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P0A7V8

- RS4_ECOLI

UniProt

P0A7V8 - RS4_ECOLI

Protein

30S ribosomal protein S4

Gene

rpsD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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: InterPro
    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. response to antibiotic Source: UniProtKB-KW
    4. transcription antitermination Source: EcoCyc
    5. translation Source: UniProtKB-HAMAP

    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.

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10903. rpsD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

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

    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 – 157
    Beta strandi20 – 223
    Beta strandi24 – 263
    Beta strandi30 – 323
    Beta strandi34 – 363
    Beta strandi38 – 414
    Beta strandi42 – 443
    Helixi50 – 6516
    Helixi69 – 8113
    Beta strandi82 – 843
    Helixi86 – 9611
    Helixi98 – 1047
    Beta strandi107 – 1104
    Helixi111 – 1199
    Turni120 – 1223
    Beta strandi123 – 1297
    Beta strandi132 – 1343
    Beta strandi142 – 1454
    Helixi147 – 1493
    Helixi153 – 16311
    Turni164 – 1663
    Beta strandi169 – 1724
    Beta strandi175 – 1773
    Beta strandi179 – 1824
    Helixi188 – 1903
    Beta strandi193 – 1953
    Helixi198 – 2058

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50A43-200[»]
    1M5Gmodel-D2-206[»]
    1P6Gelectron microscopy12.30D2-206[»]
    1P87electron microscopy11.50D2-206[»]
    1VS5X-ray3.46D1-206[»]
    1VS7X-ray3.46D1-206[»]
    2AVYX-ray3.46D2-206[»]
    2AW7X-ray3.46D2-206[»]
    2GY9electron microscopy15.00D3-206[»]
    2GYBelectron microscopy15.00D3-206[»]
    2I2PX-ray3.22D2-206[»]
    2I2UX-ray3.22D2-206[»]
    2QALX-ray3.21D2-206[»]
    2QANX-ray3.21D2-206[»]
    2QB9X-ray3.54D2-206[»]
    2QBBX-ray3.54D2-206[»]
    2QBDX-ray3.30D2-206[»]
    2QBFX-ray3.30D2-206[»]
    2QBHX-ray4.00D2-206[»]
    2QBJX-ray4.00D2-206[»]
    2QOUX-ray3.93D2-206[»]
    2QOWX-ray3.93D2-206[»]
    2QOYX-ray3.50D2-206[»]
    2QP0X-ray3.50D2-206[»]
    2VHPX-ray3.74D2-206[»]
    2WWLelectron microscopy5.80D2-206[»]
    2YKRelectron microscopy9.80D2-206[»]
    2Z4KX-ray4.45D2-206[»]
    2Z4MX-ray4.45D2-206[»]
    3DF1X-ray3.50D2-205[»]
    3DF3X-ray3.50D2-205[»]
    3E1Aelectron microscopy-R1-206[»]
    3E1Celectron microscopy-R1-206[»]
    3FIHelectron microscopy6.70D2-206[»]
    3I1MX-ray3.19D1-206[»]
    3I1OX-ray3.19D1-206[»]
    3I1QX-ray3.81D1-206[»]
    3I1SX-ray3.81D1-206[»]
    3I1ZX-ray3.71D1-206[»]
    3I21X-ray3.71D1-206[»]
    3IZVelectron microscopy-H1-206[»]
    3IZWelectron microscopy-H1-206[»]
    3J00electron microscopy-D2-206[»]
    3J0Uelectron microscopy12.10G2-206[»]
    3J0Velectron microscopy14.70G2-206[»]
    3J0Xelectron microscopy13.50G2-206[»]
    3J0Zelectron microscopy11.50G2-206[»]
    3J10electron microscopy11.50G2-206[»]
    3J13electron microscopy13.10F2-206[»]
    3J18electron microscopy8.30D2-206[»]
    3J36electron microscopy9.80D2-206[»]
    3J4Velectron microscopy12.00D1-206[»]
    3J4Welectron microscopy12.00D1-206[»]
    3J4Yelectron microscopy17.00D1-206[»]
    3J4Zelectron microscopy20.00D1-206[»]
    3J53electron microscopy13.00D1-206[»]
    3J55electron microscopy15.00D1-206[»]
    3J57electron microscopy17.00D1-206[»]
    3J59electron microscopy12.00D1-206[»]
    3J5Belectron microscopy17.00D1-206[»]
    3J5Delectron microscopy17.00D1-206[»]
    3J5Felectron microscopy20.00D1-206[»]
    3J5Helectron microscopy15.00D1-206[»]
    3J5Jelectron microscopy9.00D1-206[»]
    3J5Nelectron microscopy6.80D1-206[»]
    3J5Telectron microscopy7.60D2-206[»]
    3J5Xelectron microscopy7.60D2-206[»]
    3KC4electron microscopy-D1-206[»]
    3OAQX-ray3.25D2-206[»]
    3OARX-ray3.25D2-206[»]
    3OFAX-ray3.19D2-206[»]
    3OFBX-ray3.19D2-206[»]
    3OFOX-ray3.10D2-206[»]
    3OFPX-ray3.10D2-206[»]
    3OFXX-ray3.29D2-206[»]
    3OFYX-ray3.29D2-206[»]
    3OR9X-ray3.30D1-206[»]
    3ORAX-ray3.30D1-206[»]
    3SFSX-ray3.20D1-206[»]
    3UOQX-ray3.70D1-206[»]
    4A2Ielectron microscopy16.50D2-206[»]
    4ADVelectron microscopy13.50D2-206[»]
    4GAQX-ray3.30D1-206[»]
    4GASX-ray3.30D1-206[»]
    4GD1X-ray3.00D2-206[»]
    4GD2X-ray3.00D2-206[»]
    4KIYX-ray2.90D1-206[»]
    4KJ0X-ray2.90D1-206[»]
    4KJ2X-ray2.90D1-206[»]
    4KJ4X-ray2.90D1-206[»]
    4KJ6X-ray2.90D1-206[»]
    4KJ8X-ray2.90D1-206[»]
    4KJAX-ray2.90D1-206[»]
    4KJCX-ray2.90D1-206[»]
    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.
    KOiK02986.
    OMAiTCKLSRR.
    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

    MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD    50
    YGVQLREKQK VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN 100
    VVYRMGFGAT RAEARQLVSH KAIMVNGRVV NIASYQVSPN DVVSIREKAK 150
    KQSRVKAALE LAEQREKPTW LEVDAGKMEG TFKRKPERSD LSADINEHLI 200
    VELYSK 206
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi C23807. R3EC4.
    RefSeqi NP_417755.1. NC_000913.3.
    YP_492136.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG0 electron microscopy 11.50 A 43-200 [» ]
    1M5G model - D 2-206 [» ]
    1P6G electron microscopy 12.30 D 2-206 [» ]
    1P87 electron microscopy 11.50 D 2-206 [» ]
    1VS5 X-ray 3.46 D 1-206 [» ]
    1VS7 X-ray 3.46 D 1-206 [» ]
    2AVY X-ray 3.46 D 2-206 [» ]
    2AW7 X-ray 3.46 D 2-206 [» ]
    2GY9 electron microscopy 15.00 D 3-206 [» ]
    2GYB electron microscopy 15.00 D 3-206 [» ]
    2I2P X-ray 3.22 D 2-206 [» ]
    2I2U X-ray 3.22 D 2-206 [» ]
    2QAL X-ray 3.21 D 2-206 [» ]
    2QAN X-ray 3.21 D 2-206 [» ]
    2QB9 X-ray 3.54 D 2-206 [» ]
    2QBB X-ray 3.54 D 2-206 [» ]
    2QBD X-ray 3.30 D 2-206 [» ]
    2QBF X-ray 3.30 D 2-206 [» ]
    2QBH X-ray 4.00 D 2-206 [» ]
    2QBJ X-ray 4.00 D 2-206 [» ]
    2QOU X-ray 3.93 D 2-206 [» ]
    2QOW X-ray 3.93 D 2-206 [» ]
    2QOY X-ray 3.50 D 2-206 [» ]
    2QP0 X-ray 3.50 D 2-206 [» ]
    2VHP X-ray 3.74 D 2-206 [» ]
    2WWL electron microscopy 5.80 D 2-206 [» ]
    2YKR electron microscopy 9.80 D 2-206 [» ]
    2Z4K X-ray 4.45 D 2-206 [» ]
    2Z4M X-ray 4.45 D 2-206 [» ]
    3DF1 X-ray 3.50 D 2-205 [» ]
    3DF3 X-ray 3.50 D 2-205 [» ]
    3E1A electron microscopy - R 1-206 [» ]
    3E1C electron microscopy - R 1-206 [» ]
    3FIH electron microscopy 6.70 D 2-206 [» ]
    3I1M X-ray 3.19 D 1-206 [» ]
    3I1O X-ray 3.19 D 1-206 [» ]
    3I1Q X-ray 3.81 D 1-206 [» ]
    3I1S X-ray 3.81 D 1-206 [» ]
    3I1Z X-ray 3.71 D 1-206 [» ]
    3I21 X-ray 3.71 D 1-206 [» ]
    3IZV electron microscopy - H 1-206 [» ]
    3IZW electron microscopy - H 1-206 [» ]
    3J00 electron microscopy - D 2-206 [» ]
    3J0U electron microscopy 12.10 G 2-206 [» ]
    3J0V electron microscopy 14.70 G 2-206 [» ]
    3J0X electron microscopy 13.50 G 2-206 [» ]
    3J0Z electron microscopy 11.50 G 2-206 [» ]
    3J10 electron microscopy 11.50 G 2-206 [» ]
    3J13 electron microscopy 13.10 F 2-206 [» ]
    3J18 electron microscopy 8.30 D 2-206 [» ]
    3J36 electron microscopy 9.80 D 2-206 [» ]
    3J4V electron microscopy 12.00 D 1-206 [» ]
    3J4W electron microscopy 12.00 D 1-206 [» ]
    3J4Y electron microscopy 17.00 D 1-206 [» ]
    3J4Z electron microscopy 20.00 D 1-206 [» ]
    3J53 electron microscopy 13.00 D 1-206 [» ]
    3J55 electron microscopy 15.00 D 1-206 [» ]
    3J57 electron microscopy 17.00 D 1-206 [» ]
    3J59 electron microscopy 12.00 D 1-206 [» ]
    3J5B electron microscopy 17.00 D 1-206 [» ]
    3J5D electron microscopy 17.00 D 1-206 [» ]
    3J5F electron microscopy 20.00 D 1-206 [» ]
    3J5H electron microscopy 15.00 D 1-206 [» ]
    3J5J electron microscopy 9.00 D 1-206 [» ]
    3J5N electron microscopy 6.80 D 1-206 [» ]
    3J5T electron microscopy 7.60 D 2-206 [» ]
    3J5X electron microscopy 7.60 D 2-206 [» ]
    3KC4 electron microscopy - D 1-206 [» ]
    3OAQ X-ray 3.25 D 2-206 [» ]
    3OAR X-ray 3.25 D 2-206 [» ]
    3OFA X-ray 3.19 D 2-206 [» ]
    3OFB X-ray 3.19 D 2-206 [» ]
    3OFO X-ray 3.10 D 2-206 [» ]
    3OFP X-ray 3.10 D 2-206 [» ]
    3OFX X-ray 3.29 D 2-206 [» ]
    3OFY X-ray 3.29 D 2-206 [» ]
    3OR9 X-ray 3.30 D 1-206 [» ]
    3ORA X-ray 3.30 D 1-206 [» ]
    3SFS X-ray 3.20 D 1-206 [» ]
    3UOQ X-ray 3.70 D 1-206 [» ]
    4A2I electron microscopy 16.50 D 2-206 [» ]
    4ADV electron microscopy 13.50 D 2-206 [» ]
    4GAQ X-ray 3.30 D 1-206 [» ]
    4GAS X-ray 3.30 D 1-206 [» ]
    4GD1 X-ray 3.00 D 2-206 [» ]
    4GD2 X-ray 3.00 D 2-206 [» ]
    4KIY X-ray 2.90 D 1-206 [» ]
    4KJ0 X-ray 2.90 D 1-206 [» ]
    4KJ2 X-ray 2.90 D 1-206 [» ]
    4KJ4 X-ray 2.90 D 1-206 [» ]
    4KJ6 X-ray 2.90 D 1-206 [» ]
    4KJ8 X-ray 2.90 D 1-206 [» ]
    4KJA X-ray 2.90 D 1-206 [» ]
    4KJC X-ray 2.90 D 1-206 [» ]
    ProteinModelPortali P0A7V8.
    SMRi P0A7V8. Positions 2-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852105. 1 interaction.
    DIPi DIP-35794N.
    IntActi P0A7V8. 214 interactions.
    MINTi MINT-6478162.
    STRINGi 511145.b3296.

