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Protein

30S ribosomal protein S15

Gene

rpsO

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

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (PubMed:12809609, PubMed:16272117). Binds to its own mRNA, stabilizing it 5-UTR and preventing its translation (PubMed:24339747).3 Publications
In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations.3 Publications

GO - Molecular functioni

  • rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • mRNA polyadenylation Source: EcoliWiki
  • regulation of translation Source: UniProtKB-KW
  • ribosomal small subunit assembly Source: CAFA
  • translation Source: InterPro

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
Biological processTranslation regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG10914-MONOMER
MetaCyc:EG10914-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S15UniRule annotation
Alternative name(s):
Small ribosomal subunit protein uS151 Publication
Gene namesi
Name:rpsOUniRule annotation
Synonyms:secC
Ordered Locus Names:b3165, JW3134
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10914 rpsO

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001154372 – 8930S ribosomal protein S15Add BLAST88

Proteomic databases

EPDiP0ADZ4
PaxDbiP0ADZ4
PRIDEiP0ADZ4

Expressioni

Inductioni

Part of the metY operon that extends to pnp, also has its own promoter (PubMed:2849753).1 Publication

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:776686, PubMed:10094780, PubMed:12244297, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:27906160, PubMed:27906161). Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA (PubMed:12809609, PubMed:16272117).8 Publications

