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P0A7U3

- RS19_ECOLI

UniProt

P0A7U3 - RS19_ECOLI

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Protein

30S ribosomal protein S19

Gene

rpsS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:12859903), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (PubMed:16272117) 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.3 Publications
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA.

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S19
Gene namesi
Name:rpsS
Ordered Locus Names:b3316, JW3278
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10918. rpsS.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 929130S ribosomal protein S19PRO_0000129819Add
BLAST

Proteomic databases

PaxDbiP0A7U3.
PRIDEiP0A7U3.

Expressioni

Gene expression databases

GenevestigatoriP0A7U3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Binds S13 and L5 and cross-links to the A site tRNA.

Protein-protein interaction databases

BioGridi852123. 1 interaction.
DIPiDIP-47904N.
IntActiP0A7U3. 30 interactions.
STRINGi511145.b3316.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi13 – 208Combined sources
Turni21 – 255Combined sources
Beta strandi29 – 335Combined sources
Beta strandi37 – 393Combined sources
Helixi42 – 443Combined sources
Beta strandi48 – 525Combined sources
Beta strandi54 – 618Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Helixi71 – 744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-S3-81[»]
1P6Gelectron microscopy12.30S2-92[»]
1P87electron microscopy11.50S2-92[»]
1VS5X-ray3.46S1-92[»]
1VS7X-ray3.46S1-92[»]
2AVYX-ray3.46S2-92[»]
2AW7X-ray3.46S2-92[»]
2GY9electron microscopy15.00S2-88[»]
2GYBelectron microscopy15.00S2-88[»]
2I2PX-ray3.22S2-92[»]
2I2UX-ray3.22S2-92[»]
2QALX-ray3.21S2-92[»]
2QANX-ray3.21S2-92[»]
2QB9X-ray3.54S2-92[»]
2QBBX-ray3.54S2-92[»]
2QBDX-ray3.30S2-92[»]
2QBFX-ray3.30S2-92[»]
2QBHX-ray4.00S2-92[»]
2QBJX-ray4.00S2-92[»]
2QOUX-ray3.93S2-92[»]
2QOWX-ray3.93S2-92[»]
2QOYX-ray3.50S2-92[»]
2QP0X-ray3.50S2-92[»]
2VHOX-ray3.74S2-92[»]
2VHPX-ray3.74S2-92[»]
2WWLelectron microscopy5.80S3-81[»]
2YKRelectron microscopy9.80S3-81[»]
2Z4KX-ray4.45S2-92[»]
2Z4MX-ray4.45S2-92[»]
3DF1X-ray3.50S2-91[»]
3DF3X-ray3.50S2-91[»]
3E1Aelectron microscopy-L1-92[»]
3E1Celectron microscopy-L1-92[»]
3FIHelectron microscopy6.70S3-81[»]
3I1MX-ray3.19S1-92[»]
3I1OX-ray3.19S1-92[»]
3I1QX-ray3.81S1-92[»]
3I1SX-ray3.81S1-92[»]
3I1ZX-ray3.71S1-92[»]
3I21X-ray3.71S1-92[»]
3IZVelectron microscopy-W1-92[»]
3IZWelectron microscopy-W1-92[»]
3J00electron microscopy-S2-92[»]
3J0Uelectron microscopy12.10V2-92[»]
3J0Velectron microscopy14.70V2-92[»]
3J0Xelectron microscopy13.50V2-92[»]
3J0Zelectron microscopy11.50V2-92[»]
3J10electron microscopy11.50V2-92[»]
3J13electron microscopy13.10U2-92[»]
3J18electron microscopy8.30S3-81[»]
3J36electron microscopy9.80S2-92[»]
3J4Velectron microscopy12.00S3-81[»]
3J4Welectron microscopy12.00S3-81[»]
3J4Yelectron microscopy17.00S3-81[»]
3J4Zelectron microscopy20.00S3-81[»]
3J53electron microscopy13.00S3-81[»]
3J55electron microscopy15.00S3-81[»]
3J57electron microscopy17.00S3-81[»]
3J59electron microscopy12.00S3-81[»]
3J5Belectron microscopy17.00S3-81[»]
3J5Delectron microscopy17.00S3-81[»]
3J5Felectron microscopy20.00S3-81[»]
3J5Helectron microscopy15.00S3-81[»]
3J5Jelectron microscopy9.00S3-81[»]
3J5Nelectron microscopy6.80S1-92[»]
3J5Telectron microscopy7.60S2-92[»]
3J5Xelectron microscopy7.60S2-92[»]
3KC4electron microscopy-S1-92[»]
3OAQX-ray3.25S3-81[»]
3OARX-ray3.25S3-81[»]
3OFAX-ray3.19S3-81[»]
3OFBX-ray3.19S3-81[»]
3OFOX-ray3.10S3-81[»]
3OFPX-ray3.10S3-81[»]
3OFXX-ray3.29S3-81[»]
3OFYX-ray3.29S3-81[»]
3OR9X-ray3.30S1-92[»]
3ORAX-ray3.30S1-92[»]
3SFSX-ray3.20S1-92[»]
3UOQX-ray3.70S1-92[»]
4A2Ielectron microscopy16.50S3-81[»]
4ADVelectron microscopy13.50S2-92[»]
4GAQX-ray3.30S1-92[»]
4GASX-ray3.30S1-92[»]
4GD1X-ray3.00S3-81[»]
4GD2X-ray3.00S3-81[»]
4KIYX-ray2.90S1-92[»]
4KJ0X-ray2.90S1-92[»]
4KJ2X-ray2.90S1-92[»]
4KJ4X-ray2.90S1-92[»]
4KJ6X-ray2.90S1-92[»]
4KJ8X-ray2.90S1-92[»]
4KJAX-ray2.90S1-92[»]
4KJCX-ray2.90S1-92[»]
4PE9X-ray2.95S3-81[»]
4PEAX-ray2.95S3-81[»]
4TOLX-ray3.00S3-81[»]
4TONX-ray3.00S3-81[»]
4TOUX-ray2.90S3-81[»]
4TOWX-ray2.90S3-81[»]
4TP0X-ray2.90S3-81[»]
4TP2X-ray2.90S3-81[»]
4TP4X-ray2.90S3-81[»]
4TP6X-ray2.90S3-81[»]
4TP8X-ray2.80S3-81[»]
4TPAX-ray2.80S3-81[»]
4TPCX-ray2.80S3-81[»]
4TPEX-ray2.80S3-81[»]
DisProtiDP00147.
ProteinModelPortaliP0A7U3.
SMRiP0A7U3. Positions 2-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19P family.Curated

