Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A7S9

- RS13_ECOLI

UniProt

P0A7S9 - RS13_ECOLI

Protein

30S ribosomal protein S13

Gene

rpsM

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

    Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.1 Publication
    In the E.coli 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; bridge B1a is broken in the model with bound EF-G, while the protein-protein contacts between S13 and L5 in B1b change (PubMed:12809609). The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:16272117), contacting alternately S13 or S19. In the two 3.5 angstroms resolved ribosome structures (PubMed:12859903) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.4 Publications
    Contacts the tRNAs in the A and P sites.1 Publication
    The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs.1 Publication

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro
    3. tRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. ribosome biogenesis Source: RefGenome
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10912-MONOMER.
    ECOL316407:JW3260-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S13
    Gene namesi
    Name:rpsM
    Ordered Locus Names:b3298, JW3260
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10912. rpsM.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 11836Missing: Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 PublicationAdd
    BLAST
    Mutagenesisi114 – 1185Missing: Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11811730S ribosomal protein S13PRO_0000132089Add
    BLAST

    Proteomic databases

    PaxDbiP0A7S9.
    PRIDEiP0A7S9.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7S9.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Cross-links to the P site tRNA and weakly to the A site tRNA. Forms two bridges to the 50S subunit in the 70S ribosome, contacting the 16S rRNA and proteins S19 and L5.

    Protein-protein interaction databases

    DIPiDIP-35855N.
    IntActiP0A7S9. 101 interactions.
    MINTiMINT-1290225.
    STRINGi511145.b3298.

    Structurei

    Secondary structure

    1
    118
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Beta strandi12 – 143
    Helixi15 – 184
    Helixi19 – 213
    Beta strandi22 – 243
    Helixi27 – 359
    Turni36 – 383
    Beta strandi41 – 433
    Turni45 – 473
    Helixi50 – 578
    Helixi60 – 623
    Helixi66 – 8318
    Helixi86 – 938
    Beta strandi97 – 993
    Beta strandi102 – 1043
    Helixi107 – 1104