Protein-protein interaction databases

DIPiDIP-47909N
IntActiP0ADZ4 30 interactors.
STRINGi316385.ECDH10B_3339

Structurei

Secondary structure

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Beta strandi16 – 18Combined sources3
Helixi25 – 44Combined sources20
Helixi50 – 73Combined sources24
Helixi75 – 85Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50F1-89[»]
2VAZelectron microscopy10.00F2-89[»]
2YKRelectron microscopy9.80O2-89[»]
3J9Yelectron microscopy3.90o1-89[»]
3J9Zelectron microscopy3.60SO2-89[»]
3JA1electron microscopy3.60SO2-89[»]
3JBUelectron microscopy3.64O1-89[»]
3JBVelectron microscopy3.32O1-89[»]
3JCDelectron microscopy3.70o1-89[»]
3JCEelectron microscopy3.20o1-89[»]
3JCJelectron microscopy3.70u1-89[»]
3JCNelectron microscopy4.60p1-89[»]
4A2Ielectron microscopy16.50O2-89[»]
4ADVelectron microscopy13.50O1-89[»]
4U1UX-ray2.95AO/CO2-89[»]
4U1VX-ray3.00AO/CO2-89[»]
4U20X-ray2.90AO/CO2-89[»]
4U24X-ray2.90AO/CO2-89[»]
4U25X-ray2.90AO/CO2-89[»]
4U26X-ray2.80AO/CO2-89[»]
4U27X-ray2.80AO/CO2-89[»]
4V47electron microscopy12.30BO2-89[»]
4V48electron microscopy11.50BO2-89[»]
4V4HX-ray3.46AO/CO1-89[»]
4V4QX-ray3.46AO/CO1-89[»]
4V4Velectron microscopy15.00AO3-88[»]
4V4Welectron microscopy15.00AO3-88[»]
4V50X-ray3.22AO/CO2-89[»]
4V52X-ray3.21AO/CO1-89[»]
4V53X-ray3.54AO/CO1-89[»]
4V54X-ray3.30AO/CO1-89[»]
4V55X-ray4.00AO/CO1-89[»]
4V56X-ray3.93AO/CO1-89[»]
4V57X-ray3.50AO/CO1-89[»]
4V5BX-ray3.74BO/DO1-89[»]
4V5Helectron microscopy5.80AO2-89[»]
4V5YX-ray4.45AO/CO1-89[»]
4V64X-ray3.50AO/CO1-89[»]
4V65electron microscopy9.00AH1-89[»]
4V66electron microscopy9.00AH1-89[»]
4V69electron microscopy6.70AO2-89[»]
4V6CX-ray3.19AO/CO1-89[»]
4V6DX-ray3.81AO/CO1-89[»]
4V6EX-ray3.71AO/CO1-89[»]
4V6Kelectron microscopy8.25BS1-89[»]
4V6Lelectron microscopy13.20AS1-89[»]
4V6Melectron microscopy-O2-89[»]
4V6Nelectron microscopy12.10BR2-89[»]
4V6Oelectron microscopy14.70AR2-89[»]
4V6Pelectron microscopy13.50AR2-89[»]
4V6Qelectron microscopy11.50AR2-89[»]
4V6Relectron microscopy11.50AR2-89[»]
4V6Selectron microscopy13.10BQ2-89[»]
4V6Telectron microscopy8.30AO2-89[»]
4V6Velectron microscopy9.80AO2-89[»]
4V6Yelectron microscopy12.00AO1-89[»]
4V6Zelectron microscopy12.00AO1-89[»]
4V70electron microscopy17.00AO1-89[»]
4V71electron microscopy20.00AO1-89[»]
4V72electron microscopy13.00AO1-89[»]
4V73electron microscopy15.00AO1-89[»]
4V74electron microscopy17.00AO1-89[»]
4V75electron microscopy12.00AO1-89[»]
4V76electron microscopy17.00AO1-89[»]
4V77electron microscopy17.00AO1-89[»]
4V78electron microscopy20.00AO1-89[»]
4V79electron microscopy15.00AO1-89[»]
4V7Aelectron microscopy9.00AO1-89[»]
4V7Belectron microscopy6.80AO1-89[»]
4V7Celectron microscopy7.60AO2-89[»]
4V7Delectron microscopy7.60BO2-89[»]
4V7Ielectron microscopy9.60BO1-89[»]
4V7SX-ray3.25AO/CO2-89[»]
4V7TX-ray3.19AO/CO2-89[»]
4V7UX-ray3.10AO/CO2-89[»]
4V7VX-ray3.29AO/CO2-89[»]
4V85X-ray3.20O1-89[»]
4V89X-ray3.70AO1-89[»]
4V9CX-ray3.30AO/CO1-89[»]
4V9DX-ray3.00AO/BO2-89[»]
4V9OX-ray2.90BO/DO/FO/HO1-89[»]
4V9PX-ray2.90BO/DO/FO/HO1-89[»]
4WF1X-ray3.09AO/CO2-89[»]
4WWWX-ray3.10QO/XO2-89[»]
4YBBX-ray2.10AO/BO2-89[»]
5AFIelectron microscopy2.90o1-89[»]
5H5Uelectron microscopy3.00v2-89[»]
5IQRelectron microscopy3.00t1-89[»]
5IT8X-ray3.12AO/BO2-89[»]
5J5BX-ray2.80AO/BO2-89[»]
5J7LX-ray3.00AO/BO2-89[»]
5J88X-ray3.32AO/BO2-89[»]
5J8AX-ray3.10AO/BO2-89[»]
5J91X-ray2.96AO/BO2-89[»]
5JC9X-ray3.03AO/BO2-89[»]
5JTEelectron microscopy3.60AO1-89[»]
5JU8electron microscopy3.60AO1-89[»]
5KCRelectron microscopy3.601o1-89[»]
5KCSelectron microscopy3.901o1-89[»]
5KPSelectron microscopy3.90201-89[»]
5KPVelectron microscopy4.10191-89[»]
5KPWelectron microscopy3.90191-89[»]
5KPXelectron microscopy3.90191-89[»]
5L3Pelectron microscopy3.70o1-89[»]
5LZAelectron microscopy3.60o2-89[»]
5LZBelectron microscopy5.30o2-89[»]
5LZCelectron microscopy4.80o2-89[»]
5LZDelectron microscopy3.40o2-89[»]
5LZEelectron microscopy3.50o2-89[»]
5LZFelectron microscopy4.60o2-89[»]
5MDVelectron microscopy2.97t1-89[»]
5MDWelectron microscopy3.06t1-89[»]
5MDYelectron microscopy3.35t1-89[»]
5MDZelectron microscopy3.10t1-89[»]
5ME0electron microscopy13.50O1-89[»]
5ME1electron microscopy13.50O1-89[»]
5MGPelectron microscopy3.10o2-89[»]
5MY1electron microscopy7.60O1-89[»]
5NO2electron microscopy5.16O2-89[»]
5NO3electron microscopy5.16O2-89[»]
5NO4electron microscopy5.16O2-89[»]
5NP6electron microscopy3.60R2-89[»]
5NWYelectron microscopy2.93E1-89[»]
5O2Relectron microscopy3.40o2-89[»]
5U4Ielectron microscopy3.50o2-89[»]
5U9Felectron microscopy3.20O1-89[»]
5U9Gelectron microscopy3.20O1-89[»]
5UYKelectron microscopy3.90O2-89[»]
5UYLelectron microscopy3.60O2-89[»]
5UYMelectron microscopy3.20O2-89[»]
5UYNelectron microscopy4.00O2-89[»]
5UYPelectron microscopy3.90O2-89[»]
5UYQelectron microscopy3.80O2-89[»]
5UZ4electron microscopy5.80O1-89[»]
6BU8electron microscopy3.50O2-89[»]
6C4Ielectron microscopy3.24o1-89[»]
6ENFelectron microscopy3.20o2-89[»]
6ENJelectron microscopy3.70o2-89[»]
6ENUelectron microscopy3.10o2-89[»]
ProteinModelPortaliP0ADZ4
SMRiP0ADZ4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADZ4

