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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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051Y → A: Decreased binding of Q beta-derived M-site RNA, 80% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication
Mutagenesisi208 – 2081F → A: Decreased binding of Q beta-derived M-site RNA, 50% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication
Mutagenesisi219 – 2191H → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication
Mutagenesisi254 – 2541R → A: Decreased binding of Q beta-derived M-site RNA, 40% synthesis of (-) strand RNA, in construct expressing residues 1-273. 1 Publication

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 55755730S ribosomal protein S1PRO_0000196033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291N6-acetyllysine1 Publication
Modified residuei279 – 2791N6-acetyllysine1 Publication
Modified residuei363 – 3631N6-acetyllysine1 Publication

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 interactions.
849910. 1 interaction.
DIPiDIP-35884N.
IntActiP0AG67. 80 interactions.
MINTiMINT-1315122.
STRINGi511145.b0911.

Structurei

Secondary structure

1
557
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi21 – 3111Combined sources
Beta strandi36 – 394Combined sources
Beta strandi41 – 444Combined sources
Beta strandi46 – 483Combined sources
Beta strandi53 – 564Combined sources
Turni59 – 613Combined sources
Beta strandi67 – 715Combined sources
Helixi79 – 824Combined sources
Helixi85 – 10117Combined sources
Turni102 – 1054Combined sources
Beta strandi107 – 1159Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi127 – 1337Combined sources
Helixi143 – 1453Combined sources
Turni147 – 1493Combined sources
Beta strandi151 – 1599Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi166 – 1705Combined sources
Helixi171 – 1755Combined sources
Beta strandi279 – 28810Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi308 – 3103Combined sources
Turni319 – 3213Combined sources
Beta strandi327 – 3337Combined sources
Turni337 – 3393Combined sources
Helixi441 – 4444Combined sources
Turni445 – 4473Combined sources
Beta strandi450 – 46112Combined sources
Beta strandi466 – 4694Combined sources
Beta strandi485 – 4906Combined sources
Helixi491 – 4933Combined sources
Beta strandi500 – 50910Combined sources
Turni510 – 5134Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi521 – 5244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-178, 191-439, 441-528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 8767S1 motif 1PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 17167S1 motif 2PROSITE-ProRule annotationAdd
BLAST
Domaini192 – 26069S1 motif 3PROSITE-ProRule annotationAdd
BLAST
Domaini277 – 34771S1 motif 4PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 43471S1 motif 5PROSITE-ProRule annotationAdd
BLAST
Domaini451 – 52070S1 motif 6PROSITE-ProRule annotationAdd
BLAST

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.
OrthoDBiEOG6WT8CC.
PhylomeDBiP0AG67.

Family and domain databases

Gene3Di2.40.50.140. 6 hits.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251N → D AA sequence (PubMed:7041110).Curated
Sequence conflicti181 – 1822ER → D in CAA23630 (PubMed:7041110).Curated
Sequence conflicti181 – 1822ER → D in CAA23644 (PubMed:6281725).Curated

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
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. Positions 2-178, 191-439, 441-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263060. 145 interactions.
849910. 1 interaction.
DIPiDIP-35884N.
IntActiP0AG67. 80 interactions.
MINTiMINT-1315122.
STRINGi511145.b0911.

Chemistry

ChEMBLiCHEMBL2363135.

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.
OrthoDBiEOG6WT8CC.
PhylomeDBiP0AG67.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AG67.
PROiP0AG67.