    Chemistry

    ChEMBLi CHEMBL2363135.
    DrugBanki DB00453. Clomocycline.
    DB00618. Demeclocycline.
    DB00254. Doxycycline.
    DB00256. Lymecycline.
    DB01017. Minocycline.
    DB00595. Oxytetracycline.
    DB00759. Tetracycline.
    DB00560. Tigecycline.

    Proteomic databases

    PaxDbi P0A7V8.
    PRIDEi P0A7V8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76321 ; AAC76321 ; b3296 .
    BAE77995 ; BAE77995 ; BAE77995 .
    GeneIDi 12934394.
    947793.
    KEGGi ecj:Y75_p3880.
    eco:b3296.
    PATRICi 32122024. VBIEscCol129921_3389.

    Organism-specific databases

    EchoBASEi EB0896.
    EcoGenei EG10903. rpsD.

    Phylogenomic databases

    eggNOGi COG0522.
    HOGENOMi HOG000221003.
    KOi K02986.
    OMAi TCKLSRR.
    OrthoDBi EOG6N3CXM.
    PhylomeDBi P0A7V8.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10903-MONOMER.
    ECOL316407:JW3258-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7V8.
    PROi P0A7V8.

    Gene expression databases

    Genevestigatori P0A7V8.

    Family and domain databases

    Gene3Di 1.10.1050.10. 1 hit.
    3.10.290.10. 1 hit.
    HAMAPi MF_01306_B. Ribosomal_S4_B.
    InterProi IPR022801. Ribosomal_S4/S9.
    IPR001912. Ribosomal_S4/S9_N.
    IPR005709. Ribosomal_S4_bac-type.
    IPR018079. Ribosomal_S4_CS.
    IPR002942. S4_RNA-bd.
    [Graphical view ]
    PANTHERi PTHR11831. PTHR11831. 1 hit.
    Pfami PF00163. Ribosomal_S4. 1 hit.
    PF01479. S4. 1 hit.
    [Graphical view ]
    SMARTi SM00363. S4. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01017. rpsD_bact. 1 hit.
    PROSITEi PS00632. RIBOSOMAL_S4. 1 hit.
    PS50889. S4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 106 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