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Protein

30S ribosomal protein S4

Gene

rpsD

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

Functioni

One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).
Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.
Protein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.
Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase.

GO - Molecular functioni

  1. mRNA 5'-UTR binding Source: EcoCyc
  2. rRNA binding Source: EcoliWiki
  3. structural constituent of ribosome Source: GO_Central
  4. translation repressor activity, nucleic acid binding Source: EcoCyc

GO - Biological processi

  1. DNA-templated transcription, termination Source: UniProtKB-KW
  2. negative regulation of translational initiation Source: EcoCyc
  3. positive regulation of translational fidelity Source: GO_Central
  4. response to antibiotic Source: UniProtKB-KW
  5. transcription antitermination Source: EcoCyc
  6. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation, Transcription termination, Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10903-MONOMER.
ECOL316407:JW3258-MONOMER.

Protein family/group databases

MoonProtiP0A7V8.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S4
Gene namesi
Name:rpsD
Synonyms:ramA
Ordered Locus Names:b3296, JW3258
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10903. rpsD.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 474RKPR → AKPA: Decreases mRNA unwinding ability of the ribosome. 1 Publication

Chemistry

DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 20620530S ribosomal protein S4PRO_0000132380Add
BLAST

Proteomic databases

PaxDbiP0A7V8.
PRIDEiP0A7V8.

Expressioni

Gene expression databases

GenevestigatoriP0A7V8.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts protein S5. With proteins S3 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity. Some nascent polypeptide chains are able to cross-link to this protein in situ.

Protein-protein interaction databases

BioGridi852105. 1 interaction.
DIPiDIP-35794N.
IntActiP0A7V8. 214 interactions.
MINTiMINT-6478162.
STRINGi511145.b3296.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 325Combined sources
Beta strandi34 – 363Combined sources
Beta strandi38 – 414Combined sources
Beta strandi42 – 443Combined sources
Helixi50 – 6516Combined sources
Helixi69 – 8113Combined sources
Beta strandi82 – 843Combined sources
Helixi86 – 9510Combined sources
Helixi98 – 1047Combined sources
Beta strandi107 – 1104Combined sources
Helixi111 – 1199Combined sources
Turni120 – 1223Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi142 – 1443Combined sources
Turni147 – 1515Combined sources
Helixi153 – 16412Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi179 – 1824Combined sources
Helixi188 – 1903Combined sources
Beta strandi193 – 1953Combined sources
Helixi197 – 2037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50A43-200[»]
1M5Gmodel-D2-206[»]
2YKRelectron microscopy9.80D2-206[»]
4A2Ielectron microscopy16.50D2-206[»]
4ADVelectron microscopy13.50D2-206[»]
4U1UX-ray2.95AD/CD2-206[»]
4U1VX-ray3.00AD/CD2-206[»]
4U20X-ray2.90AD/CD2-206[»]
4U24X-ray2.90AD/CD2-206[»]
4U25X-ray2.90AD/CD2-206[»]
4U26X-ray2.80AD/CD2-206[»]
4U27X-ray2.80AD/CD2-206[»]
4V47electron microscopy12.30BD2-206[»]
4V48electron microscopy11.50BD2-206[»]
4V4HX-ray3.46AD/CD1-206[»]
4V4QX-ray3.46AD/CD2-206[»]
4V4Velectron microscopy15.00AD3-206[»]
4V4Welectron microscopy15.00AD3-206[»]
4V50X-ray3.22AD/CD2-206[»]
4V52X-ray3.21AD/CD2-206[»]
4V53X-ray3.54AD/CD2-206[»]
4V54X-ray3.30AD/CD2-206[»]
4V55X-ray4.00AD/CD2-206[»]
4V56X-ray3.93AD/CD2-206[»]
4V57X-ray3.50AD/CD2-206[»]
4V5BX-ray3.74BD/DD2-206[»]
4V5Helectron microscopy5.80AD2-206[»]
4V5YX-ray4.45AD/CD2-206[»]
4V64X-ray3.50AD/CD2-206[»]
4V65electron microscopy9.00AR1-206[»]
4V66electron microscopy9.00AR1-206[»]
4V69electron microscopy6.70AD2-206[»]
4V6CX-ray3.19AD/CD1-206[»]
4V6DX-ray3.81AD/CD1-206[»]
4V6EX-ray3.71AD/CD1-206[»]
4V6Kelectron microscopy8.25BH1-206[»]
4V6Lelectron microscopy13.20AH1-206[»]
4V6Melectron microscopy7.10AD2-206[»]
4V6Nelectron microscopy12.10BG2-206[»]
4V6Oelectron microscopy14.70AG2-206[»]
4V6Pelectron microscopy13.50AG2-206[»]
4V6Qelectron microscopy11.50AG2-206[»]
4V6Relectron microscopy11.50AG2-206[»]
4V6Selectron microscopy13.10BF2-206[»]
4V6Telectron microscopy8.30AD2-206[»]
4V6Velectron microscopy9.80AD2-206[»]
4V6Yelectron microscopy12.00AD1-206[»]
4V6Zelectron microscopy12.00AD1-206[»]
4V70electron microscopy17.00AD1-206[»]
4V71electron microscopy20.00AD1-206[»]
4V72electron microscopy13.00AD1-206[»]
4V73electron microscopy15.00AD1-206[»]
4V74electron microscopy17.00AD1-206[»]
4V75electron microscopy12.00AD1-206[»]
4V76electron microscopy17.00AD1-206[»]
4V77electron microscopy17.00AD1-206[»]
4V78electron microscopy20.00AD1-206[»]
4V79electron microscopy15.00AD1-206[»]
4V7Aelectron microscopy9.00AD1-206[»]
4V7Belectron microscopy6.80AD1-206[»]
4V7Celectron microscopy7.60AD2-206[»]
4V7Delectron microscopy7.60BD2-206[»]
4V7Ielectron microscopy9.60BD1-206[»]
4V7SX-ray3.25AD/CD2-206[»]
4V7TX-ray3.19AD/CD2-206[»]
4V7UX-ray3.10AD/CD2-206[»]
4V7VX-ray3.29AD/CD2-206[»]
4V85X-ray3.20AD1-206[»]
4V89X-ray3.70AD1-206[»]
4V9CX-ray3.30AD/CD1-206[»]
4V9DX-ray3.00AD/BD2-206[»]
4V9OX-ray2.90BD/DD/FD/HD1-206[»]
4V9PX-ray2.90BD/DD/FD/HD1-206[»]
4WF1X-ray3.09AD/CD2-206[»]
4WWWX-ray3.10QD/XD2-206[»]
5AFIelectron microscopy2.90d1-206[»]
ProteinModelPortaliP0A7V8.
SMRiP0A7V8. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 15661S4 RNA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.Curated