Family and domain databases

Gene3Di2.40.50.140. 6 hits.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of Escherichia coli ribosomal protein S1 and of its gene rpsA."
    Schnier J., Kimura M., Foulaki K., Subramanian A.R., Isono K., Wittmann-Liebold B.
    Proc. Natl. Acad. Sci. U.S.A. 79:1008-1011(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, SUBUNIT.
    Strain: K12 / JS6.5 and MRE-600.
  2. "The DNA sequence of the gene rpsA of Escherichia coli coding for ribosomal protein S1."
    Schnier J., Isono K.
    Nucleic Acids Res. 10:1857-1865(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / JS6.5.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Transcriptional organization of the rpsA operon of Escherichia coli."
    Pedersen S., Skouv J., Kajitani M., Ishihama A.
    Mol. Gen. Genet. 196:135-140(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
  7. "The major ribosome binding site of Escherichia coli ribosomal protein S1 is located in its N-terminal segment."
    Giorginis S., Subramanian A.R.
    J. Mol. Biol. 141:393-408(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-6 AND 332-334, FUNCTION, SUBUNIT, DOMAIN.
    Strain: MRE600.
  8. Bienvenut W.V., Barblan J., Quadroni M.
    Submitted (JAN-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 118-128, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Primary structure of the hip gene of Escherichia coli and of its product, the beta subunit of integration host factor."
    Flamm E., Weisberg R.A.
    J. Mol. Biol. 183:117-128(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-557.
    Strain: K12.
  10. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / EMG2.
  11. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  12. "Alteration of polynucleotide secondary structure by ribosomal protein S1."
    Bear D.G., Ng R., Van Derveer D., Johnson N.P., Thomas G., Schleich T., Noller H.F.
    Proc. Natl. Acad. Sci. U.S.A. 73:1824-1828(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, RNA-BINDING.
    Strain: Q13.
  13. "Immunochemical analysis of the functions of the subunits of phage Qbeta ribonucleic acid replicase."
    Carmichael G.G., Landers T.A., Weber K.
    J. Biol. Chem. 251:2744-2748(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN QBETA VIRAL RNA REPLICATION, SUBUNIT.
  14. "Exchange of individual ribosomal proteins between ribosomes as studied by heavy isotope-transfer experiments."
    Subramanian A.R., van Duin J.
    Mol. Gen. Genet. 158:1-9(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: MRE600.
  15. "The activity of discrete fragments of ribosomal protein S1 in Q beta replicase function."
    Guerrier-Takada C., Subramanian A.R., Cole P.E.
    J. Biol. Chem. 258:13649-13652(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN QBETA VIRAL RNA REPLICATION, SUBUNIT, DOMAIN.
  16. "Ribosomal protein S1 of Escherichia coli is the effector for the regulation of its own synthesis."
    Skouv J., Schnier J., Rasmussen M.D., Subramanian A.R., Pedersen S.
    J. Biol. Chem. 265:17044-17049(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DOMAIN.
  17. "The path of mRNA through the Escherichia coli ribosome; site-directed cross-linking of mRNA analogues carrying a photo-reactive label at various points 3' to the decoding site."
    Rinke-Appel J., Juenke N., Stade K., Brimacombe R.
    EMBO J. 10:2195-2202(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, CROSS-LINKING TO MRNA.
  18. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  19. "Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
    Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
    Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
  20. "Identification of phosphoproteins in Escherichia coli."
    Freestone P., Grant S., Toth I., Norris V.
    Mol. Microbiol. 15:573-580(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, PROTEIN SEQUENCE OF 1-13.
  21. "Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo."
    Sorensen M.A., Fricke J., Pedersen S.
    J. Mol. Biol. 280:561-569(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  22. "Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome."
    Wower I.K., Zwieb C.W., Guven S.A., Wower J.
    EMBO J. 19:6612-6621(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TMRNA BINDING.
    Strain: MRE600.
  23. "Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box helicase on translation of leaderless and canonical mRNAs in Escherichia coli."
    Moll I., Grill S., Gruendling A., Blaesi U.
    Mol. Microbiol. 44:1387-1396(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  24. "Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules."
    McGinness K.E., Sauer R.T.
    Proc. Natl. Acad. Sci. U.S.A. 101:13454-13459(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, TMRNA BINDING, MRNA BINDING.
    Strain: X90.
  25. "Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence."
    Durand S., Richard G., Bisaglia M., Laalami S., Bontems F., Uzan M.
    Nucleic Acids Res. 34:6549-6560(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T4 VIRUS REGB ACTIVATION.
  26. "Ribosomal protein S1 is not essential for the trans-translation machinery."
    Qi H., Shimizu Y., Ueda T.
    J. Mol. Biol. 368:845-852(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF FUNCTION IN TRANS-TRANSLATION.
  27. "Ribosomal protein S1 influences trans-translation in vitro and in vivo."
    Saguy M., Gillet R., Skorski P., Hermann-Le Denmat S., Felden B.
    Nucleic Acids Res. 35:2368-2376(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANS-TRANSLATION.
  28. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229; LYS-279 AND LYS-363, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  29. "Ribosomal protein S1 unwinds double-stranded RNA in multiple steps."
    Qu X., Lancaster L., Noller H.F., Bustamante C., Tinoco I. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 109:14458-14463(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UNWINDING DSRNA, RNA-BINDING.
  30. "Ribosomal protein S1 functions as a termination factor in RNA synthesis by Qbeta phage replicase."
    Vasilyev N.N., Kutlubaeva Z.S., Ugarov V.I., Chetverina H.V., Chetverin A.B.
    Nat. Commun. 4:1781-1781(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN QBETA VIRAL RNA REPLICATION, RNA-BINDING.
  31. "Escherichia coli ribosomal protein S1 unfolds structured mRNAs onto the ribosome for active translation initiation."
    Duval M., Korepanov A., Fuchsbauer O., Fechter P., Haller A., Fabbretti A., Choulier L., Micura R., Klaholz B.P., Romby P., Springer M., Marzi S.
    PLoS Biol. 11:E1001731-E1001731(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RIBOSOME CHAPERONE, DOMAIN, MRNA-BINDING.
  32. "Multiple activities of RNA-binding proteins S1 and Hfq."
    Hajnsdorf E., Boni I.V.
    Biochimie 94:1544-1553(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  33. "Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA."
    Sengupta J., Agrawal R.K., Frank J.
    Proc. Natl. Acad. Sci. U.S.A. 98:11991-11996(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSITION BY CRYO-ELECTRON MICROSCOPY, SUBUNIT.
  34. "Probing the relationship between Gram-negative and Gram-positive S1 proteins by sequence analysis."
    Salah P., Bisaglia M., Aliprandi P., Uzan M., Sizun C., Bontems F.
    Nucleic Acids Res. 37:5578-5588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 267-361 AND OF 441-528, RNA-BINDING.
  35. "Molecular insights into replication initiation by Qbeta replicase using ribosomal protein S1."
    Takeshita D., Yamashita S., Tomita K.
    Nucleic Acids Res. 42:10809-10822(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-273 IN QBETA VIRUS RNA POLYMERASE, FUNCTION IN VIRAL RNA REPLICATION, SUBUNIT, DOMAIN, RNA-BINDING, MUTAGENESIS OF TYR-205; PHE-208; HIS-219 AND ARG-254.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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: April 13, 2016
This is version 100 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.