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P0A7V3

- RS3_ECOLI

UniProt

P0A7V3 - RS3_ECOLI

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Protein

30S ribosomal protein S3

Gene

rpsC

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

Functioni

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity).By similarity
Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

GO - Molecular functioni

  1. DNA-(apurinic or apyrimidinic site) lyase activity Source: RefGenome
  2. mRNA binding Source: UniProtKB-HAMAP
  3. rRNA binding Source: UniProtKB-HAMAP
  4. structural constituent of ribosome Source: RefGenome

GO - Biological processi

  1. cytoplasmic translation Source: RefGenome
  2. DNA catabolic process, endonucleolytic Source: GOC
  3. DNA repair Source: RefGenome
  4. regulation of apoptotic process Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S3
Gene namesi
Name:rpsC
Ordered Locus Names:b3314, JW3276
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10902. rpsC.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1355RRAMK → AAAMA: Decreases mRNA unwinding ability of the ribosome. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 23323230S ribosomal protein S3PRO_0000130113Add
BLAST

Proteomic databases

PaxDbiP0A7V3.
PRIDEiP0A7V3.

Expressioni

Gene expression databases

GenevestigatoriP0A7V3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14 (By similarity). With proteins S4 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.By similarity

Protein-protein interaction databases

BioGridi852126. 1 interaction.
DIPiDIP-35807N.
IntActiP0A7V3. 188 interactions.
MINTiMINT-6478122.
STRINGi511145.b3314.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Turni12 – 154
Beta strandi19 – 213
Helixi26 – 4621
Helixi47 – 493
Beta strandi52 – 576
Beta strandi61 – 644
Beta strandi67 – 715
Helixi73 – 775
Turni78 – 814
Helixi82 – 9514
Beta strandi102 – 1054
Helixi109 – 1113
Helixi113 – 12513
Helixi130 – 14314
Beta strandi147 – 15610
Helixi157 – 1593
Beta strandi165 – 1717
Beta strandi175 – 1773
Beta strandi178 – 1803
Beta strandi182 – 19110
Beta strandi194 – 20310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-C2-207[»]
1P6Gelectron microscopy12.30C2-233[»]
1P87electron microscopy11.50C2-233[»]
1VS5X-ray3.46C1-233[»]
1VS7X-ray3.46C1-233[»]
2AVYX-ray3.46C2-233[»]
2AW7X-ray3.46C2-233[»]
2GY9electron microscopy15.00C2-207[»]
2GYBelectron microscopy15.00C2-207[»]
2I2PX-ray3.22C2-233[»]
2I2UX-ray3.22C2-233[»]
2QALX-ray3.21C2-233[»]
2QANX-ray3.21C2-233[»]
2QB9X-ray3.54C2-233[»]
2QBBX-ray3.54C2-233[»]
2QBDX-ray3.30C2-233[»]
2QBFX-ray3.30C2-233[»]
2QBHX-ray4.00C2-233[»]
2QBJX-ray4.00C2-233[»]
2QOUX-ray3.93C2-233[»]
2QOWX-ray3.93C2-233[»]
2QOYX-ray3.50C2-233[»]
2QP0X-ray3.50C2-233[»]
2VHOX-ray3.74C2-233[»]
2VHPX-ray3.74C2-233[»]
2WWLelectron microscopy5.80C2-207[»]
2YKRelectron microscopy9.80C2-207[»]
2Z4KX-ray4.45C2-233[»]
2Z4MX-ray4.45C2-233[»]
3DF1X-ray3.50C2-232[»]
3DF3X-ray3.50C2-232[»]
3E1Aelectron microscopy-O1-233[»]
3E1Celectron microscopy-O1-233[»]
3FIHelectron microscopy6.70C2-207[»]
3I1MX-ray3.19C1-233[»]
3I1OX-ray3.19C1-233[»]
3I1QX-ray3.81C1-233[»]
3I1SX-ray3.81C1-233[»]
3I1ZX-ray3.71C1-233[»]
3I21X-ray3.71C1-233[»]
3IZVelectron microscopy-G1-233[»]
3IZWelectron microscopy-G1-233[»]
3J00electron microscopy-C2-233[»]
3J0Uelectron microscopy12.10F2-233[»]
3J0Velectron microscopy14.70F2-233[»]
3J0Xelectron microscopy13.50F2-233[»]
3J0Zelectron microscopy11.50F2-233[»]
3J10electron microscopy11.50F2-233[»]
3J13electron microscopy13.10E2-233[»]
3J18electron microscopy8.30C2-207[»]
3J36electron microscopy9.80C2-233[»]
3J4Velectron microscopy12.00C1-207[»]
3J4Welectron microscopy12.00C1-207[»]
3J4Yelectron microscopy17.00C1-207[»]
3J4Zelectron microscopy20.00C1-207[»]
3J53electron microscopy13.00C1-207[»]
3J55electron microscopy15.00C1-207[»]
3J57electron microscopy17.00C1-207[»]
3J59electron microscopy12.00C1-207[»]
3J5Belectron microscopy17.00C1-207[»]
3J5Delectron microscopy17.00C1-207[»]
3J5Felectron microscopy20.00C1-207[»]
3J5Helectron microscopy15.00C1-207[»]
3J5Jelectron microscopy9.00C1-207[»]
3J5Nelectron microscopy6.80C1-233[»]
3J5Telectron microscopy7.60C2-233[»]
3J5Xelectron microscopy7.60C2-233[»]
3KC4electron microscopy-C1-233[»]
3OAQX-ray3.25C2-207[»]
3OARX-ray3.25C2-207[»]
3OFAX-ray3.19C2-207[»]
3OFBX-ray3.19C2-207[»]
3OFOX-ray3.10C2-207[»]
3OFPX-ray3.10C2-207[»]
3OFXX-ray3.29C2-207[»]
3OFYX-ray3.29C2-207[»]
3OR9X-ray3.30C1-233[»]
3ORAX-ray3.30C1-233[»]
3SFSX-ray3.20C1-233[»]
3UOQX-ray3.70C1-233[»]
4A2Ielectron microscopy16.50C2-207[»]
4ADVelectron microscopy13.50C2-233[»]
4GAQX-ray3.30C1-233[»]
4GASX-ray3.30C1-233[»]
4GD1X-ray3.00C2-207[»]
4GD2X-ray3.00C2-207[»]
4KIYX-ray2.90C1-233[»]
4KJ0X-ray2.90C1-233[»]
4KJ2X-ray2.90C1-233[»]
4KJ4X-ray2.90C1-233[»]
4KJ6X-ray2.90C1-233[»]
4KJ8X-ray2.90C1-233[»]
4KJAX-ray2.90C1-233[»]
4KJCX-ray2.90C1-233[»]
4PE9X-ray2.95C2-207[»]
4PEAX-ray2.95C2-207[»]
4TOLX-ray3.00C2-207[»]
4TONX-ray3.00C2-207[»]
4TOUX-ray2.90C2-207[»]
4TOWX-ray2.90C2-207[»]
4TP0X-ray2.90C2-207[»]
4TP2X-ray2.90C2-207[»]
4TP4X-ray2.90C2-207[»]
4TP6X-ray2.90C2-207[»]
4TP8X-ray2.80C2-207[»]
4TPAX-ray2.80C2-207[»]
4TPCX-ray2.80C2-207[»]
4TPEX-ray2.80C2-207[»]
ProteinModelPortaliP0A7V3.
SMRiP0A7V3. Positions 2-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 10769KH type-2Add
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S3P family.Curated
Contains 1 KH type-2 domain.Curated