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-M2-118[»]
    1P6Gelectron microscopy12.30M2-118[»]
    1P87electron microscopy11.50M2-118[»]
    1VS5X-ray3.46M1-118[»]
    1VS7X-ray3.46M1-118[»]
    2AVYX-ray3.46M2-118[»]
    2AW7X-ray3.46M2-118[»]
    2GY9electron microscopy15.00M2-116[»]
    2GYBelectron microscopy15.00M2-116[»]
    2I2PX-ray3.22M2-118[»]
    2I2UX-ray3.22M2-118[»]
    2QALX-ray3.21M2-118[»]
    2QANX-ray3.21M2-118[»]
    2QB9X-ray3.54M2-118[»]
    2QBBX-ray3.54M2-118[»]
    2QBDX-ray3.30M2-118[»]
    2QBFX-ray3.30M2-118[»]
    2QBHX-ray4.00M2-118[»]
    2QBJX-ray4.00M2-118[»]
    2QOUX-ray3.93M2-118[»]
    2QOWX-ray3.93M2-118[»]
    2QOYX-ray3.50M2-118[»]
    2QP0X-ray3.50M2-118[»]
    2VHOX-ray3.74M2-118[»]
    2VHPX-ray3.74M2-118[»]
    2WWLelectron microscopy5.80M2-114[»]
    2YKRelectron microscopy9.80M2-115[»]
    2Z4KX-ray4.45M2-118[»]
    2Z4MX-ray4.45M2-118[»]
    3DF1X-ray3.50M2-117[»]
    3DF3X-ray3.50M2-117[»]
    3E1Aelectron microscopy-F1-118[»]
    3E1Celectron microscopy-F1-118[»]
    3FIHelectron microscopy6.70M2-114[»]
    3I1MX-ray3.19M1-118[»]
    3I1OX-ray3.19M1-118[»]
    3I1QX-ray3.81M1-118[»]
    3I1SX-ray3.81M1-118[»]
    3I1ZX-ray3.71M1-118[»]
    3I21X-ray3.71M1-118[»]
    3IZVelectron microscopy-Q1-118[»]
    3IZWelectron microscopy-Q1-118[»]
    3J00electron microscopy-M2-118[»]
    3J0Uelectron microscopy12.10P2-118[»]
    3J0Velectron microscopy14.70P2-118[»]
    3J0Xelectron microscopy13.50P2-118[»]
    3J0Zelectron microscopy11.50P2-118[»]
    3J10electron microscopy11.50P2-118[»]
    3J13electron microscopy13.10O2-118[»]
    3J18electron microscopy8.30M2-115[»]
    3J36electron microscopy9.80M2-118[»]
    3J4Velectron microscopy12.00M1-114[»]
    3J4Welectron microscopy12.00M1-114[»]
    3J4Yelectron microscopy17.00M1-114[»]
    3J4Zelectron microscopy20.00M1-114[»]
    3J53electron microscopy13.00M1-114[»]
    3J55electron microscopy15.00M1-114[»]
    3J57electron microscopy17.00M1-114[»]
    3J59electron microscopy12.00M1-114[»]
    3J5Belectron microscopy17.00M1-114[»]
    3J5Delectron microscopy17.00M1-114[»]
    3J5Felectron microscopy20.00M1-114[»]
    3J5Helectron microscopy15.00M1-114[»]
    3J5Jelectron microscopy9.00M1-114[»]
    3J5Nelectron microscopy6.80M1-118[»]
    3J5Telectron microscopy7.60M2-118[»]
    3J5Xelectron microscopy7.60M2-118[»]
    3KC4electron microscopy-M1-118[»]
    3OAQX-ray3.25M2-115[»]
    3OARX-ray3.25M2-114[»]
    3OFAX-ray3.19M2-115[»]
    3OFBX-ray3.19M2-114[»]
    3OFOX-ray3.10M2-115[»]
    3OFPX-ray3.10M2-114[»]
    3OFXX-ray3.29M2-115[»]
    3OFYX-ray3.29M2-114[»]
    3OR9X-ray3.30M1-118[»]
    3ORAX-ray3.30M1-118[»]
    3SFSX-ray3.20M1-118[»]
    3UOQX-ray3.70M1-118[»]
    4A2Ielectron microscopy16.50M2-115[»]
    4ADVelectron microscopy13.50M2-118[»]
    4GAQX-ray3.30M1-118[»]
    4GASX-ray3.30M1-118[»]
    4GD1X-ray3.00M2-115[»]
    4GD2X-ray3.00M2-115[»]
    4KIYX-ray2.90M1-118[»]
    4KJ0X-ray2.90M1-118[»]
    4KJ2X-ray2.90M1-118[»]
    4KJ4X-ray2.90M1-118[»]
    4KJ6X-ray2.90M1-118[»]
    4KJ8X-ray2.90M1-118[»]
    4KJAX-ray2.90M1-118[»]
    4KJCX-ray2.90M1-118[»]
    ProteinModelPortaliP0A7S9.
    SMRiP0A7S9. Positions 2-116.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7S9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S13P family.Curated

    Phylogenomic databases

    eggNOGiCOG0099.
    HOGENOMiHOG000039879.
    KOiK02952.
    OMAiVAKYPVE.
    OrthoDBiEOG618R01.
    PhylomeDBiP0A7S9.

    Family and domain databases

    Gene3Di4.10.910.10. 1 hit.
    HAMAPiMF_01315. Ribosomal_S13_S18.
    InterProiIPR027437. 30s_Rbsml_prot_S13_C.
    IPR001892. Ribosomal_S13.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR019980. Ribosomal_S13_bac-type.
    IPR018269. Ribosomal_S13_CS.
    [Graphical view]
    PfamiPF00416. Ribosomal_S13. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
    SUPFAMiSSF46946. SSF46946. 1 hit.
    TIGRFAMsiTIGR03631. bact_S13. 1 hit.
    PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
    PS50159. RIBOSOMAL_S13_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7S9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE    50
    GQIDTLRDEV AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ 100
    RTKTNARTRK GPRKPIKK 118
    Length:118
    Mass (Da):13,099
    Last modified:January 23, 2007 - v2
    Checksum:i6277C365EBE4F732
    GO