Phylogenomic databases

eggNOGiCOG0185.
HOGENOMiHOG000111560.
InParanoidiP0A7U3.
KOiK02965.
OMAiFIDHHLL.
OrthoDBiEOG61S365.
PhylomeDBiP0A7U3.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19.
InterProiIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01050. rpsS_bact. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7U3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA
60 70 80 90
VHNGRQHVPV FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK
Length:92
Mass (Da):10,430
Last modified:January 23, 2007 - v2
Checksum:i439F951848E95CB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 437RSTIFPN → STIFPDR AA sequence (PubMed:348496)Curated
Sequence conflicti86 – 861D → N AA sequence (PubMed:348496)Curated

Mass spectrometryi

Molecular mass is 10299.6 Da from positions 2 - 92. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831H → Y in MW145; suppresses a rimM deletion.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26464.1.
U18997 Genomic DNA. Translation: AAA58113.1.
U00096 Genomic DNA. Translation: AAC76341.1.
AP009048 Genomic DNA. Translation: BAE77975.1.
PIRiF23129. R3EC19.
RefSeqiNP_417775.1. NC_000913.3.
YP_492116.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.
GeneIDi12932294.
947811.
KEGGiecj:Y75_p3860.
eco:b3316.
PATRICi32122064. VBIEscCol129921_3409.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26464.1 .
U18997 Genomic DNA. Translation: AAA58113.1 .
U00096 Genomic DNA. Translation: AAC76341.1 .
AP009048 Genomic DNA. Translation: BAE77975.1 .
PIRi F23129. R3EC19.
RefSeqi NP_417775.1. NC_000913.3.
YP_492116.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - S 3-81 [» ]
1P6G electron microscopy 12.30 S 2-92 [» ]
1P87 electron microscopy 11.50 S 2-92 [» ]
1VS5 X-ray 3.46 S 1-92 [» ]
1VS7 X-ray 3.46 S 1-92 [» ]
2AVY X-ray 3.46 S 2-92 [» ]
2AW7 X-ray 3.46 S 2-92 [» ]
2GY9 electron microscopy 15.00 S 2-88 [» ]
2GYB electron microscopy 15.00 S 2-88 [» ]
2I2P X-ray 3.22 S 2-92 [» ]
2I2U X-ray 3.22 S 2-92 [» ]
2QAL X-ray 3.21 S 2-92 [» ]
2QAN X-ray 3.21 S 2-92 [» ]
2QB9 X-ray 3.54 S 2-92 [» ]
2QBB X-ray 3.54 S 2-92 [» ]
2QBD X-ray 3.30 S 2-92 [» ]
2QBF X-ray 3.30 S 2-92 [» ]
2QBH X-ray 4.00 S 2-92 [» ]
2QBJ X-ray 4.00 S 2-92 [» ]
2QOU X-ray 3.93 S 2-92 [» ]
2QOW X-ray 3.93 S 2-92 [» ]
2QOY X-ray 3.50 S 2-92 [» ]
2QP0 X-ray 3.50 S 2-92 [» ]
2VHO X-ray 3.74 S 2-92 [» ]
2VHP X-ray 3.74 S 2-92 [» ]
2WWL electron microscopy 5.80 S 3-81 [» ]
2YKR electron microscopy 9.80 S 3-81 [» ]
2Z4K X-ray 4.45 S 2-92 [» ]
2Z4M X-ray 4.45 S 2-92 [» ]
3DF1 X-ray 3.50 S 2-91 [» ]
3DF3 X-ray 3.50 S 2-91 [» ]
3E1A electron microscopy - L 1-92 [» ]
3E1C electron microscopy - L 1-92 [» ]
3FIH electron microscopy 6.70 S 3-81 [» ]
