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Protein

30S ribosomal protein S9

Gene

rpsI

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

  • RNA binding Source: GO_Central
  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER.
MetaCyc:EG10908-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S9
Alternative name(s):
Small ribosomal subunit protein uS91 Publication
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

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

PaxDbiP0A7X3.
PRIDEiP0A7X3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:1091515, PubMed:7556101, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts 16S rRNA (PubMed:7556101). Cross-links to the P site tRNA and weakly to the A site tRNA (PubMed:8524654, PubMed:15308780).12 Publications

Protein-protein interaction databases

DIPiDIP-35799N.
IntActiP0A7X3. 151 interactors.
MINTiMINT-1290939.
STRINGi316385.ECDH10B_3407.

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[»]
5H5Uelectron microscopy3.00p2-130[»]
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[»]
5LZAelectron microscopy3.60i4-130[»]
5LZBelectron microscopy5.30i4-130[»]
5LZCelectron microscopy4.80i4-130[»]
5LZDelectron microscopy3.40i4-130[»]
5LZEelectron microscopy3.50i4-130[»]
5LZFelectron microscopy4.60i4-130[»]
5MDVelectron microscopy2.97n1-130[»]
5MDWelectron microscopy3.06n1-130[»]
5MDYelectron microscopy3.35n1-130[»]
5MDZelectron microscopy3.10n1-130[»]
5ME0electron microscopy13.50I1-130[»]
5ME1electron microscopy13.50I1-130[»]
5MGPelectron microscopy3.10i4-130[»]
5MY1electron microscopy7.60I2-130[»]
5NO2electron microscopy5.16I4-130[»]
5NO3electron microscopy5.16I4-130[»]
5NO4electron microscopy5.16I4-130[»]
5NP6electron microscopy3.60L4-130[»]
5NWYelectron microscopy2.9381-130[»]
5O2Relectron microscopy3.40i4-130[»]
5U4Ielectron microscopy3.50i1-130[»]
5U9Felectron microscopy3.20I1-130[»]
5U9Gelectron microscopy3.20I1-130[»]
5UYKelectron microscopy3.90I4-130[»]
5UYLelectron microscopy3.60I4-130[»]
5UYMelectron microscopy3.20I4-130[»]
5UYNelectron microscopy4.00I4-130[»]
5UYPelectron microscopy3.90I4-130[»]
5UYQelectron microscopy3.80I4-130[»]
ProteinModelPortaliP0A7X3.
SMRiP0A7X3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7X3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B. 1 hit.
InterProiView protein in InterPro
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiView protein in Pfam
PF00380. Ribosomal_S9. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiView protein in PROSITE
PS00360. RIBOSOMAL_S9. 1 hit.

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

P0A7X3: 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.
GeneIDi31655915.
949000.
KEGGiecj:JW3199.
eco:b3230.
PATRICifig|1411691.4.peg.3498.

Similar proteinsi

Entry informationi

Entry nameiRS9_ECOLI
AccessioniPrimary (citable) accession number: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 129 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