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Protein

30S ribosomal protein S11

Gene

rpsK

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

Functioni

Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity).By similarity

Miscellaneous

Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies; exactly how IF-3 interacts with the 30S subunit is controversial (PubMed:7000779, PubMed:7020604, PubMed:6349681).1 Publication3 Publications

GO - Molecular functioni

  • mRNA 5'-UTR binding Source: GO_Central
  • small ribosomal subunit rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10910-MONOMER
MetaCyc:EG10910-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S11
Alternative name(s):
Small ribosomal subunit protein uS111 Publication
Gene namesi
Name:rpsK
Ordered Locus Names:b3297, JW3259
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10910 rpsK

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoliWiki

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001231442 – 12930S ribosomal protein S11Add BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-methylalanine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

EPDiP0A7R9
PaxDbiP0A7R9
PRIDEiP0A7R9

PTM databases

iPTMnetiP0A7R9

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:7007074, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Interacts with proteins S7 and S18 (By similarity). Cross-links to IF-3 (PubMed:7000779, PubMed:7020604, PubMed:6349681).By similarity12 Publications

Protein-protein interaction databases

BioGridi852104, 1 interactor
DIPiDIP-47838N
IntActiP0A7R9, 18 interactors
STRINGi316385.ECDH10B_3472

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 26Combined sources10
Beta strandi29 – 38Combined sources10
Beta strandi43 – 46Combined sources4
Helixi47 – 50Combined sources4
Helixi55 – 57Combined sources3
Helixi60 – 74Combined sources15
Helixi75 – 77Combined sources3
Beta strandi81 – 90Combined sources10
Turni91 – 94Combined sources4
Helixi95 – 104Combined sources10
Beta strandi106 – 112Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-K13-129[»]
2YKRelectron microscopy9.80K13-129[»]
3J9Yelectron microscopy3.90k1-129[»]
3J9Zelectron microscopy3.60SK2-129[»]
3JA1electron microscopy3.60SK2-129[»]
3JBUelectron microscopy3.64K1-129[»]
3JBVelectron microscopy3.32K1-129[»]
3JCDelectron microscopy3.70k1-129[»]
3JCEelectron microscopy3.20k1-129[»]
3JCJelectron microscopy3.70q1-129[»]
3JCNelectron microscopy4.60l1-129[»]
4A2Ielectron microscopy16.50K13-129[»]
4ADVelectron microscopy13.50K2-129[»]
4U1UX-ray2.95AK/CK13-129[»]
4U1VX-ray3.00AK/CK13-129[»]
4U20X-ray2.90AK/CK13-129[»]
4U24X-ray2.90AK/CK13-129[»]
4U25X-ray2.90AK/CK13-129[»]
4U26X-ray2.80AK/CK13-129[»]
4U27X-ray2.80AK/CK13-129[»]
4V47electron microscopy12.30BK2-129[»]
4V48electron microscopy11.50BK2-129[»]
4V4HX-ray3.46AK/CK1-129[»]
4V4QX-ray3.46AK/CK2-129[»]
4V4Velectron microscopy15.00AK13-128[»]
4V4Welectron microscopy15.00AK13-128[»]
4V50X-ray3.22AK/CK2-129[»]
4V52X-ray3.21AK/CK2-129[»]
4V53X-ray3.54AK/CK2-129[»]
4V54X-ray3.30AK/CK2-129[»]
4V55X-ray4.00AK/CK2-129[»]
4V56X-ray3.93AK/CK2-129[»]
4V57X-ray3.50AK/CK2-129[»]
4V5BX-ray3.74BK/DK2-129[»]
4V5Helectron microscopy5.80AK13-129[»]
4V5YX-ray4.45AK/CK2-129[»]
4V64X-ray3.50AK/CK2-129[»]
4V65electron microscopy9.00AC1-129[»]
4V66electron microscopy9.00AC1-129[»]
4V69electron microscopy6.70AK13-129[»]
4V6CX-ray3.19AK/CK1-129[»]
4V6DX-ray3.81AK/CK1-129[»]
4V6EX-ray3.71AK/CK1-129[»]
4V6Kelectron microscopy8.25BO1-129[»]
4V6Lelectron microscopy13.20AO1-129[»]
4V6Melectron microscopy7.10AK2-129[»]