3I1M X-ray 3.19 S 1-92 [» ]
3I1O X-ray 3.19 S 1-92 [» ]
3I1Q X-ray 3.81 S 1-92 [» ]
3I1S X-ray 3.81 S 1-92 [» ]
3I1Z X-ray 3.71 S 1-92 [» ]
3I21 X-ray 3.71 S 1-92 [» ]
3IZV electron microscopy - W 1-92 [» ]
3IZW electron microscopy - W 1-92 [» ]
3J00 electron microscopy - S 2-92 [» ]
3J0U electron microscopy 12.10 V 2-92 [» ]
3J0V electron microscopy 14.70 V 2-92 [» ]
3J0X electron microscopy 13.50 V 2-92 [» ]
3J0Z electron microscopy 11.50 V 2-92 [» ]
3J10 electron microscopy 11.50 V 2-92 [» ]
3J13 electron microscopy 13.10 U 2-92 [» ]
3J18 electron microscopy 8.30 S 3-81 [» ]
3J36 electron microscopy 9.80 S 2-92 [» ]
3J4V electron microscopy 12.00 S 3-81 [» ]
3J4W electron microscopy 12.00 S 3-81 [» ]
3J4Y electron microscopy 17.00 S 3-81 [» ]
3J4Z electron microscopy 20.00 S 3-81 [» ]
3J53 electron microscopy 13.00 S 3-81 [» ]
3J55 electron microscopy 15.00 S 3-81 [» ]
3J57 electron microscopy 17.00 S 3-81 [» ]
3J59 electron microscopy 12.00 S 3-81 [» ]
3J5B electron microscopy 17.00 S 3-81 [» ]
3J5D electron microscopy 17.00 S 3-81 [» ]
3J5F electron microscopy 20.00 S 3-81 [» ]
3J5H electron microscopy 15.00 S 3-81 [» ]
3J5J electron microscopy 9.00 S 3-81 [» ]
3J5N electron microscopy 6.80 S 1-92 [» ]
3J5T electron microscopy 7.60 S 2-92 [» ]
3J5X electron microscopy 7.60 S 2-92 [» ]
3KC4 electron microscopy - S 1-92 [» ]
3OAQ X-ray 3.25 S 3-81 [» ]
3OAR X-ray 3.25 S 3-81 [» ]
3OFA X-ray 3.19 S 3-81 [» ]
3OFB X-ray 3.19 S 3-81 [» ]
3OFO X-ray 3.10 S 3-81 [» ]
3OFP X-ray 3.10 S 3-81 [» ]
3OFX X-ray 3.29 S 3-81 [» ]
3OFY X-ray 3.29 S 3-81 [» ]
3OR9 X-ray 3.30 S 1-92 [» ]
3ORA X-ray 3.30 S 1-92 [» ]
3SFS X-ray 3.20 S 1-92 [» ]
3UOQ X-ray 3.70 S 1-92 [» ]
4A2I electron microscopy 16.50 S 3-81 [» ]
4ADV electron microscopy 13.50 S 2-92 [» ]
4GAQ X-ray 3.30 S 1-92 [» ]
4GAS X-ray 3.30 S 1-92 [» ]
4GD1 X-ray 3.00 S 3-81 [» ]
4GD2 X-ray 3.00 S 3-81 [» ]
4KIY X-ray 2.90 S 1-92 [» ]
4KJ0 X-ray 2.90 S 1-92 [» ]
4KJ2 X-ray 2.90 S 1-92 [» ]
4KJ4 X-ray 2.90 S 1-92 [» ]
4KJ6 X-ray 2.90 S 1-92 [» ]
4KJ8 X-ray 2.90 S 1-92 [» ]
4KJA X-ray 2.90 S 1-92 [» ]
4KJC X-ray 2.90 S 1-92 [» ]
4PE9 X-ray 2.95 S 3-81 [» ]
4PEA X-ray 2.95 S 3-81 [» ]
4TOL X-ray 3.00 S 3-81 [» ]
4TON X-ray 3.00 S 3-81 [» ]
4TOU X-ray 2.90 S 3-81 [» ]
4TOW X-ray 2.90 S 3-81 [» ]
4TP0 X-ray 2.90 S 3-81 [» ]
4TP2 X-ray 2.90 S 3-81 [» ]
4TP4 X-ray 2.90 S 3-81 [» ]
4TP6 X-ray 2.90 S 3-81 [» ]
4TP8 X-ray 2.80 S 3-81 [» ]
4TPA X-ray 2.80 S 3-81 [» ]
4TPC X-ray 2.80 S 3-81 [» ]
4TPE X-ray 2.80 S 3-81 [» ]
DisProti DP00147.
ProteinModelPortali P0A7U3.
SMRi P0A7U3. Positions 2-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852123. 1 interaction.
DIPi DIP-47904N.
IntActi P0A7U3. 30 interactions.
STRINGi 511145.b3316.