Phylogenomic databases

eggNOGiCOG0522.
HOGENOMiHOG000221003.
InParanoidiP0A7V8.
KOiK02986.
OMAiTHGHILV.
OrthoDBiEOG6N3CXM.
PhylomeDBiP0A7V8.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7V8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD
60 70 80 90 100
YGVQLREKQK VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN
110 120 130 140 150
VVYRMGFGAT RAEARQLVSH KAIMVNGRVV NIASYQVSPN DVVSIREKAK
160 170 180 190 200
KQSRVKAALE LAEQREKPTW LEVDAGKMEG TFKRKPERSD LSADINEHLI

VELYSK
Length:206
Mass (Da):23,469
Last modified:January 23, 2007 - v2
Checksum:i4015969DF8E582BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911Missing AA sequence (PubMed:4587210).Curated
Sequence conflicti91 – 911Missing AA sequence (PubMed:1100394).Curated
Sequence conflicti95 – 951E → Q AA sequence (PubMed:4587210).Curated
Sequence conflicti95 – 951E → Q AA sequence (PubMed:1100394).Curated
Sequence conflicti138 – 1447SPNDVVS → DPNSVV AA sequence (PubMed:4587210).Curated
Sequence conflicti138 – 1447SPNDVVS → DPNSVV AA sequence (PubMed:1100394).Curated
Sequence conflicti152 – 1521Q → E AA sequence (PubMed:4587210).Curated
Sequence conflicti152 – 1521Q → E AA sequence (PubMed:1100394).Curated
Sequence conflicti166 – 1661E → Q AA sequence (PubMed:4587210).Curated
Sequence conflicti166 – 1661E → Q AA sequence (PubMed:1100394).Curated

