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Protein

30S ribosomal protein S6

Gene

rpsF

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

Functioni

Binds together with S18 to 16S ribosomal RNA.

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER.
MetaCyc:EG10905-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S6
Alternative name(s):
Small ribosomal subunit protein bS61 Publication
Cleaved into the following 2 chains:
Gene namesi
Name:rpsF
Ordered Locus Names:b4200, JW4158
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10905. rpsF.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000306401 – 13530S ribosomal protein S6, fully modified isoform1 PublicationAdd BLAST135
ChainiPRO_00000306411 – 13130S ribosomal protein S6, non-modified isoformAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei93N6-acetyllysine1 Publication1

Post-translational modificationi

5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP02358.
PRIDEiP02358.

2D gel databases

SWISS-2DPAGEiP02358.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:328274, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsRP0A7T74EBI-543068,EBI-548844

Protein-protein interaction databases

BioGridi4259641. 276 interactors.
DIPiDIP-10782N.
IntActiP02358. 57 interactors.
MINTiMINT-1279331.
STRINGi316385.ECDH10B_4395.

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Beta strandi7 – 10Combined sources4
Helixi13 – 17Combined sources5
Helixi18 – 31Combined sources14
Beta strandi35 – 37Combined sources3
Beta strandi40 – 45Combined sources6
Beta strandi51 – 53Combined sources3
Beta strandi57 – 61Combined sources5
Beta strandi64 – 66Combined sources3
Helixi70 – 80Combined sources11
Beta strandi82 – 88Combined sources7
Beta strandi89 – 91Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50C1-97[»]
1M5Gmodel-F1-100[»]
2YKRelectron microscopy9.80F1-100[»]
3IY8electron microscopy14.10F2-100[»]
3J9Yelectron microscopy3.90f1-135[»]
3J9Zelectron microscopy3.60SF1-135[»]
3JA1electron microscopy3.60SF1-135[»]
3JBUelectron microscopy3.64F1-131[»]
3JBVelectron microscopy3.32F1-131[»]
3JCDelectron microscopy3.70f1-135[»]
3JCEelectron microscopy3.20f1-135[»]
3JCJelectron microscopy3.70n1-135[»]
3JCNelectron microscopy4.60i1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4U1UX-ray2.95AF/CF1-100[»]
4U1VX-ray3.00AF/CF1-100[»]
4U20X-ray2.90AF/CF1-100[»]
4U24X-ray2.90AF/CF1-100[»]
4U25X-ray2.90AF/CF1-100[»]
4U26X-ray2.80AF/CF1-100[»]
4U27X-ray2.80AF/CF1-100[»]
4V47electron microscopy12.30BF1-135[»]
4V48electron microscopy11.50BF1-135[»]
4V4HX-ray3.46AF/CF1-135[»]
4V4QX-ray3.46AF/CF1-135[»]
4V4Velectron microscopy15.00AF1-95[»]
4V4Welectron microscopy15.00AF1-95[»]
4V50X-ray3.22AF/CF1-135[»]
4V52X-ray3.21AF/CF1-135[»]
4V53X-ray3.54AF/CF1-135[»]
4V54X-ray3.30AF/CF1-135[»]
4V55X-ray4.00AF/CF1-135[»]
4V56X-ray3.93AF/CF1-135[»]
4V57X-ray3.50AF/CF1-135[»]
4V5BX-ray3.74BF/DF1-135[»]
4V5Helectron microscopy5.80AF1-100[»]
4V5YX-ray4.45AF/CF1-135[»]
4V64X-ray3.50AF/CF1-135[»]
4V65electron microscopy9.00AT1-135[»]
4V66electron microscopy9.00AT1-135[»]
4V69electron microscopy6.70AF1-100[»]
4V6CX-ray3.19AF/CF1-135[»]
4V6DX-ray3.81AF/CF1-135[»]
4V6EX-ray3.71AF/CF1-135[»]
4V6Kelectron microscopy8.25BJ1-135[»]
4V6Lelectron microscopy13.20AJ1-135[»]
4V6Melectron microscopy7.10AF1-135[»]
4V6Nelectron microscopy12.10BI1-135[»]
4V6Oelectron microscopy14.70AI1-135[»]
4V6Pelectron microscopy13.50AI1-135[»]
4V6Qelectron microscopy11.50AI1-135[»]
4V6Relectron microscopy11.50AI1-135[»]
4V6Selectron microscopy13.10BH1-135[»]
4V6Telectron microscopy8.30AF1-100[»]
4V6Velectron microscopy9.80AF1-135[»]
4V6Yelectron microscopy12.00AF1-100[»]
4V6Zelectron microscopy12.00AF1-100[»]
4V70electron microscopy17.00AF1-100[»]
4V71electron microscopy20.00AF1-100[»]
4V72electron microscopy13.00AF1-100[»]
4V73electron microscopy15.00AF1-100[»]
4V74electron microscopy17.00AF1-100[»]
4V75electron microscopy12.00AF1-100[»]
4V76electron microscopy17.00AF1-100[»]
4V77electron microscopy17.00AF1-100[»]
4V78electron microscopy20.00AF1-100[»]
4V79electron microscopy15.00AF1-100[»]
4V7Aelectron microscopy9.00AF1-100[»]
4V7Belectron microscopy6.80AF1-135[»]
4V7Celectron microscopy7.60AF1-131[»]
4V7Delectron microscopy7.60BF1-131[»]
4V7Ielectron microscopy9.60BF1-135[»]
4V7SX-ray3.25AF/CF1-100[»]
4V7TX-ray3.19AF/CF1-100[»]
4V7UX-ray3.10AF/CF1-100[»]
4V7VX-ray3.29AF/CF1-100[»]
4V85X-ray3.20F1-131[»]
4V89X-ray3.70AF1-135[»]
4V9CX-ray3.30AF/CF1-135[»]
4V9DX-ray3.00AF/BF1-100[»]
4V9OX-ray2.90BF/DF/FF/HF1-135[»]
4V9PX-ray2.90BF/DF/FF/HF1-135[»]
4WF1X-ray3.09AF/CF1-100[»]
4WOIX-ray3.00AF/DF1-135[»]
4WWWX-ray3.10QF/XF1-100[»]
4YBBX-ray2.10AF/BF1-106[»]
5AFIelectron microscopy2.90f1-135[»]
5H5Uelectron microscopy3.00m1-135[»]
5IQRelectron microscopy3.00k1-135[»]
5IT8X-ray3.12AF/BF1-106[»]
5J5BX-ray2.80AF/BF1-106[»]
5J7LX-ray3.00AF/BF1-106[»]
5J88X-ray3.32AF/BF1-106[»]
5J8AX-ray3.10AF/BF1-106[»]
5J91X-ray2.96AF/BF1-106[»]
5JC9X-ray3.03AF/BF1-106[»]
5JTEelectron microscopy3.60AF1-135[»]
5JU8electron microscopy3.60AF1-135[»]
5KCRelectron microscopy3.601f1-135[»]
5KCSelectron microscopy3.901f1-135[»]
5KPSelectron microscopy3.90111-135[»]
5KPVelectron microscopy4.10101-135[»]
5KPWelectron microscopy3.90101-135[»]
5KPXelectron microscopy3.90101-135[»]
5L3Pelectron microscopy3.70f1-135[»]
5LZAelectron microscopy3.60f1-100[»]
5LZBelectron microscopy5.30f1-100[»]
5LZCelectron microscopy4.80f1-100[»]
5LZDelectron microscopy3.40f1-100[»]
5LZEelectron microscopy3.50f1-100[»]
5LZFelectron microscopy4.60f1-100[»]
5MDVelectron microscopy2.97k1-135[»]
5MDWelectron microscopy3.06k1-135[»]
5MDYelectron microscopy3.35k1-135[»]
5MDZelectron microscopy3.10k1-135[»]
5ME0electron microscopy13.50F1-131[»]
5ME1electron microscopy13.50F1-131[»]
5MGPelectron microscopy3.10f1-100[»]
5MY1electron microscopy7.60F1-135[»]
5NO2electron microscopy5.16F1-106[»]
5NO3electron microscopy5.16F1-106[»]
5NO4electron microscopy5.16F1-106[»]
5NP6electron microscopy3.60I1-100[»]
5U4Ielectron microscopy3.50f1-135[»]
5U9Felectron microscopy3.20F1-131[»]
5U9Gelectron microscopy3.20F1-131[»]
5UYKelectron microscopy3.90F1-100[»]
5UYLelectron microscopy3.60F1-100[»]
5UYMelectron microscopy3.20F1-100[»]
5UYNelectron microscopy4.00F1-100[»]
5UYPelectron microscopy3.90F1-100[»]
5UYQelectron microscopy3.80F1-100[»]
5UZ4electron microscopy5.80F1-131[»]
ProteinModelPortaliP02358.
SMRiP02358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02358.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108ZDX. Bacteria.
COG0360. LUCA.
HOGENOMiHOG000040438.
InParanoidiP02358.
KOiK02990.
PhylomeDBiP02358.

