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Protein

30S ribosomal protein S1

Gene

rpsA

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

Functioni

Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5'-UTR structure, thus it may help fine-tune which mRNAs that are translated (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides (PubMed:22908248). Has a preference for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its own translation (PubMed:2120211).10 Publications
It is not clear if it plays a role in trans-translation (a process which rescues stalled ribosomes). Evidence for its role; binds to tmRNA with very high affinity, is required for binding of tmRNA to 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role only in translation of the tmRNA in vitro (PubMed:17392345). Evidence against its role; overexpression of whole protein or various S1 fragments inhibits translation, they have no effect on trans-translation, and an in vitro system with S1-less ribosomes performs trans-translation (PubMed:15340139, PubMed:17376482). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the "tag peptide" encoded by the tmRNA and thus targeted for degradation.4 Publications
In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex; this subunit is required for RNA replication initiation activity during synthesis of (-) strand RNA from the (+) strand genomic RNA but not for (+) strand synthesis from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an approximately 70 mucleotide RNA internal to the viral replicase gene (the M-site) (PubMed:25122749). Others have reported it is not involved in RNA replication initiation but rather in termination of RNA synthesis and is required for termination whether it is the (+) or (-) strand that is being synthesized (PubMed:23653193).4 Publications
In case of infection by bacteriophage T4, plays a significant role in substrate choice by viral endoribonuclease RegB.1 Publication

GO - Molecular functioni

  • mRNA binding Source: EcoCyc
  • RNA binding Source: EcoCyc
  • structural constituent of ribosome Source: EcoCyc

GO - Biological processi

  • negative regulation of cytoplasmic translation Source: EcoCyc
  • translation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10900-MONOMER.
ECOL316407:JW0894-MONOMER.
MetaCyc:EG10900-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S1
Alternative name(s):
Bacteriophage Q beta RNA-directed RNA polymerase subunit I1 Publication
Gene namesi
Name:rpsA
Synonyms:ssyF
Ordered Locus Names:b0911, JW0894
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10900. rpsA.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosolic small ribosomal subunit Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted. Upon depletion cell growth and total protein synthesis become linear.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi205Y → A: Decreased binding of Q beta-derived M-site RNA, 80% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi208F → A: Decreased binding of Q beta-derived M-site RNA, 50% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi219H → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1
Mutagenesisi254R → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001960331 – 55730S ribosomal protein S1Add BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei229N6-acetyllysine1 Publication1
Modified residuei279N6-acetyllysine1 Publication1
Modified residuei363N6-acetyllysine1 Publication1

Post-translational modificationi

Phosphorylated; probably on a serine.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP0AG67.
PaxDbiP0AG67.
PRIDEiP0AG67.

2D gel databases

SWISS-2DPAGEP0AG67.

Expressioni

Inductioni

Represses its own translation via the N-terminus (at protein level).1 Publication

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit; the largest protein subunit, it is loosely associated and rarely found in ribosomal crystal structures (PubMed:7041110, PubMed:7003157, PubMed:778845, PubMed:342903). Does not bind rRNA. Probably requires ribosomal protein S2 to associate with the 30S subunit (PubMed:12068815). Binds in the junction of the head, platform and main body of the 30S subunit; the N-terminus penetrates the 30S subunit while the C-terminus faces ribosomal protein S2 (PubMed:11593008). Nascent polypeptide chains cross-link this protein in situ (PubMed:9716382). Can be cross-linked to mRNA in the ribosome (PubMed:1712292). In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host EF-Tu and EF-Ts (PubMed:816798, PubMed:6358207, PubMed:25122749).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-546520,EBI-546520

Protein-protein interaction databases

BioGridi4263060. 145 interactors.
849910. 1 interactor.
DIPiDIP-35884N.
IntActiP0AG67. 80 interactors.
MINTiMINT-1315122.
STRINGi511145.b0911.