4V6Nelectron microscopy12.10BN2-129[»]
4V6Oelectron microscopy14.70AN2-129[»]
4V6Pelectron microscopy13.50AN2-129[»]
4V6Qelectron microscopy11.50AN2-129[»]
4V6Relectron microscopy11.50AN2-129[»]
4V6Selectron microscopy13.10BM2-129[»]
4V6Telectron microscopy8.30AK13-129[»]
4V6Velectron microscopy9.80AK2-129[»]
4V6Yelectron microscopy12.00AK13-129[»]
4V6Zelectron microscopy12.00AK13-129[»]
4V70electron microscopy17.00AK13-129[»]
4V71electron microscopy20.00AK13-129[»]
4V72electron microscopy13.00AK13-129[»]
4V73electron microscopy15.00AK13-129[»]
4V74electron microscopy17.00AK13-129[»]
4V75electron microscopy12.00AK13-129[»]
4V76electron microscopy17.00AK13-129[»]
4V77electron microscopy17.00AK13-129[»]
4V78electron microscopy20.00AK13-129[»]
4V79electron microscopy15.00AK13-129[»]
4V7Aelectron microscopy9.00AK13-129[»]
4V7Belectron microscopy6.80AK1-129[»]
4V7Celectron microscopy7.60AK2-129[»]
4V7Delectron microscopy7.60BK2-129[»]
4V7Ielectron microscopy9.60BK1-129[»]
4V7SX-ray3.25AK/CK13-129[»]
4V7TX-ray3.19AK/CK13-129[»]
4V7UX-ray3.10AK/CK13-129[»]
4V7VX-ray3.29AK/CK13-129[»]
4V85X-ray3.20AK1-129[»]
4V89X-ray3.70AK1-129[»]
4V9CX-ray3.30AK/CK1-129[»]
4V9DX-ray3.00AK/BK13-129[»]
4V9OX-ray2.90BK/DK/FK/HK1-129[»]
4V9PX-ray2.90BK/DK/FK/HK1-129[»]
4WF1X-ray3.09AK/CK13-129[»]
4WOIX-ray3.00AK/DK1-129[»]
4WWWX-ray3.10QK/XK13-129[»]
4YBBX-ray2.10AK/BK13-129[»]
5AFIelectron microscopy2.90k1-129[»]
5H5Uelectron microscopy3.00r2-129[»]
5IQRelectron microscopy3.00p1-129[»]
5IT8X-ray3.12AK/BK13-129[»]
5J5BX-ray2.80AK/BK13-129[»]
5J7LX-ray3.00AK/BK13-129[»]
5J88X-ray3.32AK/BK1-129[»]
5J8AX-ray3.10AK/BK13-129[»]
5J91X-ray2.96AK/BK13-129[»]
5JC9X-ray3.03AK/BK13-129[»]
5JTEelectron microscopy3.60AK1-129[»]
5JU8electron microscopy3.60AK1-129[»]
5KCRelectron microscopy3.601k1-129[»]
5KCSelectron microscopy3.901k1-129[»]
5KPSelectron microscopy3.90161-129[»]
5KPVelectron microscopy4.10151-129[»]
5KPWelectron microscopy3.90151-129[»]
5KPXelectron microscopy3.90151-129[»]
5L3Pelectron microscopy3.70k1-129[»]
5LZAelectron microscopy3.60k13-128[»]
5LZBelectron microscopy5.30k13-128[»]
5LZCelectron microscopy4.80k13-128[»]
5LZDelectron microscopy3.40k13-128[»]
5LZEelectron microscopy3.50k13-128[»]
5LZFelectron microscopy4.60k13-128[»]
5MDVelectron microscopy2.97p1-129[»]
5MDWelectron microscopy3.06p1-129[»]
5MDYelectron microscopy3.35p1-129[»]
5MDZelectron microscopy3.10p1-129[»]
5ME0electron microscopy13.50K1-129[»]
5ME1electron microscopy13.50K1-129[»]
5MGPelectron microscopy3.10k13-128[»]
5MY1electron microscopy7.60K2-129[»]
5NO2electron microscopy5.16K13-129[»]
5NO3electron microscopy5.16K13-129[»]
5NO4electron microscopy5.16K13-129[»]
5NP6electron microscopy3.60N13-128[»]
5NWYelectron microscopy2.93A1-129[»]
5O2Relectron microscopy3.40k13-128[»]
5U4Ielectron microscopy3.50k13-129[»]
5U9Felectron microscopy3.20K1-129[»]
5U9Gelectron microscopy3.20K1-129[»]
5UYKelectron microscopy3.90K13-128[»]
5UYLelectron microscopy3.60K13-128[»]
5UYMelectron microscopy3.20K13-128[»]
5UYNelectron microscopy4.00K13-128[»]
5UYPelectron microscopy3.90K13-128[»]
5UYQelectron microscopy3.80K13-128[»]
5WDTelectron microscopy3.00k13-128[»]
5WE4electron microscopy3.10k13-128[»]
5WE6electron microscopy3.40k13-128[»]
5WFKelectron microscopy3.40k13-128[»]
6BU8electron microscopy3.50K13-128[»]
6C4Ielectron microscopy3.24k1-129[»]
6ENFelectron microscopy3.20k13-128[»]
6ENJelectron microscopy3.70k13-128[»]
6ENUelectron microscopy3.10k13-128[»]
ProteinModelPortaliP0A7R9
SMRiP0A7R9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7R9

