Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S3

Gene

rpsC

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

Functioni

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity).By similarity
Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

GO - Molecular functioni

  • mRNA binding Source: UniProtKB-UniRule
  • rRNA binding Source: UniProtKB-UniRule
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10902-MONOMER
MetaCyc:EG10902-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S3
Alternative name(s):
Small ribosomal subunit protein uS31 Publication
Gene namesi
Name:rpsC
Ordered Locus Names:b3314, JW3276
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10902 rpsC

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi131 – 135RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome. 1 Publication5

Chemistry databases

DrugBankiDB00759 Tetracycline

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001301132 – 23330S ribosomal protein S3Add BLAST232

Proteomic databases

EPDiP0A7V3
PaxDbiP0A7V3
PRIDEiP0A7V3

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:387449, PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Forms a tight complex with proteins S10 and S14 (By similarity). With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.UniRule annotation10 Publications

Protein-protein interaction databases

BioGridi852126, 1 interactor
DIPiDIP-35807N
IntActiP0A7V3, 194 interactors
MINTiP0A7V3
STRINGi316385.ECDH10B_p1

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A7V3
SMRiP0A7V3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 107KH type-2Add BLAST69

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CKE Bacteria
COG0092 LUCA
HOGENOMiHOG000210610
InParanoidiP0A7V3
KOiK02982
OMAiKTNPIGN
PhylomeDBiP0A7V3

Family and domain databases

Gene3Di3.30.1140.32, 1 hit
3.30.300.20, 1 hit
HAMAPiMF_01309_B Ribosomal_S3_B, 1 hit
InterProiView protein in InterPro
IPR004087 KH_dom
IPR015946 KH_dom-like_a/b
IPR004044 KH_dom_type_2
IPR009019 KH_sf_prok-type
IPR005704 Ribosomal_S3_bac
IPR001351 Ribosomal_S3_C
IPR036419 Ribosomal_S3_C_sf
IPR018280 Ribosomal_S3_CS
PANTHERiPTHR11760:SF19 PTHR11760:SF19, 1 hit
PfamiView protein in Pfam
PF07650 KH_2, 1 hit
PF00189 Ribosomal_S3_C, 1 hit
SMARTiView protein in SMART
SM00322 KH, 1 hit
SUPFAMiSSF54814 SSF54814, 1 hit
SSF54821 SSF54821, 1 hit
TIGRFAMsiTIGR01009 rpsC_bact, 1 hit
PROSITEiView protein in PROSITE
PS50823 KH_TYPE_2, 1 hit
PS00548 RIBOSOMAL_S3, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A7V3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA
60 70 80 90 100
SVSRIVIERP AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ
110 120 130 140 150
INIAEVRKPE LDAKLVADSI TSQLERRVMF RRAMKRAVQN AMRLGAKGIK
160 170 180 190 200
VEVSGRLGGA EIARTEWYRE GRVPLHTLRA DIDYNTSEAH TTYGVIGVKV
210 220 230
WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK
Length:233
Mass (Da):25,983
Last modified:January 23, 2007 - v2
Checksum:i6D0131A285B7AAB3
GO

Mass spectrometryi

Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26466.1
U18997 Genomic DNA Translation: AAA58111.1
U00096 Genomic DNA Translation: AAC76339.1
AP009048 Genomic DNA Translation: BAE77977.1
PIRiH23129 R3EC3
RefSeqiNP_417773.1, NC_000913.3
WP_000529945.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76339; AAC76339; b3314
BAE77977; BAE77977; BAE77977
GeneIDi35808224
947814
KEGGiecj:JW3276
eco:b3314
PATRICifig|1411691.4.peg.3417