Phylogenomic databases

eggNOGiCOG0092.
HOGENOMiHOG000210610.
InParanoidiP0A7V3.
KOiK02982.
OMAiIARAEWY.
OrthoDBiEOG6K13X3.
PhylomeDBiP0A7V3.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
HAMAPiMF_01309_B. Ribosomal_S3_B.
InterProiIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01009. rpsC_bact. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7V3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGQKVHPNGI RLGIVKPWNS TWFANTKEFA DNLDSDFKVR QYLTKELAKA
60 70 80 90 100
SVSRIVIERP AKSIRVTIHT ARPGIVIGKK GEDVEKLRKV VADIAGVPAQ
110 120 130 140 150
INIAEVRKPE LDAKLVADSI TSQLERRVMF RRAMKRAVQN AMRLGAKGIK
160 170 180 190 200
VEVSGRLGGA EIARTEWYRE GRVPLHTLRA DIDYNTSEAH TTYGVIGVKV
210 220 230
WIFKGEILGG MAAVEQPEKP AAQPKKQQRK GRK
Length:233
Mass (Da):25,983
Last modified:January 23, 2007 - v2
Checksum:i6D0131A285B7AAB3
GO

Mass spectrometryi

Molecular mass is 25851.9 Da from positions 2 - 233. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26466.1.
U18997 Genomic DNA. Translation: AAA58111.1.
U00096 Genomic DNA. Translation: AAC76339.1.
AP009048 Genomic DNA. Translation: BAE77977.1.
PIRiH23129. R3EC3.
RefSeqiNP_417773.1. NC_000913.3.
YP_492118.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76339; AAC76339; b3314.
BAE77977; BAE77977; BAE77977.
GeneIDi12932292.
947814.
KEGGiecj:Y75_p3862.
eco:b3314.
PATRICi32122060. VBIEscCol129921_3407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26466.1 .
U18997 Genomic DNA. Translation: AAA58111.1 .
U00096 Genomic DNA. Translation: AAC76339.1 .
AP009048 Genomic DNA. Translation: BAE77977.1 .
PIRi H23129. R3EC3.
RefSeqi NP_417773.1. NC_000913.3.
YP_492118.1. 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 - C 2-207 [» ]
1P6G electron microscopy 12.30 C 2-233 [» ]
1P87 electron microscopy 11.50 C 2-233 [» ]
1VS5 X-ray 3.46 C 1-233 [» ]
1VS7 X-ray 3.46 C 1-233 [» ]
2AVY X-ray 3.46 C 2-233 [» ]
2AW7 X-ray 3.46 C 2-233 [» ]
2GY9 electron microscopy 15.00 C 2-207 [» ]
2GYB electron microscopy 15.00 C 2-207 [» ]
2I2P X-ray 3.22 C 2-233 [» ]
2I2U X-ray 3.22 C 2-233 [» ]
2QAL X-ray 3.21 C 2-233 [» ]
2QAN X-ray 3.21 C 2-233 [» ]
2QB9 X-ray 3.54 C 2-233 [» ]
2QBB X-ray 3.54 C 2-233 [» ]
2QBD X-ray 3.30 C 2-233 [» ]
2QBF X-ray 3.30 C 2-233 [» ]
2QBH X-ray 4.00 C 2-233 [» ]
2QBJ X-ray 4.00 C 2-233 [» ]
2QOU X-ray 3.93 C 2-233 [» ]
2QOW X-ray 3.93 C 2-233 [» ]
2QOY X-ray 3.50 C 2-233 [» ]
2QP0 X-ray 3.50 C 2-233 [» ]
2VHO X-ray 3.74 C 2-233 [» ]
2VHP X-ray 3.74 C 2-233 [» ]
2WWL electron microscopy 5.80 C 2-207 [» ]
2YKR electron microscopy 9.80 C 2-207 [» ]
2Z4K X-ray 4.45 C 2-233 [» ]
2Z4M X-ray 4.45 C 2-233 [» ]
3DF1 X-ray 3.50 C 2-232 [» ]
3DF3 X-ray 3.50 C 2-232 [» ]
3E1A electron microscopy - O 1-233 [» ]
3E1C electron microscopy - O 1-233 [» ]
3FIH electron microscopy 6.70 C 2-207 [» ]
