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Protein

30S ribosomal protein S19

Gene

rpsS

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

Functioni

In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:12859903), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.3 Publications
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA.

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER
MetaCyc:EG10918-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S19
Alternative name(s):
Small ribosomal subunit protein uS191 Publication
Gene namesi
Name:rpsS
Ordered Locus Names:b3316, JW3278
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10918 rpsS

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

DrugBankiDB00759 Tetracycline
DB00560 Tigecycline

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001298192 – 9230S ribosomal protein S19Add BLAST91

Proteomic databases

EPDiP0A7U3
PaxDbiP0A7U3
PRIDEiP0A7U3

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:348496, PubMed:3279034, PubMed:10094780, PubMed:12244297, PubMed:12809609, PubMed:12859903, PubMed:16272117, PubMed:27934701, PubMed:27906160, PubMed:27906161). Binds S13 and L5 and cross-links to the A site tRNA (PubMed:12809609, PubMed:16272117, PubMed:12859903).10 Publications

Protein-protein interaction databases

BioGridi852123, 1 interactor
DIPiDIP-47904N
IntActiP0A7U3, 33 interactors
STRINGi316385.ECDH10B_3491

Structurei

Secondary structure

192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi13 – 20Combined sources8
Turni21 – 25Combined sources5
Beta strandi29 – 33Combined sources5
Beta strandi37 – 39Combined sources3
Helixi42 – 44Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi54 – 61Combined sources8
Helixi64 – 66Combined sources3
Beta strandi67 – 70Combined sources4
Helixi71 – 74Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-S3-81[»]
2YKRelectron microscopy9.80S3-81[»]
3J9Yelectron microscopy3.90s1-92[»]
3J9Zelectron microscopy3.60SS2-92[»]
3JA1electron microscopy3.60SS2-92[»]
3JBUelectron microscopy3.64S1-92[»]
3JBVelectron microscopy3.32S1-92[»]
3JCDelectron microscopy3.70s1-92[»]
3JCEelectron microscopy3.20s1-92[»]
3JCJelectron microscopy3.70z1-92[»]
3JCNelectron microscopy4.60t1-92[»]
4A2Ielectron microscopy16.50S3-81[»]
4ADVelectron microscopy13.50S2-92[»]
4U1UX-ray2.95AS/CS3-81[»]
4U1VX-ray3.00AS/CS3-81[»]
4U20X-ray2.90AS/CS3-81[»]
4U24X-ray2.90AS/CS3-81[»]
4U25X-ray2.90AS/CS3-81[»]
4U26X-ray2.80AS/CS3-81[»]
4U27X-ray2.80AS/CS3-81[»]
4V47electron microscopy12.30BS2-92[»]
4V48electron microscopy11.50BS2-92[»]
4V4HX-ray3.46AS/CS1-92[»]
4V4QX-ray3.46AS/CS2-92[»]
4V4Velectron microscopy15.00AS2-88[»]
4V4Welectron microscopy15.00AS2-88[»]
4V50X-ray3.22AS/CS2-92[»]
4V52X-ray3.21AS/CS2-92[»]
4V53X-ray3.54AS/CS2-92[»]
4V54X-ray3.30AS/CS2-92[»]
4V55X-ray4.00AS/CS2-92[»]
4V56X-ray3.93AS/CS2-92[»]
4V57X-ray3.50AS/CS2-92[»]
4V5BX-ray3.74BS/DS2-92[»]
4V5Helectron microscopy5.80AS3-81[»]
4V5YX-ray4.45AS/CS2-92[»]
4V64X-ray3.50AS/CS2-92[»]
4V65electron microscopy9.00AL1-92[»]
4V66electron microscopy9.00AL1-92[»]
4V69electron microscopy6.70AS3-81[»]
4V6CX-ray3.19AS/CS1-92[»]
4V6DX-ray3.81AS/CS1-92[»]
4V6EX-ray3.71AS/CS1-92[»]
4V6Kelectron microscopy8.25BW1-92[»]
4V6Lelectron microscopy13.20AW1-92[»]
4V6Melectron microscopy7.10AS2-92[»]
4V6Nelectron microscopy12.10BV2-92[»]