    Mass spectrometryi

    Molecular mass is 12968.1 Da from positions 2 - 118. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 9911Missing in PW118; partially suppresses a rimM deletion.
    Add
    BLAST
    Natural varianti100 – 11819Missing in rpsM413; pseudorevertant of streptomycin resistance. A strong antisuppressor of two tRNA suppressors, decreases translation step time and growth rate.
    Add
    BLAST
    Natural varianti105 – 1051N → H in PW095; partially suppresses a rimM deletion.
    Natural varianti105 – 1051N → K in PW097; partially suppresses a rimM deletion.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26392.1.
    U18997 Genomic DNA. Translation: AAA58093.1.
    U00096 Genomic DNA. Translation: AAC76323.1.
    AP009048 Genomic DNA. Translation: BAE77993.1.
    M12432 Genomic DNA. Translation: AAA83903.1.
    M10213 Genomic DNA. Translation: AAA72457.1.
    PIRiA23807. R3EC13.
    RefSeqiNP_417757.1. NC_000913.3.
    YP_492134.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76323; AAC76323; b3298.
    BAE77993; BAE77993; BAE77993.
    GeneIDi12934445.
    947791.
    KEGGiecj:Y75_p3878.
    eco:b3298.
    PATRICi32122028. VBIEscCol129921_3391.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26392.1 .
    U18997 Genomic DNA. Translation: AAA58093.1 .
    U00096 Genomic DNA. Translation: AAC76323.1 .
    AP009048 Genomic DNA. Translation: BAE77993.1 .
    M12432 Genomic DNA. Translation: AAA83903.1 .
    M10213 Genomic DNA. Translation: AAA72457.1 .
    PIRi A23807. R3EC13.
    RefSeqi NP_417757.1. NC_000913.3.
    YP_492134.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M5G model - M 2-118 [» ]
    1P6G electron microscopy 12.30 M 2-118 [» ]
    1P87 electron microscopy 11.50 M 2-118 [» ]
    1VS5 X-ray 3.46 M 1-118 [» ]
    1VS7 X-ray 3.46 M 1-118 [» ]
    2AVY X-ray 3.46 M 2-118 [» ]
    2AW7 X-ray 3.46 M 2-118 [» ]
    2GY9 electron microscopy 15.00 M 2-116 [» ]
    2GYB electron microscopy 15.00 M 2-116 [» ]
    2I2P X-ray 3.22 M 2-118 [» ]
    2I2U X-ray 3.22 M 2-118 [» ]
    2QAL X-ray 3.21 M 2-118 [» ]
    2QAN X-ray 3.21 M 2-118 [» ]
    2QB9 X-ray 3.54 M 2-118 [» ]
    2QBB X-ray 3.54 M 2-118 [» ]
    2QBD X-ray 3.30 M 2-118 [» ]
    2QBF X-ray 3.30 M 2-118 [» ]
    2QBH X-ray 4.00 M 2-118 [» ]
    2QBJ X-ray 4.00 M 2-118 [» ]
    2QOU X-ray 3.93 M 2-118 [» ]
    2QOW X-ray 3.93 M 2-118 [» ]
    2QOY X-ray 3.50 M 2-118 [» ]
    2QP0 X-ray 3.50 M 2-118 [» ]
    2VHO X-ray 3.74 M 2-118 [» ]
    2VHP X-ray 3.74 M 2-118 [» ]
    2WWL electron microscopy 5.80 M 2-114 [» ]
    2YKR electron microscopy 9.80 M 2-115 [» ]
    2Z4K X-ray 4.45 M 2-118 [» ]
    2Z4M X-ray 4.45 M 2-118 [» ]
    3DF1 X-ray 3.50 M 2-117 [» ]
    3DF3 X-ray 3.50 M 2-117 [» ]
    3E1A electron microscopy - F 1-118 [» ]
    3E1C electron microscopy - F 1-118 [» ]
    3FIH electron microscopy 6.70 M 2-114 [» ]
    3I1M X-ray 3.19 M 1-118 [» ]