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26466.1
U18997 Genomic DNA Translation: AAA58111.1
U00096 Genomic DNA Translation: AAC76339.1
AP009048 Genomic DNA Translation: BAE77977.1
PIRiH23129 R3EC3
RefSeqiNP_417773.1, NC_000913.3
WP_000529945.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-C2-207[»]
2YKRelectron microscopy9.80C2-207[»]
3J9Yelectron microscopy3.90c1-233[»]
3J9Zelectron microscopy3.60SC2-233[»]
3JA1electron microscopy3.60SC2-233[»]
3JBUelectron microscopy3.64C1-233[»]
3JBVelectron microscopy3.32C1-233[»]
3JCDelectron microscopy3.70c1-233[»]
3JCEelectron microscopy3.20c1-233[»]
3JCJelectron microscopy3.70h1-233[»]
3JCNelectron microscopy4.60c1-233[»]
4A2Ielectron microscopy16.50C2-207[»]
4ADVelectron microscopy13.50C2-233[»]
4ODQX-ray2.00B11-25[»]
4U1UX-ray2.95AC/CC2-207[»]
4U1VX-ray3.00AC/CC2-207[»]
4U20X-ray2.90AC/CC2-207[»]
4U24X-ray2.90AC/CC2-207[»]
4U25X-ray2.90AC/CC2-207[»]
4U26X-ray2.80AC/CC2-207[»]
4U27X-ray2.80AC/CC2-207[»]
4V47electron microscopy12.30BC2-233[»]
4V48electron microscopy11.50BC2-233[»]
4V4HX-ray3.46AC/CC1-233[»]
4V4QX-ray3.46AC/CC2-233[»]
4V4Velectron microscopy15.00AC2-207[»]
4V4Welectron microscopy15.00AC2-207[»]
4V50X-ray3.22AC/CC2-233[»]
4V52X-ray3.21AC/CC2-233[»]
4V53X-ray3.54AC/CC2-233[»]
4V54X-ray3.30AC/CC2-233[»]
4V55X-ray4.00AC/CC2-233[»]
4V56X-ray3.93AC/CC2-233[»]
4V57X-ray3.50AC/CC2-233[»]
4V5BX-ray3.74BC/DC2-233[»]
4V5Helectron microscopy5.80AC2-207[»]
4V5YX-ray4.45AC/CC2-233[»]
4V64X-ray3.50AC/CC2-233[»]
4V65electron microscopy9.00AO1-233[»]
4V66electron microscopy9.00AO1-233[»]
4V69electron microscopy6.70AC2-207[»]
4V6CX-ray3.19AC/CC1-233[»]
4V6DX-ray3.81AC/CC1-233[»]
4V6EX-ray3.71AC/CC1-233[»]
4V6Kelectron microscopy8.25BG1-233[»]
4V6Lelectron microscopy13.20AG1-233[»]
4V6Melectron microscopy7.10AC2-233[»]
4V6Nelectron microscopy12.10BF2-233[»]
4V6Oelectron microscopy14.70AF2-233[»]
4V6Pelectron microscopy13.50AF2-233[»]
4V6Qelectron microscopy11.50AF2-233[»]
4V6Relectron microscopy11.50AF2-233[»]
4V6Selectron microscopy13.10BE2-233[»]
4V6Telectron microscopy8.30AC2-207[»]
4V6Velectron microscopy9.80AC2-233[»]
4V6Yelectron microscopy12.00AC1-207[»]
4V6Zelectron microscopy12.00AC1-207[»]
4V70electron microscopy17.00AC1-207[»]
4V71electron microscopy20.00AC1-207[»]
4V72electron microscopy13.00AC1-207[»]
4V73electron microscopy15.00AC1-207[»]
4V74electron microscopy17.00AC1-207[»]
4V75electron microscopy12.00AC1-207[»]
4V76electron microscopy17.00AC1-207[»]
4V77electron microscopy17.00AC1-207[»]
4V78electron microscopy20.00AC1-207[»]
4V79electron microscopy15.00AC1-207[»]
4V7Aelectron microscopy9.00AC1-207[»]
4V7Belectron microscopy6.80AC1-233[»]
4V7Celectron microscopy7.60AC2-233[»]
4V7Delectron microscopy7.60BC2-233[»]
4V7Ielectron microscopy9.60BC1-233[»]
4V7SX-ray3.25AC/CC2-207[»]
4V7TX-ray3.19AC/CC2-207[»]
4V7UX-ray3.10AC/CC2-207[»]
4V7VX-ray3.29AC/CC2-207[»]
4V85X-ray3.20C1-233[»]
4V89X-ray3.70AC1-233[»]
4V9CX-ray3.30AC/CC1-233[»]
4V9DX-ray3.00AC/BC2-207[»]
4V9OX-ray2.90BC/DC/FC/HC1-233[»]
4V9PX-ray2.90BC/DC/FC/HC1-233[»]
4WF1X-ray3.09AC/CC2-207[»]
4WOIX-ray3.00AC/DC1-233[»]
4WWWX-ray3.10QC/XC2-207[»]
4YBBX-ray2.10AC/BC2-207[»]
5AFIelectron microscopy2.90c1-233[»]
5H5Uelectron microscopy3.00j2-233[»]
5IQRelectron microscopy3.00h1-233[»]
5IT8X-ray3.12AC/BC2-207[»]
5J5BX-ray2.80AC/BC2-207[»]
5J7LX-ray3.00AC/BC2-207[»]
5J88X-ray3.32AC/BC2-207[»]
5J8AX-ray3.10AC/BC2-207[»]
5J91X-ray2.96AC/BC2-207[»]
5JC9X-ray3.03AC/BC2-207[»]
5JTEelectron microscopy3.60AC1-233[»]
5JU8electron microscopy3.60AC1-233[»]
5KCRelectron microscopy3.601c1-233[»]
5KCSelectron microscopy3.901c1-233[»]
5KPSelectron microscopy3.9081-233[»]
5KPVelectron microscopy4.1071-233[»]
5KPWelectron microscopy3.9071-233[»]
5KPXelectron microscopy3.9071-233[»]
5L3Pelectron microscopy3.70c1-233[»]
5LZAelectron microscopy3.60c2-207[»]
5LZBelectron microscopy5.30c2-207[»]
5LZCelectron microscopy4.80c2-207[»]
5LZDelectron microscopy3.40c2-207[»]
5LZEelectron microscopy3.50c2-207[»]
5LZFelectron microscopy4.60c2-207[»]
5MDVelectron microscopy2.97h1-233[»]
5MDWelectron microscopy3.06h1-233[»]
5MDYelectron microscopy3.35h1-233[»]
5MDZelectron microscopy3.10h1-233[»]
5ME0electron microscopy13.50C1-233[»]
5ME1electron microscopy13.50C1-233[»]
5MGPelectron microscopy3.10c2-207[»]
5MY1electron microscopy7.60C2-233[»]
5NO4electron microscopy5.16C2-207[»]
5NP6electron microscopy3.60F2-207[»]
5NWYelectron microscopy2.9321-233[»]
5O2Relectron microscopy3.40c2-207[»]
5U4Ielectron microscopy3.50c1-233[»]
5U4Jelectron microscopy3.70c1-233[»]
5U9Felectron microscopy3.20C1-233[»]
5U9Gelectron microscopy3.20C1-233[»]
5UYKelectron microscopy3.90C2-207[»]
5UYLelectron microscopy3.60C2-207[»]
5UYMelectron microscopy3.20C2-207[»]
5UYNelectron microscopy4.00C2-207[»]
5UYPelectron microscopy3.90C2-207[»]
5UYQelectron microscopy3.80C2-207[»]
5UZ4electron microscopy5.80C1-233[»]
5WDTelectron microscopy3.00c2-207[»]
5WE4electron microscopy3.10c2-207[»]
5WE6electron microscopy3.40c2-207[»]
5WFKelectron microscopy3.40c2-207[»]
6BU8electron microscopy3.50C2-207[»]
6C4Ielectron microscopy3.24c1-233[»]
6ENFelectron microscopy3.20c2-207[»]
6ENJelectron microscopy3.70c2-207[»]
6ENUelectron microscopy3.10c2-207[»]
6GWTelectron microscopy3.80c2-207[»]
6GXMelectron microscopy3.80c2-207[»]
6GXNelectron microscopy3.90c2-207[»]
6GXOelectron microscopy3.90c2-207[»]
6GXPelectron microscopy4.40c2-207[»]
ProteinModelPortaliP0A7V3
SMRiP0A7V3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852126, 1 interactor
DIPiDIP-35807N
IntActiP0A7V3, 194 interactors
MINTiP0A7V3
STRINGi316385.ECDH10B_p1