3I1M X-ray 3.19 C 1-233 [» ]
3I1O X-ray 3.19 C 1-233 [» ]
3I1Q X-ray 3.81 C 1-233 [» ]
3I1S X-ray 3.81 C 1-233 [» ]
3I1Z X-ray 3.71 C 1-233 [» ]
3I21 X-ray 3.71 C 1-233 [» ]
3IZV electron microscopy - G 1-233 [» ]
3IZW electron microscopy - G 1-233 [» ]
3J00 electron microscopy - C 2-233 [» ]
3J0U electron microscopy 12.10 F 2-233 [» ]
3J0V electron microscopy 14.70 F 2-233 [» ]
3J0X electron microscopy 13.50 F 2-233 [» ]
3J0Z electron microscopy 11.50 F 2-233 [» ]
3J10 electron microscopy 11.50 F 2-233 [» ]
3J13 electron microscopy 13.10 E 2-233 [» ]
3J18 electron microscopy 8.30 C 2-207 [» ]
3J36 electron microscopy 9.80 C 2-233 [» ]
3J4V electron microscopy 12.00 C 1-207 [» ]
3J4W electron microscopy 12.00 C 1-207 [» ]
3J4Y electron microscopy 17.00 C 1-207 [» ]
3J4Z electron microscopy 20.00 C 1-207 [» ]
3J53 electron microscopy 13.00 C 1-207 [» ]
3J55 electron microscopy 15.00 C 1-207 [» ]
3J57 electron microscopy 17.00 C 1-207 [» ]
3J59 electron microscopy 12.00 C 1-207 [» ]
3J5B electron microscopy 17.00 C 1-207 [» ]
3J5D electron microscopy 17.00 C 1-207 [» ]
3J5F electron microscopy 20.00 C 1-207 [» ]
3J5H electron microscopy 15.00 C 1-207 [» ]
3J5J electron microscopy 9.00 C 1-207 [» ]
3J5N electron microscopy 6.80 C 1-233 [» ]
3J5T electron microscopy 7.60 C 2-233 [» ]
3J5X electron microscopy 7.60 C 2-233 [» ]
3KC4 electron microscopy - C 1-233 [» ]
3OAQ X-ray 3.25 C 2-207 [» ]
3OAR X-ray 3.25 C 2-207 [» ]
3OFA X-ray 3.19 C 2-207 [» ]
3OFB X-ray 3.19 C 2-207 [» ]
3OFO X-ray 3.10 C 2-207 [» ]
3OFP X-ray 3.10 C 2-207 [» ]
3OFX X-ray 3.29 C 2-207 [» ]
3OFY X-ray 3.29 C 2-207 [» ]
3OR9 X-ray 3.30 C 1-233 [» ]
3ORA X-ray 3.30 C 1-233 [» ]
3SFS X-ray 3.20 C 1-233 [» ]
3UOQ X-ray 3.70 C 1-233 [» ]
4A2I electron microscopy 16.50 C 2-207 [» ]
4ADV electron microscopy 13.50 C 2-233 [» ]
4GAQ X-ray 3.30 C 1-233 [» ]
4GAS X-ray 3.30 C 1-233 [» ]
4GD1 X-ray 3.00 C 2-207 [» ]
4GD2 X-ray 3.00 C 2-207 [» ]
4KIY X-ray 2.90 C 1-233 [» ]
4KJ0 X-ray 2.90 C 1-233 [» ]
4KJ2 X-ray 2.90 C 1-233 [» ]
4KJ4 X-ray 2.90 C 1-233 [» ]
4KJ6 X-ray 2.90 C 1-233 [» ]
4KJ8 X-ray 2.90 C 1-233 [» ]
4KJA X-ray 2.90 C 1-233 [» ]
4KJC X-ray 2.90 C 1-233 [» ]
4PE9 X-ray 2.95 C 2-207 [» ]
4PEA X-ray 2.95 C 2-207 [» ]
4TOL X-ray 3.00 C 2-207 [» ]
4TON X-ray 3.00 C 2-207 [» ]
4TOU X-ray 2.90 C 2-207 [» ]
4TOW X-ray 2.90 C 2-207 [» ]
4TP0 X-ray 2.90 C 2-207 [» ]
4TP2 X-ray 2.90 C 2-207 [» ]
4TP4 X-ray 2.90 C 2-207 [» ]
4TP6 X-ray 2.90 C 2-207 [» ]
4TP8 X-ray 2.80 C 2-207 [» ]
4TPA X-ray 2.80 C 2-207 [» ]
4TPC X-ray 2.80 C 2-207 [» ]
4TPE X-ray 2.80 C 2-207 [» ]
ProteinModelPortali P0A7V3.
SMRi P0A7V3. Positions 2-233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852126. 1 interaction.
DIPi DIP-35807N.
IntActi P0A7V3. 188 interactions.
MINTi MINT-6478122.
STRINGi 511145.b3314.