    3I1O X-ray 3.19 M 1-118 [» ]
    3I1Q X-ray 3.81 M 1-118 [» ]
    3I1S X-ray 3.81 M 1-118 [» ]
    3I1Z X-ray 3.71 M 1-118 [» ]
    3I21 X-ray 3.71 M 1-118 [» ]
    3IZV electron microscopy - Q 1-118 [» ]
    3IZW electron microscopy - Q 1-118 [» ]
    3J00 electron microscopy - M 2-118 [» ]
    3J0U electron microscopy 12.10 P 2-118 [» ]
    3J0V electron microscopy 14.70 P 2-118 [» ]
    3J0X electron microscopy 13.50 P 2-118 [» ]
    3J0Z electron microscopy 11.50 P 2-118 [» ]
    3J10 electron microscopy 11.50 P 2-118 [» ]
    3J13 electron microscopy 13.10 O 2-118 [» ]
    3J18 electron microscopy 8.30 M 2-115 [» ]
    3J36 electron microscopy 9.80 M 2-118 [» ]
    3J4V electron microscopy 12.00 M 1-114 [» ]
    3J4W electron microscopy 12.00 M 1-114 [» ]
    3J4Y electron microscopy 17.00 M 1-114 [» ]
    3J4Z electron microscopy 20.00 M 1-114 [» ]
    3J53 electron microscopy 13.00 M 1-114 [» ]
    3J55 electron microscopy 15.00 M 1-114 [» ]
    3J57 electron microscopy 17.00 M 1-114 [» ]
    3J59 electron microscopy 12.00 M 1-114 [» ]
    3J5B electron microscopy 17.00 M 1-114 [» ]
    3J5D electron microscopy 17.00 M 1-114 [» ]
    3J5F electron microscopy 20.00 M 1-114 [» ]
    3J5H electron microscopy 15.00 M 1-114 [» ]
    3J5J electron microscopy 9.00 M 1-114 [» ]
    3J5N electron microscopy 6.80 M 1-118 [» ]
    3J5T electron microscopy 7.60 M 2-118 [» ]
    3J5X electron microscopy 7.60 M 2-118 [» ]
    3KC4 electron microscopy - M 1-118 [» ]
    3OAQ X-ray 3.25 M 2-115 [» ]
    3OAR X-ray 3.25 M 2-114 [» ]
    3OFA X-ray 3.19 M 2-115 [» ]
    3OFB X-ray 3.19 M 2-114 [» ]
    3OFO X-ray 3.10 M 2-115 [» ]
    3OFP X-ray 3.10 M 2-114 [» ]
    3OFX X-ray 3.29 M 2-115 [» ]
    3OFY X-ray 3.29 M 2-114 [» ]
    3OR9 X-ray 3.30 M 1-118 [» ]
    3ORA X-ray 3.30 M 1-118 [» ]
    3SFS X-ray 3.20 M 1-118 [» ]
    3UOQ X-ray 3.70 M 1-118 [» ]
    4A2I electron microscopy 16.50 M 2-115 [» ]
    4ADV electron microscopy 13.50 M 2-118 [» ]
    4GAQ X-ray 3.30 M 1-118 [» ]
    4GAS X-ray 3.30 M 1-118 [» ]
    4GD1 X-ray 3.00 M 2-115 [» ]
    4GD2 X-ray 3.00 M 2-115 [» ]
    4KIY X-ray 2.90 M 1-118 [» ]
    4KJ0 X-ray 2.90 M 1-118 [» ]
    4KJ2 X-ray 2.90 M 1-118 [» ]
    4KJ4 X-ray 2.90 M 1-118 [» ]
    4KJ6 X-ray 2.90 M 1-118 [» ]
    4KJ8 X-ray 2.90 M 1-118 [» ]
    4KJA X-ray 2.90 M 1-118 [» ]
    4KJC X-ray 2.90 M 1-118 [» ]
    ProteinModelPortali P0A7S9.
    SMRi P0A7S9. Positions 2-116.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35855N.
    IntActi P0A7S9. 101 interactions.
    MINTi MINT-1290225.
    STRINGi 511145.b3298.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7S9.
    PRIDEi P0A7S9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76323 ; AAC76323 ; b3298 .
    BAE77993 ; BAE77993 ; BAE77993 .
    GeneIDi 12934445.
    947791.
    KEGGi ecj:Y75_p3878.
    eco:b3298.
    PATRICi 32122028. VBIEscCol129921_3391.