Structurei

Secondary structure

1557
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Beta strandi21 – 31Combined sources11
Beta strandi36 – 39Combined sources4
Beta strandi41 – 44Combined sources4
Beta strandi46 – 48Combined sources3
Beta strandi53 – 56Combined sources4
Turni59 – 61Combined sources3
Beta strandi67 – 71Combined sources5
Helixi79 – 82Combined sources4
Helixi85 – 101Combined sources17
Turni102 – 105Combined sources4
Beta strandi107 – 115Combined sources9
Beta strandi117 – 124Combined sources8
Beta strandi127 – 133Combined sources7
Helixi143 – 145Combined sources3
Turni147 – 149Combined sources3
Beta strandi151 – 159Combined sources9
Beta strandi161 – 163Combined sources3
Beta strandi166 – 170Combined sources5
Helixi171 – 175Combined sources5
Beta strandi279 – 288Combined sources10
Beta strandi291 – 295Combined sources5
Beta strandi301 – 305Combined sources5
Beta strandi308 – 310Combined sources3
Turni319 – 321Combined sources3
Beta strandi327 – 333Combined sources7
Turni337 – 339Combined sources3
Helixi441 – 444Combined sources4
Turni445 – 447Combined sources3
Beta strandi450 – 461Combined sources12
Beta strandi466 – 469Combined sources4
Beta strandi485 – 490Combined sources6
Helixi491 – 493Combined sources3
Beta strandi500 – 509Combined sources10
Turni510 – 513Combined sources4
Beta strandi514 – 518Combined sources5
Beta strandi521 – 524Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BH8X-ray1.90A/B364-398[»]
2KHINMR-A267-361[»]
2KHJNMR-A441-528[»]
4Q7JX-ray2.90D/H1-273[»]
4R71X-ray3.21E/F2-171[»]
ProteinModelPortaliP0AG67.
SMRiP0AG67.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 87S1 motif 1PROSITE-ProRule annotationAdd BLAST67
Domaini105 – 171S1 motif 2PROSITE-ProRule annotationAdd BLAST67
Domaini192 – 260S1 motif 3PROSITE-ProRule annotationAdd BLAST69
Domaini277 – 347S1 motif 4PROSITE-ProRule annotationAdd BLAST71
Domaini364 – 434S1 motif 5PROSITE-ProRule annotationAdd BLAST71
Domaini451 – 520S1 motif 6PROSITE-ProRule annotationAdd BLAST70

Domaini

The 6 S1 motif domains are not equivalent; the first 2 no longer bind rRNA but instead are involved in protein-ribosome and protein-protein interactions. Binds to the 30S ribosomal subunit via its N-terminal fragment (190 residues, the first 2 S1 motifs) and allows translation by S1-free ribosomes (PubMed:7003157, PubMed:15340139). The same fragment represses its own translation (PubMed:2120211). The first 3 S1 motifs do however bind to mRNA pseudoknots in the 5'-UTR of at least 1 mRNA (rpsO); deletion of S1 motifs 1-3 but not motifs 4-6 is not viable, although a deletion of motifs 4-6 grows slowly and is cold-sensitive (PubMed:24339747). In case of infection by bacteriophage Qbeta the same N-terminal fragment is necessary and sufficient to form the Qbeta virus RNA-dependent RNA polymerase, although in vitro (-) strand RNA synthesis from the (+) strand genomic RNA also requires the third S1 motif (residues 1-273) (PubMed:6358207, PubMed:25122749). The third S1 motif is required to bind mRNA, tmRNA and viral M-site RNA but requires cooperation with other S1 motifs (PubMed:15340139, PubMed:25122749).6 Publications

Sequence similaritiesi

Belongs to the ribosomal protein S1P family.Curated
Contains 6 S1 motif domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CAV. Bacteria.
COG0539. LUCA.
HOGENOMiHOG000044052.
InParanoidiP0AG67.
KOiK02945.
OMAiISWDKNV.
PhylomeDBiP0AG67.

Family and domain databases

InterProiIPR012340. NA-bd_OB-fold.
IPR000110. Ribosomal_S1.
IPR022967. S1_dom.
IPR003029. S1_domain.
[Graphical view]
PfamiPF00575. S1. 6 hits.
[Graphical view]
PIRSFiPIRSF002111. RpsA. 1 hit.
PRINTSiPR00681. RIBOSOMALS1.
SMARTiSM00316. S1. 6 hits.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 6 hits.
TIGRFAMsiTIGR00717. rpsA. 1 hit.
PROSITEiPS50126. S1. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AG67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTESFAQLFE ESLKEIETRP GSIVRGVVVA IDKDVVLVDA GLKSESAIPA
60 70 80 90 100
EQFKNAQGEL EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK
110 120 130 140 150
AYEDAETVTG VINGKVKGGF TVELNGIRAF LPGSLVDVRP VRDTLHLEGK
160 170 180 190 200
ELEFKVIKLD QKRNNVVVSR RAVIESENSA ERDQLLENLQ EGMEVKGIVK
210 220 230 240 250
NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE ITVKVLKFDR
260 270 280 290 300
ERTRVSLGLK QLGEDPWVAI AKRYPEGTKL TGRVTNLTDY GCFVEIEEGV
310 320 330 340 350
EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK
360 370 380 390 400
ANPWQQFAET HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNV
410 420 430 440 450
AGEEAVREYK KGDEIAAVVL QVDAERERIS LGVKQLAEDP FNNWVALNKK
460 470 480 490 500
GAIVTGKVTA VDAKGATVEL ADGVEGYLRA SEASRDRVED ATLVLSVGDE
510 520 530 540 550
VEAKFTGVDR KNRAISLSVR AKDEADEKDA IATVNKQEDA NFSNNAMAEA

