopy3.33H1-149[»]
5GAFelectron microscopy4.30H1-149[»]
5GAGelectron microscopy3.80H1-149[»]
5GAHelectron microscopy3.80H1-149[»]
5IQRelectron microscopy3.00G1-149[»]
5IT8X-ray3.12CH/DH1-149[»]
5J5BX-ray2.80CH/DH1-149[»]
5J7LX-ray3.00CH/DH1-149[»]
5J88X-ray3.32CH/DH1-149[»]
5J8AX-ray3.10CH/DH1-149[»]
5J91X-ray2.96CH/DH1-149[»]
5JC9X-ray3.03CH/DH1-149[»]
5JTEelectron microscopy3.60BH1-149[»]
5JU8electron microscopy3.60BH1-149[»]
5KCRelectron microscopy3.601I1-149[»]
5KCSelectron microscopy3.901I1-149[»]
5KPSelectron microscopy3.90G1-149[»]
5KPVelectron microscopy4.10F1-149[»]
5KPWelectron microscopy3.90F1-149[»]
5KPXelectron microscopy3.90F1-149[»]
5L3Pelectron microscopy3.70I1-149[»]
ProteinModelPortaliP0A7R1.
SMRiP0A7R1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7R1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L9P family.Curated

Phylogenomic databases

eggNOGiENOG4105K9Q. Bacteria.
COG0359. LUCA.
HOGENOMiHOG000040337.
InParanoidiP0A7R1.
KOiK02939.
OMAiAIRWTKG.
PhylomeDBiP0A7R1.

Family and domain databases

Gene3Di3.10.430.100. 1 hit.
3.40.5.10. 1 hit.
HAMAPiMF_00503. Ribosomal_L9. 1 hit.
InterProiIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERiPTHR21368. PTHR21368. 1 hit.
PfamiPF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMiSSF55653. SSF55653. 1 hit.
SSF55658. SSF55658. 1 hit.
TIGRFAMsiTIGR00158. L9. 1 hit.
PROSITEiPS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVILLDKVA NLGSLGDQVN VKAGYARNFL VPQGKAVPAT KKNIEFFEAR
60 70 80 90 100
RAELEAKLAE VLAAANARAE KINALETVTI ASKAGDEGKL FGSIGTRDIA
110 120 130 140
DAVTAAGVEV AKSEVRLPNG VLRTTGEHEV SFQVHSEVFA KVIVNVVAE
Length:149
Mass (Da):15,769
Last modified:April 1, 1988 - v1
Checksum:iF8FF527DBB9458CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106A → AD AA sequence (Ref. 1) Curated1
Sequence conflicti125 – 128TGEH → HGE AA sequence (Ref. 1) Curated4
Sequence conflicti136Missing AA sequence (Ref. 1) Curated1