Chemistry

ChEMBLi CHEMBL2363135.
DrugBanki DB00759. Tetracycline.

Proteomic databases

PaxDbi P0A7V3.
PRIDEi P0A7V3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76339 ; AAC76339 ; b3314 .
BAE77977 ; BAE77977 ; BAE77977 .
GeneIDi 12932292.
947814.
KEGGi ecj:Y75_p3862.
eco:b3314.
PATRICi 32122060. VBIEscCol129921_3407.

Organism-specific databases

EchoBASEi EB0895.
EcoGenei EG10902. rpsC.

Phylogenomic databases

eggNOGi COG0092.
HOGENOMi HOG000210610.
InParanoidi P0A7V3.
KOi K02982.
OMAi IARAEWY.
OrthoDBi EOG6K13X3.
PhylomeDBi P0A7V3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10902-MONOMER.
ECOL316407:JW3276-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7V3.
PROi P0A7V3.

Gene expression databases

Genevestigatori P0A7V3.

Family and domain databases

Gene3Di 3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
HAMAPi MF_01309_B. Ribosomal_S3_B.
InterProi IPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR005704. Ribosomal_S3_bac.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
[Graphical view ]
Pfami PF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 1 hit.
[Graphical view ]
SUPFAMi SSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsi TIGR01009. rpsC_bact. 1 hit.
PROSITEi PS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(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 protein S3 from the small ribosomal subunit of Escherichia coli."
    Brauer D., Roming R.
    FEBS Lett. 106:352-357(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-233.
    Strain: K.
  5. "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 39-49 AND 87-108, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS3_ECOLI
AccessioniPrimary (citable) accession number: P0A7V3
Secondary accession number(s): P02352, Q2M6X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 104 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