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Protein

30S ribosomal protein S13

Gene

rpsM

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

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10912. rpsM.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

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

Chemistry

DrugBankiDB00560. Tigecycline.

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.

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 – 73Combined sources
Beta strandi12 – 143Combined sources
Helixi15 – 195Combined sources
Turni21 – 244Combined sources
Helixi28 – 369Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Helixi50 – 6011Combined sources
Beta strandi61 – 633Combined sources
Helixi67 – 8317Combined sources
Helixi86 – 927Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1043Combined sources
Helixi107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-M2-118[»]
2YKRelectron microscopy9.80M2-115[»]
3J9Yelectron microscopy3.90m1-118[»]
4A2Ielectron microscopy16.50M2-115[»]
4ADVelectron microscopy13.50M2-118[»]
4U1UX-ray2.95AM/CM2-115[»]
4U1VX-ray3.00AM/CM2-115[»]
4U20X-ray2.90AM/CM2-115[»]
4U24X-ray2.90AM/CM2-115[»]
4U25X-ray2.90AM/CM2-115[»]
4U26X-ray2.80AM/CM2-115[»]
4U27X-ray2.80AM/CM2-115[»]
4V47electron microscopy12.30BM2-118[»]
4V48electron microscopy11.50BM2-118[»]
4V4HX-ray3.46AM/CM1-118[»]
4V4QX-ray3.46AM/CM2-118[»]
4V4Velectron microscopy15.00AM2-116[»]
4V4Welectron microscopy15.00AM2-116[»]
4V50X-ray3.22AM/CM2-118[»]
4V52X-ray3.21AM/CM2-118[»]
4V53X-ray3.54AM/CM2-118[»]
4V54X-ray3.30AM/CM2-118[»]
4V55X-ray4.00AM/CM2-118[»]
4V56X-ray3.93AM/CM2-118[»]
4V57X-ray3.50AM/CM2-118[»]
4V5BX-ray3.74BM/DM2-118[»]
4V5Helectron microscopy5.80AM2-114[»]
4V5YX-ray4.45AM/CM2-118[»]
4V64X-ray3.50AM/CM2-118[»]
4V65electron microscopy9.00AF1-118[»]
4V66electron microscopy9.00AF1-118[»]
4V69electron microscopy6.70AM2-114[»]
4V6CX-ray3.19AM/CM1-118[»]
4V6DX-ray3.81AM/CM1-118[»]
4V6EX-ray3.71AM/CM1-118[»]
4V6Kelectron microscopy8.25BQ1-118[»]
4V6Lelectron microscopy13.20AQ1-118[»]
4V6Nelectron microscopy12.10BP2-118[»]
4V6Oelectron microscopy14.70AP2-118[»]
4V6Pelectron microscopy13.50AP2-118[»]
4V6Qelectron microscopy11.50AP2-118[»]
4V6Relectron microscopy11.50AP2-118[»]
4V6Selectron microscopy13.10BO2-118[»]
4V6Telectron microscopy8.30AM2-115[»]
4V6Velectron microscopy9.80AM2-118[»]
4V6Yelectron microscopy12.00AM1-114[»]
4V6Zelectron microscopy12.00AM1-114[»]
4V70electron microscopy17.00AM1-114[»]
4V71electron microscopy20.00AM1-114[»]
4V72electron microscopy13.00AM1-114[»]
4V73electron microscopy15.00AM1-114[»]
4V74electron microscopy17.00AM1-114[»]
4V75electron microscopy12.00AM1-114[»]
4V76electron microscopy17.00AM1-114[»]
4V77electron microscopy17.00AM1-114[»]
4V78electron microscopy20.00AM1-114[»]
4V79electron microscopy15.00AM1-114[»]
4V7Aelectron microscopy9.00AM1-114[»]
4V7Belectron microscopy6.80AM1-118[»]
4V7Celectron microscopy7.60AM2-118[»]
4V7Delectron microscopy7.60BM2-118[»]
4V7Ielectron microscopy9.60BM1-118[»]
4V7SX-ray3.25AM2-115[»]
CM2-114[»]
4V7TX-ray3.19AM2-115[»]
CM2-114[»]
4V7UX-ray3.10AM/CM2-115[»]
4V7VX-ray3.29AM2-115[»]
CM2-114[»]
4V85X-ray3.20M1-118[»]
4V89X-ray3.70AM1-118[»]
4V9CX-ray3.30AM/CM1-118[»]
4V9DX-ray3.00AM/BM2-115[»]
4V9OX-ray2.90BM/DM/FM/HM1-118[»]
4V9PX-ray2.90BM/DM/FM/HM1-118[»]
4WF1X-ray3.09AM/CM2-115[»]
4WWWX-ray3.10QM/XM2-115[»]
4YBBX-ray2.10AM/BM2-115[»]
5AFIelectron microscopy2.90m1-118[»]
ProteinModelPortaliP0A7S9.
SMRiP0A7S9. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7S9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S13P family.Curated

Phylogenomic databases

eggNOGiCOG0099.
HOGENOMiHOG000039879.
InParanoidiP0A7S9.
KOiK02952.
OMAiREVAMNI.
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. uS13_bact. 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