4V6Oelectron microscopy14.70AV2-92[»]
4V6Pelectron microscopy13.50AV2-92[»]
4V6Qelectron microscopy11.50AV2-92[»]
4V6Relectron microscopy11.50AV2-92[»]
4V6Selectron microscopy13.10BU2-92[»]
4V6Telectron microscopy8.30AS3-81[»]
4V6Velectron microscopy9.80AS2-92[»]
4V6Yelectron microscopy12.00AS3-81[»]
4V6Zelectron microscopy12.00AS3-81[»]
4V70electron microscopy17.00AS3-81[»]
4V71electron microscopy20.00AS3-81[»]
4V72electron microscopy13.00AS3-81[»]
4V73electron microscopy15.00AS3-81[»]
4V74electron microscopy17.00AS3-81[»]
4V75electron microscopy12.00AS3-81[»]
4V76electron microscopy17.00AS3-81[»]
4V77electron microscopy17.00AS3-81[»]
4V78electron microscopy20.00AS3-81[»]
4V79electron microscopy15.00AS3-81[»]
4V7Aelectron microscopy9.00AS3-81[»]
4V7Belectron microscopy6.80AS1-92[»]
4V7Celectron microscopy7.60AS2-92[»]
4V7Delectron microscopy7.60BS2-92[»]
4V7Ielectron microscopy9.60BS1-92[»]
4V7SX-ray3.25AS/CS3-81[»]
4V7TX-ray3.19AS/CS3-81[»]
4V7UX-ray3.10AS/CS3-81[»]
4V7VX-ray3.29AS/CS3-81[»]
4V85X-ray3.20S1-92[»]
4V89X-ray3.70AS1-92[»]
4V9CX-ray3.30AS/CS1-92[»]
4V9DX-ray3.00AS/BS3-81[»]
4V9OX-ray2.90BS/DS/FS/HS1-92[»]
4V9PX-ray2.90BS/DS/FS/HS1-92[»]
4WF1X-ray3.09AS/CS3-81[»]
4WOIX-ray3.00AS/DS1-92[»]
4WWWX-ray3.10QS/XS3-81[»]
4YBBX-ray2.10AS/BS3-81[»]
5AFIelectron microscopy2.90s1-92[»]
5H5Uelectron microscopy3.00z2-92[»]
5IQRelectron microscopy3.00x1-92[»]
5IT8X-ray3.12AS/BS3-81[»]
5J5BX-ray2.80AS/BS3-81[»]
5J7LX-ray3.00AS/BS3-81[»]
5J88X-ray3.32AS/BS3-81[»]
5J8AX-ray3.10AS/BS3-81[»]
5J91X-ray2.96AS/BS3-81[»]
5JC9X-ray3.03AS/BS3-81[»]
5JTEelectron microscopy3.60AS1-92[»]
5JU8electron microscopy3.60AS1-92[»]
5KCRelectron microscopy3.601s1-92[»]
5KCSelectron microscopy3.901s1-92[»]
5KPSelectron microscopy3.90241-92[»]
5KPVelectron microscopy4.10231-92[»]
5KPWelectron microscopy3.90231-92[»]
5KPXelectron microscopy3.90231-92[»]
5L3Pelectron microscopy3.70s1-92[»]
5LZAelectron microscopy3.60s3-81[»]
5LZBelectron microscopy5.30s3-81[»]
5LZCelectron microscopy4.80s3-81[»]
5LZDelectron microscopy3.40s3-88[»]
5LZEelectron microscopy3.50s3-81[»]
5LZFelectron microscopy4.60s3-88[»]
5MDVelectron microscopy2.97x1-92[»]
5MDWelectron microscopy3.06x1-92[»]
5MDYelectron microscopy3.35x1-92[»]
5MDZelectron microscopy3.10x1-92[»]
5ME0electron microscopy13.50S1-92[»]
5ME1electron microscopy13.50S1-92[»]
5MGPelectron microscopy3.10s3-81[»]
5MY1electron microscopy7.60S2-92[»]
5NO2electron microscopy5.16S3-81[»]
5NO3electron microscopy5.16S3-81[»]
5NO4electron microscopy5.16S3-81[»]
5NP6electron microscopy3.60V3-81[»]
5NWYelectron microscopy2.93I1-92[»]
5O2Relectron microscopy3.40s3-81[»]
5U4Ielectron microscopy3.50s2-83[»]
5U9Felectron microscopy3.20S1-92[»]
5U9Gelectron microscopy3.20S1-92[»]
5UYKelectron microscopy3.90S3-81[»]
5UYLelectron microscopy3.60S3-81[»]
5UYMelectron microscopy3.20S3-81[»]
5UYNelectron microscopy4.00S3-81[»]
5UYPelectron microscopy3.90S3-81[»]
5UYQelectron microscopy3.80S3-81[»]
5UZ4electron microscopy5.80S1-92[»]
5WDTelectron microscopy3.00s3-81[»]
5WE4electron microscopy3.10s3-81[»]
5WE6electron microscopy3.40s3-81[»]
5WFKelectron microscopy3.40s3-81[»]
6BU8electron microscopy3.50S3-81[»]
6ENFelectron microscopy3.20s3-81[»]
6ENJelectron microscopy3.70s3-81[»]
6ENUelectron microscopy3.10s3-81[»]
DisProtiDP00147
ProteinModelPortaliP0A7U3
SMRiP0A7U3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U3