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0100 LUCA
HOGENOMiHOG000111598
InParanoidiP0A7R9
KOiK02948
OMAiKVYVKGP
PhylomeDBiP0A7R9

Family and domain databases

Gene3Di3.30.420.80, 1 hit
HAMAPiMF_01310 Ribosomal_S11, 1 hit
InterProiView protein in InterPro
IPR001971 Ribosomal_S11
IPR019981 Ribosomal_S11_bac-type
IPR018102 Ribosomal_S11_CS
IPR036967 Ribosomal_S11_sf
PANTHERiPTHR11759 PTHR11759, 1 hit
PfamiView protein in Pfam
PF00411 Ribosomal_S11, 1 hit
PIRSFiPIRSF002131 Ribosomal_S11, 1 hit
TIGRFAMsiTIGR03632 uS11_bact, 1 hit
PROSITEiView protein in PROSITE
PS00054 RIBOSOMAL_S11, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS
60 70 80 90 100
GFRGSRKSTP FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL
110 120
NAAGFRITNI TDVTPIPHNG CRPPKKRRV
Length:129
Mass (Da):13,845
Last modified:January 23, 2007 - v2
Checksum:i0C759DDA60E89C0C
GO

Mass spectrometryi

Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02543 Genomic DNA Translation: CAA26393.1
U18997 Genomic DNA Translation: AAA58095.1
U00096 Genomic DNA Translation: AAC76322.1
AP009048 Genomic DNA Translation: BAE77994.1
PIRiB23807 R3EC11
RefSeqiNP_417756.1, NC_000913.3
WP_001029684.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76322; AAC76322; b3297
BAE77994; BAE77994; BAE77994
GeneIDi947792
KEGGiecj:JW3259
eco:b3297
PATRICifig|1411691.4.peg.3434

Similar proteinsi

Entry informationi

Entry nameiRS11_ECOLI
AccessioniPrimary (citable) accession number: P0A7R9
Secondary accession number(s): P02366, Q2M6W2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 130 of the entry and version 2 of the sequence. See 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

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