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Protein

30S ribosomal protein S19

Gene

rpsS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.
MetaCyc:EG10918-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S19
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
Complete GO annotation...

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. Binds S13 and L5 and cross-links to the A site tRNA.

Protein-protein interaction databases

BioGridi852123. 1 interactor.
DIPiDIP-47904N.
IntActiP0A7U3. 30 interactors.
STRINGi511145.b3316.

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[»]
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[»]
DisProtiDP00147.
ProteinModelPortaliP0A7U3.
SMRiP0A7U3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19P family.Curated

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.
InterProiIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01050. rpsS_bact. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

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

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.
GeneIDi947811.
KEGGiecj:JW3278.
eco:b3316.
PATRICi32122064. VBIEscCol129921_3409.

Cross-referencesi

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.

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[»]
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[»]
DisProtiDP00147.
ProteinModelPortaliP0A7U3.
SMRiP0A7U3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852123. 1 interactor.
DIPiDIP-47904N.
IntActiP0A7U3. 30 interactors.
STRINGi511145.b3316.

Chemistry databases

DrugBankiDB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

EPDiP0A7U3.
PaxDbiP0A7U3.
PRIDEiP0A7U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.
GeneIDi947811.
KEGGiecj:JW3278.
eco:b3316.
PATRICi32122064. VBIEscCol129921_3409.

Organism-specific databases

EchoBASEiEB0911.
EcoGeneiEG10918. rpsS.

Phylogenomic databases

eggNOGiCOG0185. LUCA.
HOGENOMiHOG000111560.
InParanoidiP0A7U3.
KOiK02965.
OMAiVHNGRQF.
PhylomeDBiP0A7U3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.
MetaCyc:EG10918-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7U3.
PROiP0A7U3.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19. 1 hit.
InterProiIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01050. rpsS_bact. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS19_ECOLI
AccessioniPrimary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 123 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.