    Organism-specific databases

    EchoBASEi EB0905.
    EcoGenei EG10912. rpsM.

    Phylogenomic databases

    eggNOGi COG0099.
    HOGENOMi HOG000039879.
    KOi K02952.
    OMAi VAKYPVE.
    OrthoDBi EOG618R01.
    PhylomeDBi P0A7S9.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10912-MONOMER.
    ECOL316407:JW3260-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7S9.
    PROi P0A7S9.

    Gene expression databases

    Genevestigatori P0A7S9.

    Family and domain databases

    Gene3Di 4.10.910.10. 1 hit.
    HAMAPi MF_01315. Ribosomal_S13_S18.
    InterProi IPR027437. 30s_Rbsml_prot_S13_C.
    IPR001892. Ribosomal_S13.
    IPR010979. Ribosomal_S13-like_H2TH.
    IPR019980. Ribosomal_S13_bac-type.
    IPR018269. Ribosomal_S13_CS.
    [Graphical view ]
    Pfami PF00416. Ribosomal_S13. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002134. Ribosomal_S13. 1 hit.
    SUPFAMi SSF46946. SSF46946. 1 hit.
    TIGRFAMsi TIGR03631. bact_S13. 1 hit.
    PROSITEi PS00646. RIBOSOMAL_S13_1. 1 hit.
    PS50159. RIBOSOMAL_S13_2. 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].
      Strain: K12.
    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. "Primary structure of protein S13 from the small subunit of Escherichia coli ribosomes."
      Lindemann H., Wittmann-Liebold B.
      Hoppe-Seyler's Z. Physiol. Chem. 358:843-863(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-118.
      Strain: K.
    5. "DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli."
      Post L.E., Arfsten A.E., Davis G.R., Nomura M.
      J. Biol. Chem. 255:4653-4659(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    6. "Growth-rate-dependent regulation of ribosome synthesis in E. coli: expression of the lacZ and galK genes fused to ribosomal promoters."
      Miura A., Krueger J.H., Itoh S., de Boer H.A., Nomura M.
      Cell 25:773-782(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    7. "Identification of a cross-link in the Escherichia coli ribosomal protein pair S13-S19 at the amino acid level."
      Pohl T., Wittmann-Liebold B.
      J. Biol. Chem. 263:4293-4301(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 83-85, CROSS-LINKING TO S19.
      Strain: K12 / A19.
    8. "Antisuppression by a mutation in rpsM(S13) giving a shortened ribosomal protein S13."
      Faxen M., Walles-Granberg A., Isaksson L.A.
      Biochim. Biophys. Acta 1218:27-34(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT RPSM413.
      Strain: K12.
    9. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
      Osswald M., Doering T., Brimacombe R.
      Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
      Strain: MRE-600.
    10. "A novel ribosome-associated protein is important for efficient translation in Escherichia coli."
      Bylund G.O., Persson B.C., Lundberg L.A., Wikstroem P.M.
      J. Bacteriol. 179:4567-4574(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABILITY OF VARIANTS PW118; PW097 AND PW095 TO PARTIALLY SUPPRESS A RIMM DELETION.
      Strain: MW100.
    11. Cited for: ROLE IN P SITE TRNA-BINDING, MUTAGENESIS.
      Strain: CSH142.
    12. "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.
    13. "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.
    14. "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), INTERSUBUNIT BRIDGE FORMATION.
      Strain: MRE-600.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE B1B.
      Strain: MRE-600.
    16. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.

    Entry informationi

    Entry nameiRS13_ECOLI
    AccessioniPrimary (citable) accession number: P0A7S9
    Secondary accession number(s): P02369, Q2M6W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 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