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uS15 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105K77 Bacteria
COG0184 LUCA
HOGENOMiHOG000040097
InParanoidiP0ADZ4
KOiK02956
OMAiFKTHVKD
PhylomeDBiP0ADZ4

Family and domain databases

CDDicd00353 Ribosomal_S15p_S13e, 1 hit
HAMAPiMF_01343_B Ribosomal_S15_B, 1 hit
InterProiView protein in InterPro
IPR000589 Ribosomal_S15
IPR005290 Ribosomal_S15_bac-type
IPR009068 S15_NS1_RNA-bd
PANTHERiPTHR23321 PTHR23321, 1 hit
PfamiView protein in Pfam
PF00312 Ribosomal_S15, 1 hit
SMARTiView protein in SMART
SM01387 Ribosomal_S15, 1 hit
SUPFAMiSSF47060 SSF47060, 1 hit
TIGRFAMsiTIGR00952 S15_bact, 1 hit
PROSITEiView protein in PROSITE
PS00362 RIBOSOMAL_S15, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0ADZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH
60 70 80
HSRRGLLRMV SQRRKLLDYL KRKDVARYTQ LIERLGLRR
Length:89
Mass (Da):10,269
Last modified:January 23, 2007 - v2
Checksum:iAABDDA6674B99B1C
GO

Mass spectrometryi

Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01073 Genomic DNA Translation: CAA25536.1
X00761 Genomic DNA Translation: CAA25331.1
M14425 Genomic DNA Translation: AAA24595.1
J02638 Genomic DNA Translation: AAA83904.1
U18997 Genomic DNA Translation: AAA57968.1
U00096 Genomic DNA Translation: AAC76199.1
AP009048 Genomic DNA Translation: BAE77211.1
X13775 Genomic DNA Translation: CAA32022.1
PIRiB26118 R3EC15
RefSeqiNP_417634.1, NC_000913.3
WP_000059466.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76199; AAC76199; b3165
BAE77211; BAE77211; BAE77211
GeneIDi947686
KEGGiecj:JW3134
eco:b3165
PATRICifig|1411691.4.peg.3565

Similar proteinsi

Entry informationi

Entry nameiRS15_ECOLI
AccessioniPrimary (citable) accession number: P0ADZ4
Secondary accession number(s): P02371, Q2M945
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 119 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