Mass spectrometryi

Molecular mass is 23339.5 Da from positions 2 - 206. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511Y → D in rpsD101; suppresses a temperature-sensitive mutant of release factor 1, R137P. Not a ram mutation.
Natural varianti170 – 20637Missing in rpsD16; suppresses streptomycin dependence in protein S12. A ram mutation.
Add
BLAST
Natural varianti177 – 20630KMEGT…ELYSK → GRYV in rpsD12; suppresses streptomycin dependence in protein S12. A ram mutation.
Add
BLAST
Natural varianti179 – 20628EGTFK…ELYSK → ARYV in rpsD14; suppresses streptomycin dependence in protein S12. A ram mutation.
Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02543 Genomic DNA. Translation: CAA26394.1.
U18997 Genomic DNA. Translation: AAA58094.1.
U00096 Genomic DNA. Translation: AAC76321.1.
AP009048 Genomic DNA. Translation: BAE77995.1.
V00353 Genomic DNA. Translation: CAA23645.1.
J01685 Genomic DNA. Translation: AAA24576.1.
PIRiC23807. R3EC4.
RefSeqiNP_417755.1. NC_000913.3.
YP_492136.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76321; AAC76321; b3296.
BAE77995; BAE77995; BAE77995.
GeneIDi12934394.
947793.
KEGGiecj:Y75_p3880.
eco:b3296.
PATRICi32122024. VBIEscCol129921_3389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02543 Genomic DNA. Translation: CAA26394.1.
U18997 Genomic DNA. Translation: AAA58094.1.
U00096 Genomic DNA. Translation: AAC76321.1.
AP009048 Genomic DNA. Translation: BAE77995.1.
V00353 Genomic DNA. Translation: CAA23645.1.
J01685 Genomic DNA. Translation: AAA24576.1.
PIRiC23807. R3EC4.
RefSeqiNP_417755.1. NC_000913.3.
YP_492136.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50A43-200[»]
1M5Gmodel-D2-206[»]
2YKRelectron microscopy9.80D2-206[»]
4A2Ielectron microscopy16.50D2-206[»]
4ADVelectron microscopy13.50D2-206[»]
4U1UX-ray2.95AD/CD2-206[»]
4U1VX-ray3.00AD/CD2-206[»]
4U20X-ray2.90AD/CD2-206[»]
4U24X-ray2.90AD/CD2-206[»]
4U25X-ray2.90AD/CD2-206[»]
4U26X-ray2.80AD/CD2-206[»]
4U27X-ray2.80AD/CD2-206[»]
4V47electron microscopy12.30BD2-206[»]
4V48electron microscopy11.50BD2-206[»]
4V4HX-ray3.46AD/CD1-206[»]
4V4QX-ray3.46AD/CD2-206[»]
4V4Velectron microscopy15.00AD3-206[»]
4V4Welectron microscopy15.00AD3-206[»]
4V50X-ray3.22AD/CD2-206[»]
4V52X-ray3.21AD/CD2-206[»]
4V53X-ray3.54AD/CD2-206[»]
4V54X-ray3.30AD/CD2-206[»]
4V55X-ray4.00AD/CD2-206[»]
4V56X-ray3.93AD/CD2-206[»]
4V57X-ray3.50AD/CD2-206[»]
4V5BX-ray3.74BD/DD2-206[»]
4V5Helectron microscopy5.80AD2-206[»]
4V5YX-ray4.45AD/CD2-206[»]
4V64X-ray3.50AD/CD2-206[»]
4V65electron microscopy9.00AR1-206[»]
4V66electron microscopy9.00AR1-206[»]
4V69electron microscopy6.70AD2-206[»]
4V6CX-ray3.19AD/CD1-206[»]
4V6DX-ray3.81AD/CD1-206[»]
4V6EX-ray3.71AD/CD1-206[»]
4V6Kelectron microscopy8.25BH1-206[»]
4V6Lelectron microscopy13.20AH1-206[»]
4V6Melectron microscopy7.10AD2-206[»]
4V6Nelectron microscopy12.10BG2-206[»]
4V6Oelectron microscopy14.70AG2-206[»]
4V6Pelectron microscopy13.50AG2-206[»]
4V6Qelectron microscopy11.50AG2-206[»]
4V6Relectron microscopy11.50AG2-206[»]
4V6Selectron microscopy13.10BF2-206[»]
4V6Telectron microscopy8.30AD2-206[»]
4V6Velectron microscopy9.80AD2-206[»]
4V6Yelectron microscopy12.00AD1-206[»]
4V6Zelectron microscopy12.00AD1-206[»]
4V70electron microscopy17.00AD1-206[»]
4V71electron microscopy20.00AD1-206[»]
4V72electron microscopy13.00AD1-206[»]
4V73electron microscopy15.00AD1-206[»]
4V74electron microscopy17.00AD1-206[»]
4V75electron microscopy12.00AD1-206[»]
4V76electron microscopy17.00AD1-206[»]
4V77electron microscopy17.00AD1-206[»]
4V78electron microscopy20.00AD1-206[»]
4V79electron microscopy15.00AD1-206[»]
4V7Aelectron microscopy9.00AD1-206[»]
4V7Belectron microscopy6.80AD1-206[»]
4V7Celectron microscopy7.60AD2-206[»]
4V7Delectron microscopy7.60BD2-206[»]
4V7Ielectron microscopy9.60BD1-206[»]
4V7SX-ray3.25AD/CD2-206[»]
4V7TX-ray3.19AD/CD2-206[»]
4V7UX-ray3.10AD/CD2-206[»]
4V7VX-ray3.29AD/CD2-206[»]
4V85X-ray3.20AD1-206[»]
4V89X-ray3.70AD1-206[»]
4V9CX-ray3.30AD/CD1-206[»]
4V9DX-ray3.00AD/BD2-206[»]
4V9OX-ray2.90BD/DD/FD/HD1-206[»]
4V9PX-ray2.90BD/DD/FD/HD1-206[»]
4WF1X-ray3.09AD/CD2-206[»]
4WWWX-ray3.10QD/XD2-206[»]
5AFIelectron microscopy2.90d1-206[»]
ProteinModelPortaliP0A7V8.
SMRiP0A7V8. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852105. 1 interaction.
DIPiDIP-35794N.
IntActiP0A7V8. 214 interactions.
MINTiMINT-6478162.
STRINGi511145.b3296.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.