FKAAKGE
Length:557
Mass (Da):61,158
Last modified:December 20, 2005 - v1
Checksum:i0ABCDEB9E510C267
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti125N → D AA sequence (PubMed:7041110).Curated1
Sequence conflicti181 – 182ER → D in CAA23630 (PubMed:7041110).Curated2
Sequence conflicti181 – 182ER → D in CAA23644 (PubMed:6281725).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00342 Genomic DNA. Translation: CAA23630.1.
V00352 Genomic DNA. Translation: CAA23644.1.
U00096 Genomic DNA. Translation: AAC73997.1.
AP009048 Genomic DNA. Translation: BAA35655.1.
X00785 Genomic DNA. Translation: CAA25361.1.
X04864 Genomic DNA. Translation: CAA28556.1.
PIRiF64830. R3EC1.
RefSeqiNP_415431.1. NC_000913.3.
WP_000140327.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73997; AAC73997; b0911.
BAA35655; BAA35655; BAA35655.
GeneIDi945536.
KEGGiecj:JW0894.
eco:b0911.
PATRICi32117035. VBIEscCol129921_0942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00342 Genomic DNA. Translation: CAA23630.1.
V00352 Genomic DNA. Translation: CAA23644.1.
U00096 Genomic DNA. Translation: AAC73997.1.
AP009048 Genomic DNA. Translation: BAA35655.1.
X00785 Genomic DNA. Translation: CAA25361.1.
X04864 Genomic DNA. Translation: CAA28556.1.
PIRiF64830. R3EC1.
RefSeqiNP_415431.1. NC_000913.3.
WP_000140327.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BH8X-ray1.90A/B364-398[»]
2KHINMR-A267-361[»]
2KHJNMR-A441-528[»]
4Q7JX-ray2.90D/H1-273[»]
4R71X-ray3.21E/F2-171[»]
ProteinModelPortaliP0AG67.
SMRiP0AG67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263060. 145 interactors.
849910. 1 interactor.
DIPiDIP-35884N.
IntActiP0AG67. 80 interactors.
MINTiMINT-1315122.
STRINGi511145.b0911.

2D gel databases

SWISS-2DPAGEP0AG67.

Proteomic databases

EPDiP0AG67.
PaxDbiP0AG67.
PRIDEiP0AG67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73997; AAC73997; b0911.
BAA35655; BAA35655; BAA35655.
GeneIDi945536.
KEGGiecj:JW0894.
eco:b0911.
PATRICi32117035. VBIEscCol129921_0942.

Organism-specific databases

EchoBASEiEB0893.
EcoGeneiEG10900. rpsA.

Phylogenomic databases

eggNOGiENOG4105CAV. Bacteria.
COG0539. LUCA.
HOGENOMiHOG000044052.
InParanoidiP0AG67.
KOiK02945.
OMAiISWDKNV.
PhylomeDBiP0AG67.

Enzyme and pathway databases

BioCyciEcoCyc:EG10900-MONOMER.
ECOL316407:JW0894-MONOMER.
MetaCyc:EG10900-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG67.
PROiP0AG67.

Family and domain databases

InterProiIPR012340. NA-bd_OB-fold.
IPR000110. Ribosomal_S1.
IPR022967. S1_dom.
IPR003029. S1_domain.
[Graphical view]
PfamiPF00575. S1. 6 hits.
[Graphical view]
PIRSFiPIRSF002111. RpsA. 1 hit.
PRINTSiPR00681. RIBOSOMALS1.
SMARTiSM00316. S1. 6 hits.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 6 hits.
TIGRFAMsiTIGR00717. rpsA. 1 hit.
PROSITEiPS50126. S1. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS1_ECOLI
AccessioniPrimary (citable) accession number: P0AG67
Secondary accession number(s): P02349, P77352
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 103 of the entry and version 1 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.