Chemistry databases

DrugBankiDB00759 Tetracycline

Proteomic databases

EPDiP0A7V3
PaxDbiP0A7V3
PRIDEiP0A7V3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76339; AAC76339; b3314
BAE77977; BAE77977; BAE77977
GeneIDi35808224
947814
KEGGiecj:JW3276
eco:b3314
PATRICifig|1411691.4.peg.3417

Organism-specific databases

EchoBASEiEB0895
EcoGeneiEG10902 rpsC

Phylogenomic databases

eggNOGiENOG4105CKE Bacteria
COG0092 LUCA
HOGENOMiHOG000210610
InParanoidiP0A7V3
KOiK02982
OMAiKTNPIGN
PhylomeDBiP0A7V3

Enzyme and pathway databases

BioCyciEcoCyc:EG10902-MONOMER
MetaCyc:EG10902-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7V3
PROiPR:P0A7V3

Family and domain databases

Gene3Di3.30.1140.32, 1 hit
3.30.300.20, 1 hit
HAMAPiMF_01309_B Ribosomal_S3_B, 1 hit
InterProiView protein in InterPro
IPR004087 KH_dom
IPR015946 KH_dom-like_a/b
IPR004044 KH_dom_type_2
IPR009019 KH_sf_prok-type
IPR005704 Ribosomal_S3_bac
IPR001351 Ribosomal_S3_C
IPR036419 Ribosomal_S3_C_sf
IPR018280 Ribosomal_S3_CS
PANTHERiPTHR11760:SF19 PTHR11760:SF19, 1 hit
PfamiView protein in Pfam
PF07650 KH_2, 1 hit
PF00189 Ribosomal_S3_C, 1 hit
SMARTiView protein in SMART
SM00322 KH, 1 hit
SUPFAMiSSF54814 SSF54814, 1 hit
SSF54821 SSF54821, 1 hit
TIGRFAMsiTIGR01009 rpsC_bact, 1 hit
PROSITEiView protein in PROSITE
PS50823 KH_TYPE_2, 1 hit
PS00548 RIBOSOMAL_S3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS3_ECOLI
AccessioniPrimary (citable) accession number: P0A7V3
Secondary accession number(s): P02352, Q2M6X9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 140 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

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again