Mass spectrometryi

Molecular mass is 15769.7 Da from positions 1 - 149. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27655.1.
U14003 Genomic DNA. Translation: AAA97099.1.
U00096 Genomic DNA. Translation: AAC77160.1.
AP009048 Genomic DNA. Translation: BAE78204.1.
PIRiF65231. R5EC9.
RefSeqiNP_418624.1. NC_000913.3.
WP_001196062.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77160; AAC77160; b4203.
BAE78204; BAE78204; BAE78204.
GeneIDi948720.
KEGGiecj:JW4161.
eco:b4203.
PATRICi32123981. VBIEscCol129921_4335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27655.1.
U14003 Genomic DNA. Translation: AAA97099.1.
U00096 Genomic DNA. Translation: AAC77160.1.
AP009048 Genomic DNA. Translation: BAE78204.1.
PIRiF65231. R5EC9.
RefSeqiNP_418624.1. NC_000913.3.
WP_001196062.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00H1-149[»]
2RDOelectron microscopy9.10H1-149[»]
3BBXelectron microscopy10.00H1-149[»]
3J5Lelectron microscopy6.60H1-56[»]
3J7Zelectron microscopy3.90H1-149[»]
3J8Gelectron microscopy5.00H1-149[»]
3J9Yelectron microscopy3.90H1-149[»]
3J9Zelectron microscopy3.60L91-149[»]
3JA1electron microscopy3.60LI1-149[»]
3JBUelectron microscopy3.64h1-149[»]
3JBVelectron microscopy3.32h1-149[»]
3JCDelectron microscopy3.70H1-149[»]
3JCEelectron microscopy3.20H1-149[»]
3JCJelectron microscopy3.70G1-149[»]
3JCNelectron microscopy4.60H1-149[»]
487Delectron microscopy7.50K24-123[»]
4CSUelectron microscopy5.50H1-149[»]
4U1UX-ray2.95BH/DH1-149[»]
4U1VX-ray3.00BH/DH1-149[»]
4U20X-ray2.90BH/DH1-149[»]
4U24X-ray2.90BH/DH1-149[»]
4U25X-ray2.90BH/DH1-149[»]
4U26X-ray2.80BH/DH1-149[»]
4U27X-ray2.80BH/DH1-149[»]
4UY8electron microscopy3.80H1-50[»]
4V47electron microscopy12.30AF1-149[»]
4V48electron microscopy11.50AF1-149[»]
4V4HX-ray3.46BH/DH1-149[»]
4V4QX-ray3.46BH/DH1-149[»]
4V4Velectron microscopy15.00BF1-149[»]
4V4Welectron microscopy15.00BF1-149[»]
4V50X-ray3.22BH/DH1-149[»]
4V52X-ray3.21BH/DH1-149[»]
4V53X-ray3.54BH/DH1-149[»]
4V54X-ray3.30BH/DH1-149[»]
4V55X-ray4.00BH/DH1-149[»]
4V56X-ray3.93BH/DH1-149[»]
4V57X-ray3.50BH/DH1-149[»]
4V5BX-ray3.74AH/CH1-149[»]
4V5Helectron microscopy5.80BH1-149[»]
4V5YX-ray4.45BH/DH1-149[»]
4V64X-ray3.50BH/DH1-149[»]
4V65electron microscopy9.00B41-149[»]
4V66electron microscopy9.00B41-149[»]
4V69electron microscopy6.70BH1-149[»]
4V6CX-ray3.19BH/DH1-149[»]
4V6DX-ray3.81BH/DH1-149[»]
4V6EX-ray3.71BH/DH1-149[»]
4V6Kelectron microscopy8.25AI1-149[»]
4V6Lelectron microscopy13.20BI1-149[»]
4V6Melectron microscopy7.10BH1-149[»]
4V6Nelectron microscopy12.10AI1-149[»]
4V6Oelectron microscopy14.70BI1-149[»]
4V6Pelectron microscopy13.50BI1-149[»]
4V6Qelectron microscopy11.50BI1-149[»]
4V6Relectron microscopy11.50BI1-149[»]
4V6Selectron microscopy13.10AI1-149[»]
4V6Telectron microscopy8.30BH1-149[»]
4V6Velectron microscopy9.80BL1-149[»]
4V6Yelectron microscopy12.00BH1-149[»]
4V6Zelectron microscopy12.00BH1-149[»]
4V70electron microscopy17.00BH1-149[»]
4V71electron microscopy20.00BH1-149[»]
4V72electron microscopy13.00BH1-149[»]
4V73electron microscopy15.00BH1-149[»]
4V74electron microscopy17.00BH1-149[»]
4V75electron microscopy12.00BH1-149[»]
4V76electron microscopy17.00BH1-149[»]
4V77electron microscopy17.00BH1-149[»]
4V78electron microscopy20.00BH1-149[»]
4V79electron microscopy15.00BH1-149[»]
4V7Aelectron microscopy9.00BH1-149[»]
4V7Belectron microscopy6.80BH1-50[»]
4V7Celectron microscopy7.60BI1-149[»]
4V7Delectron microscopy7.60AI1-149[»]
4V7Ielectron microscopy9.60AH1-149[»]
4V7SX-ray3.25BH/DH1-149[»]
4V7TX-ray3.19BH/DH1-149[»]
4V7UX-ray3.10BH/DH1-149[»]
4V7VX-ray3.29BH/DH1-149[»]
4V9CX-ray3.30BH/DH1-149[»]
4V9DX-ray3.00CH/DH1-149[»]
4V9OX-ray2.90AH/CH/EH/GH1-50[»]
4V9PX-ray2.90AH/CH/EH/GH1-50[»]
4WF1X-ray3.09BH/DH1-149[»]
4WOIX-ray3.00BH/CH1-149[»]
4WWWX-ray3.10RH/YH1-149[»]
4YBBX-ray2.10CH/DH1-149[»]
5ADYelectron microscopy4.50H1-149[»]
5AFIelectron microscopy2.90H1-149[»]
5AKAelectron microscopy5.70H1-149[»]
5GADelectron microscopy3.70H1-149[»]
5GAEelectron microscopy3.33H1-149[»]
5GAFelectron microscopy4.30H1-149[»]
5GAGelectron microscopy3.80H1-149[»]
5GAHelectron microscopy3.80H1-149[»]
5IQRelectron microscopy3.00G1-149[»]
5IT8X-ray3.12CH/DH1-149[»]
5J5BX-ray2.80CH/DH1-149[»]
5J7LX-ray3.00CH/DH1-149[»]
5J88X-ray3.32CH/DH1-149[»]
5J8AX-ray3.10CH/DH1-149[»]
5J91X-ray2.96CH/DH1-149[»]
5JC9X-ray3.03CH/DH1-149[»]
5JTEelectron microscopy3.60BH1-149[»]
5JU8electron microscopy3.60BH1-149[»]
5KCRelectron microscopy3.601I1-149[»]
5KCSelectron microscopy3.901I1-149[»]
5KPSelectron microscopy3.90G1-149[»]
5KPVelectron microscopy4.10F1-149[»]
5KPWelectron microscopy3.90F1-149[»]
5KPXelectron microscopy3.90F1-149[»]
5L3Pelectron microscopy3.70I1-149[»]
ProteinModelPortaliP0A7R1.
SMRiP0A7R1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259635. 31 interactors.
DIPiDIP-35748N.
IntActiP0A7R1. 59 interactors.
MINTiMINT-1228834.
STRINGi511145.b4203.