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0185 LUCA
HOGENOMiHOG000111560
InParanoidiP0A7U3
KOiK02965
OMAiVHNGRQF
PhylomeDBiP0A7U3

Family and domain databases

Gene3Di3.30.860.10, 1 hit
HAMAPiMF_00531 Ribosomal_S19, 1 hit
InterProiView protein in InterPro
IPR002222 Ribosomal_S19
IPR005732 Ribosomal_S19_bac-type
IPR020934 Ribosomal_S19_CS
IPR023575 Ribosomal_S19_SF
PANTHERiPTHR11880 PTHR11880, 1 hit
PfamiView protein in Pfam
PF00203 Ribosomal_S19, 1 hit
PIRSFiPIRSF002144 Ribosomal_S19, 1 hit
PRINTSiPR00975 RIBOSOMALS19
SUPFAMiSSF54570 SSF54570, 1 hit
TIGRFAMsiTIGR01050 rpsS_bact, 1 hit
PROSITEiView protein in PROSITE
PS00323 RIBOSOMAL_S19, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A7U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA
60 70 80 90
VHNGRQHVPV FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK
Length:92
Mass (Da):10,430
Last modified:January 23, 2007 - v2
Checksum:i439F951848E95CB8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37 – 43RSTIFPN → STIFPDR AA sequence (PubMed:348496).Curated7
Sequence conflicti86D → N AA sequence (PubMed:348496).Curated1

Mass spectrometryi

Molecular mass is 10299.6 Da from positions 2 - 92. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti83H → Y in MW145; suppresses a rimM deletion. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26464.1
U18997 Genomic DNA Translation: AAA58113.1
U00096 Genomic DNA Translation: AAC76341.1
AP009048 Genomic DNA Translation: BAE77975.1
PIRiF23129 R3EC19
RefSeqiNP_417775.1, NC_000913.3
WP_001138117.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76341; AAC76341; b3316
BAE77975; BAE77975; BAE77975
GeneIDi34152300
947811
KEGGiecj:JW3278
eco:b3316
PATRICifig|1411691.4.peg.3415

Similar proteinsi

Entry informationi

Entry nameiRS19_ECOLI
AccessioniPrimary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 134 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. 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

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