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Protein

30S ribosomal protein S9

Gene

rpsI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER.
ECOL316407:JW3199-MONOMER.
MetaCyc:EG10908-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S9
Gene namesi
Name:rpsI
Ordered Locus Names:b3230, JW3199
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10908. rpsI.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105 – 130Missing : Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro. 1 PublicationAdd BLAST26
Mutagenesisi128 – 130Missing : Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro. 1 Publication3

Chemistry databases

DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.
DB01301. Rolitetracycline.
DB00560. Tigecycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001113542 – 13030S ribosomal protein S9Add BLAST129

Proteomic databases

EPDiP0A7X3.
PaxDbiP0A7X3.
PRIDEiP0A7X3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Cross-links to the P site tRNA and weakly to the A site tRNA.

Protein-protein interaction databases

DIPiDIP-35799N.
IntActiP0A7X3. 148 interactors.
MINTiMINT-1290939.
STRINGi511145.b3230.

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi11 – 14Combined sources4
Beta strandi15 – 24Combined sources10
Beta strandi28 – 30Combined sources3
Helixi35 – 39Combined sources5
Beta strandi40 – 42Combined sources3
Helixi45 – 49Combined sources5
Beta strandi52 – 55Combined sources4
Beta strandi58 – 70Combined sources13
Helixi72 – 86Combined sources15
Helixi87 – 90Combined sources4
Beta strandi92 – 96Combined sources5
Helixi97 – 101Combined sources5
Turni102 – 104Combined sources3
Beta strandi118 – 120Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
3J9Yelectron microscopy3.90i1-130[»]
3J9Zelectron microscopy3.60SI2-130[»]
3JA1electron microscopy3.60SI2-130[»]
3JBUelectron microscopy3.64I1-130[»]
3JBVelectron microscopy3.32I1-130[»]
3JCDelectron microscopy3.70i1-130[»]
3JCEelectron microscopy3.20i1-130[»]
3JCJelectron microscopy3.70o1-130[»]
3JCNelectron microscopy4.60j1-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80AI2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WOIX-ray3.00AI/DI1-130[»]
4WWWX-ray3.10QI/XI4-130[»]
4YBBX-ray2.10AI/BI4-130[»]
5AFIelectron microscopy2.90i1-130[»]
5IQRelectron microscopy3.00n1-130[»]
5IT8X-ray3.12AI/BI4-130[»]
5J5BX-ray2.80AI/BI4-130[»]
5J7LX-ray3.00AI/BI4-130[»]
5J88X-ray3.32AI/BI4-130[»]
5J8AX-ray3.10AI/BI4-130[»]
5J91X-ray2.96AI/BI4-130[»]
5JC9X-ray3.03AI/BI4-130[»]
5JTEelectron microscopy3.60AI1-130[»]
5JU8electron microscopy3.60AI1-130[»]
5KCRelectron microscopy3.601i1-130[»]
5KCSelectron microscopy3.901i1-130[»]
5KPSelectron microscopy3.90141-130[»]
5KPVelectron microscopy4.10131-130[»]
5KPWelectron microscopy3.90131-130[»]
5KPXelectron microscopy3.90131-130[»]
5L3Pelectron microscopy3.70i1-130[»]
ProteinModelPortaliP0A7X3.
SMRiP0A7X3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7X3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Phylogenomic databases

eggNOGiCOG0103. LUCA.
HOGENOMiHOG000019802.
InParanoidiP0A7X3.
KOiK02996.
OMAiIKQGAAR.
PhylomeDBiP0A7X3.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7X3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ
60 70 80 90 100
PLELVDMVEK LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK
110 120 130
AGFVTRDARQ VERKKVGLRK ARRRPQFSKR
Length:130
Mass (Da):14,856
Last modified:January 23, 2007 - v2
Checksum:i757D599168812806
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56D → N AA sequence (PubMed:1091515).Curated1
Sequence conflicti124Missing AA sequence (PubMed:1091515).Curated1
Sequence conflicti126Q → E AA sequence (PubMed:1091515).Curated1

Mass spectrometryi

Molecular mass is 14723.3 Da from positions 2 - 130. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.
PIRiH65114. R3EC9.
RefSeqiNP_417697.1. NC_000913.3.
WP_000829818.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76262; AAC76262; b3230.
BAE77273; BAE77273; BAE77273.
GeneIDi5550578.
949000.
KEGGiecj:JW3199.
eco:b3230.
PATRICi32121886. VBIEscCol129921_3327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.
PIRiH65114. R3EC9.
RefSeqiNP_417697.1. NC_000913.3.
WP_000829818.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
3J9Yelectron microscopy3.90i1-130[»]
3J9Zelectron microscopy3.60SI2-130[»]
3JA1electron microscopy3.60SI2-130[»]
3JBUelectron microscopy3.64I1-130[»]
3JBVelectron microscopy3.32I1-130[»]
3JCDelectron microscopy3.70i1-130[»]
3JCEelectron microscopy3.20i1-130[»]
3JCJelectron microscopy3.70o1-130[»]
3JCNelectron microscopy4.60j1-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80AI2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WOIX-ray3.00AI/DI1-130[»]
4WWWX-ray3.10QI/XI4-130[»]
4YBBX-ray2.10AI/BI4-130[»]
5AFIelectron microscopy2.90i1-130[»]
5IQRelectron microscopy3.00n1-130[»]
5IT8X-ray3.12AI/BI4-130[»]
5J5BX-ray2.80AI/BI4-130[»]
5J7LX-ray3.00AI/BI4-130[»]
5J88X-ray3.32AI/BI4-130[»]
5J8AX-ray3.10AI/BI4-130[»]
5J91X-ray2.96AI/BI4-130[»]
5JC9X-ray3.03AI/BI4-130[»]
5JTEelectron microscopy3.60AI1-130[»]
5JU8electron microscopy3.60AI1-130[»]
5KCRelectron microscopy3.601i1-130[»]
5KCSelectron microscopy3.901i1-130[»]
5KPSelectron microscopy3.90141-130[»]
5KPVelectron microscopy4.10131-130[»]
5KPWelectron microscopy3.90131-130[»]
5KPXelectron microscopy3.90131-130[»]
5L3Pelectron microscopy3.70i1-130[»]
ProteinModelPortaliP0A7X3.
SMRiP0A7X3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35799N.
IntActiP0A7X3. 148 interactors.
MINTiMINT-1290939.
STRINGi511145.b3230.

Chemistry databases

DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.
DB01301. Rolitetracycline.
DB00560. Tigecycline.

Proteomic databases

EPDiP0A7X3.
PaxDbiP0A7X3.
PRIDEiP0A7X3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76262; AAC76262; b3230.
BAE77273; BAE77273; BAE77273.
GeneIDi5550578.
949000.
KEGGiecj:JW3199.
eco:b3230.
PATRICi32121886. VBIEscCol129921_3327.

Organism-specific databases

EchoBASEiEB0901.
EcoGeneiEG10908. rpsI.

Phylogenomic databases

eggNOGiCOG0103. LUCA.
HOGENOMiHOG000019802.
InParanoidiP0A7X3.
KOiK02996.
OMAiIKQGAAR.
PhylomeDBiP0A7X3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER.
ECOL316407:JW3199-MONOMER.
MetaCyc:EG10908-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7X3.
PROiP0A7X3.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS9_ECOLI
AccessioniPrimary (citable) accession number: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 121 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.