Protein family/group databases

MoonProtiP0A7V8.

Proteomic databases

PaxDbiP0A7V8.
PRIDEiP0A7V8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76321; AAC76321; b3296.
BAE77995; BAE77995; BAE77995.
GeneIDi12934394.
947793.
KEGGiecj:Y75_p3880.
eco:b3296.
PATRICi32122024. VBIEscCol129921_3389.

Organism-specific databases

EchoBASEiEB0896.
EcoGeneiEG10903. rpsD.

Phylogenomic databases

eggNOGiCOG0522.
HOGENOMiHOG000221003.
InParanoidiP0A7V8.
KOiK02986.
OMAiTHGHILV.
OrthoDBiEOG6N3CXM.
PhylomeDBiP0A7V8.

Enzyme and pathway databases

BioCyciEcoCyc:EG10903-MONOMER.
ECOL316407:JW3258-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7V8.
PROiP0A7V8.

Gene expression databases

GenevestigatoriP0A7V8.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
    Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
    Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The primary structure of ribosomal protein S4 from Escherichia coli."
    Reinbolt J., Schiltz E.
    FEBS Lett. 36:250-252(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-206.
    Strain: AB774.
  5. "Determination of the complete amino-acid sequence of protein S4 from Escherichia coli ribosomes."
    Schiltz E., Reinbolt J.
    Eur. J. Biochem. 56:467-481(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-206.
    Strain: K.
  6. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 78-91, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  7. Bienvenut W.V., Barblan J., Quadroni M.
    Submitted (JAN-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 84-97 AND 129-146, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Nucleotide sequence of the intercistronic region preceding the gene for RNA polymerase subunit alpha in Escherichia coli."
    Post L.E., Nomura M.
    J. Biol. Chem. 254:10604-10606(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-206.
  9. "Regulation of alpha operon gene expression in Escherichia coli. A novel form of translational coupling."
    Thomas M.S., Bedwell D.M., Nomura M.
    J. Mol. Biol. 196:333-345(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
  10. "Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7."
    Nowotny V., Nierhaus K.H.
    Biochemistry 27:7051-7055(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN SUBUNIT ASSEMBLY.
    Strain: K12 / D10.
  11. "Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA."
    Allen P.N., Noller H.F.
    J. Mol. Biol. 208:457-468(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT OF MUTATIONS ON RRNA FOLDING.
    Strain: UD1A1.
  12. "Messenger RNA recognition by fragments of ribosomal protein S4."
    Baker A.M., Draper D.E.
    J. Biol. Chem. 270:22939-22945(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO MRNA.
  13. "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: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
  14. "A novel mutation in ribosomal protein S4 that affects the function of a mutated RF1."
    Dahlgren A., Ryden-Aulin M.
    Biochimie 82:683-691(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THAT AFFECTS TERMINATION.
    Strain: K12 / MG1655 / ATCC 47076.
  15. "Ribosomal protein S4 is a transcription factor with properties remarkably similar to NusA, a protein involved in both non-ribosomal and ribosomal RNA antitermination."
    Torres M., Condon C., Balada J.-M., Squires C., Squires C.L.
    EMBO J. 20:3811-3820(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: RHO-DEPENDENT RIBOSOMAL RNA ANTITERMINATION FUNCTION.
  16. "mRNA helicase activity of the ribosome."
    Takyar S., Hickerson R.P., Noller H.F.
    Cell 120:49-58(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS.
    Strain: MRE-600.
  17. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  18. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  19. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  20. "Limitations of translational accuracy."
    Kurland C.G., Hughes D., Ehrenberg M.
    (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. (eds.); Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.), pp.979-1004, American Society for Microbiology Press, Washington D.C. (1996)
    Cited for: REVIEW ON TRANSLATIONAL ACCURACY.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS4_ECOLI
AccessioniPrimary (citable) accession number: P0A7V8
Secondary accession number(s): P02354, Q2M6W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 113 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

External Data

Dasty 3

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 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.