        10         20         30         40         50
MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE
60 70 80 90 100
GQIDTLRDEV AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ
110
RTKTNARTRK GPRKPIKK
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:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC76323; AAC76323; b3298.
BAE77993; BAE77993; BAE77993.
GeneIDi947791.
KEGGiecj:Y75_p3878.
eco:b3298.
PATRICi32122028. VBIEscCol129921_3391.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-M2-118[»]
2YKRelectron microscopy9.80M2-115[»]
3J9Yelectron microscopy3.90m1-118[»]
4A2Ielectron microscopy16.50M2-115[»]
4ADVelectron microscopy13.50M2-118[»]
4U1UX-ray2.95AM/CM2-115[»]
4U1VX-ray3.00AM/CM2-115[»]
4U20X-ray2.90AM/CM2-115[»]
4U24X-ray2.90AM/CM2-115[»]
4U25X-ray2.90AM/CM2-115[»]
4U26X-ray2.80AM/CM2-115[»]
4U27X-ray2.80AM/CM2-115[»]
4V47electron microscopy12.30BM2-118[»]
4V48electron microscopy11.50BM2-118[»]
4V4HX-ray3.46AM/CM1-118[»]
4V4QX-ray3.46AM/CM2-118[»]
4V4Velectron microscopy15.00AM2-116[»]
4V4Welectron microscopy15.00AM2-116[»]
4V50X-ray3.22AM/CM2-118[»]
4V52X-ray3.21AM/CM2-118[»]
4V53X-ray3.54AM/CM2-118[»]
4V54X-ray3.30AM/CM2-118[»]
4V55X-ray4.00AM/CM2-118[»]
4V56X-ray3.93AM/CM2-118[»]
4V57X-ray3.50AM/CM2-118[»]
4V5BX-ray3.74BM/DM2-118[»]
4V5Helectron microscopy5.80AM2-114[»]
4V5YX-ray4.45AM/CM2-118[»]
4V64X-ray3.50AM/CM2-118[»]
4V65electron microscopy9.00AF1-118[»]
4V66electron microscopy9.00AF1-118[»]
4V69electron microscopy6.70AM2-114[»]
4V6CX-ray3.19AM/CM1-118[»]
4V6DX-ray3.81AM/CM1-118[»]
4V6EX-ray3.71AM/CM1-118[»]
4V6Kelectron microscopy8.25BQ1-118[»]
4V6Lelectron microscopy13.20AQ1-118[»]
4V6Nelectron microscopy12.10BP2-118[»]
4V6Oelectron microscopy14.70AP2-118[»]
4V6Pelectron microscopy13.50AP2-118[»]
4V6Qelectron microscopy11.50AP2-118[»]
4V6Relectron microscopy11.50AP2-118[»]
4V6Selectron microscopy13.10BO2-118[»]
4V6Telectron microscopy8.30AM2-115[»]
4V6Velectron microscopy9.80AM2-118[»]
4V6Yelectron microscopy12.00AM1-114[»]
4V6Zelectron microscopy12.00AM1-114[»]
4V70electron microscopy17.00AM1-114[»]
4V71electron microscopy20.00AM1-114[»]
4V72electron microscopy13.00AM1-114[»]
4V73electron microscopy15.00AM1-114[»]
4V74electron microscopy17.00AM1-114[»]
4V75electron microscopy12.00AM1-114[»]
4V76electron microscopy17.00AM1-114[»]
4V77electron microscopy17.00AM1-114[»]
4V78electron microscopy20.00AM1-114[»]
4V79electron microscopy15.00AM1-114[»]
4V7Aelectron microscopy9.00AM1-114[»]
4V7Belectron microscopy6.80AM1-118[»]
4V7Celectron microscopy7.60AM2-118[»]
4V7Delectron microscopy7.60BM2-118[»]
4V7Ielectron microscopy9.60BM1-118[»]
4V7SX-ray3.25AM2-115[»]
CM2-114[»]
4V7TX-ray3.19AM2-115[»]
CM2-114[»]
4V7UX-ray3.10AM/CM2-115[»]
4V7VX-ray3.29AM2-115[»]
CM2-114[»]
4V85X-ray3.20M1-118[»]
4V89X-ray3.70AM1-118[»]
4V9CX-ray3.30AM/CM1-118[»]
4V9DX-ray3.00AM/BM2-115[»]
4V9OX-ray2.90BM/DM/FM/HM1-118[»]
4V9PX-ray2.90BM/DM/FM/HM1-118[»]
4WF1X-ray3.09AM/CM2-115[»]
4WWWX-ray3.10QM/XM2-115[»]
4YBBX-ray2.10AM/BM2-115[»]
5AFIelectron microscopy2.90m1-118[»]
ProteinModelPortaliP0A7S9.
SMRiP0A7S9. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00560. Tigecycline.

Proteomic databases

PaxDbiP0A7S9.
PRIDEiP0A7S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76323; AAC76323; b3298.
BAE77993; BAE77993; BAE77993.
GeneIDi947791.
KEGGiecj:Y75_p3878.
eco:b3298.
PATRICi32122028. VBIEscCol129921_3391.

Organism-specific databases

EchoBASEiEB0905.
EcoGeneiEG10912. rpsM.

Phylogenomic databases

eggNOGiCOG0099.
HOGENOMiHOG000039879.
InParanoidiP0A7S9.
KOiK02952.
OMAiREVAMNI.
OrthoDBiEOG618R01.
PhylomeDBiP0A7S9.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7S9.
PROiP0A7S9.

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. uS13_bact. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 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].
    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: June 24, 2015
This is version 110 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.