2D gel databases

SWISS-2DPAGEP0A7R1.

Proteomic databases

EPDiP0A7R1.
PaxDbiP0A7R1.
PRIDEiP0A7R1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77160; AAC77160; b4203.
BAE78204; BAE78204; BAE78204.
GeneIDi948720.
KEGGiecj:JW4161.
eco:b4203.
PATRICi32123981. VBIEscCol129921_4335.

Organism-specific databases

EchoBASEiEB0863.
EcoGeneiEG10870. rplI.

Phylogenomic databases

eggNOGiENOG4105K9Q. Bacteria.
COG0359. LUCA.
HOGENOMiHOG000040337.
InParanoidiP0A7R1.
KOiK02939.
OMAiAIRWTKG.
PhylomeDBiP0A7R1.

Enzyme and pathway databases

BioCyciEcoCyc:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.
MetaCyc:EG10870-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7R1.
PROiP0A7R1.

Family and domain databases

Gene3Di3.10.430.100. 1 hit.
3.40.5.10. 1 hit.
HAMAPiMF_00503. Ribosomal_L9. 1 hit.
InterProiIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERiPTHR21368. PTHR21368. 1 hit.
PfamiPF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMiSSF55653. SSF55653. 1 hit.
SSF55658. SSF55658. 1 hit.
TIGRFAMsiTIGR00158. L9. 1 hit.
PROSITEiPS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL9_ECOLI
AccessioniPrimary (citable) accession number: P0A7R1
Secondary accession number(s): P02418, Q2M6A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 30, 2016
This is version 121 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.