Family and domain databases

CDDicd00473. bS6. 1 hit.
Gene3Di3.30.70.60. 1 hit.
HAMAPiMF_00360. Ribosomal_S6. 1 hit.
InterProiView protein in InterPro
IPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
PANTHERiPTHR21011. PTHR21011. 1 hit.
PfamiView protein in Pfam
PF01250. Ribosomal_S6. 1 hit.
SUPFAMiSSF54995. SSF54995. 1 hit.
TIGRFAMsiTIGR00166. S6. 1 hit.
PROSITEiView protein in PROSITE
PS01048. RIBOSOMAL_S6. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP
60 70 80 90 100
INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS
110 120 130
PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE
Length:135
Mass (Da):15,703
Last modified:July 21, 1986 - v1
Checksum:iF4CC629711C1FD0E
GO

Sequence cautioni

The sequence AAA97096 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence AAC77157 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence BAE78201 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication
The sequence CAA27652 differs from that shown. Up to 4 Glu residues can be added post-translationally.1 Publication

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14Q → T AA sequence (PubMed:9868784).Curated1
Sequence conflicti20G → A AA sequence (PubMed:9868784).Curated1

Mass spectrometryi

Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.
PIRiC65231. R3EC6.
RefSeqiNP_418621.5. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.
GeneIDi948723.
KEGGiecj:JW4158.
eco:b4200.
PATRICifig|511145.12.peg.4332.

Similar proteinsi

Entry informationi

Entry nameiRS6_ECOLI
AccessioniPrimary (citable) accession number: P02358
Secondary accession number(s): Q2M6A5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 27, 2017
This is version 188 of the entry and version 1 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

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