Chemistry

ChEMBLi CHEMBL2363135.
DrugBanki DB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbi P0A7U3.
PRIDEi P0A7U3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76341 ; AAC76341 ; b3316 .
BAE77975 ; BAE77975 ; BAE77975 .
GeneIDi 12932294.
947811.
KEGGi ecj:Y75_p3860.
eco:b3316.
PATRICi 32122064. VBIEscCol129921_3409.

Organism-specific databases

EchoBASEi EB0911.
EcoGenei EG10918. rpsS.

Phylogenomic databases

eggNOGi COG0185.
HOGENOMi HOG000111560.
InParanoidi P0A7U3.
KOi K02965.
OMAi FIDHHLL.
OrthoDBi EOG61S365.
PhylomeDBi P0A7U3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7U3.
PROi P0A7U3.

Gene expression databases

Genevestigatori P0A7U3.

Family and domain databases

Gene3Di 3.30.860.10. 1 hit.
HAMAPi MF_00531. Ribosomal_S19.
InterProi IPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view ]
PANTHERi PTHR11880. PTHR11880. 1 hit.
Pfami PF00203. Ribosomal_S19. 1 hit.
[Graphical view ]
PIRSFi PIRSF002144. Ribosomal_S19. 1 hit.
PRINTSi PR00975. RIBOSOMALS19.
SUPFAMi SSF54570. SSF54570. 1 hit.
TIGRFAMsi TIGR01050. rpsS_bact. 1 hit.
PROSITEi PS00323. RIBOSOMAL_S19. 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. "Primary structure of protein S19 from the small ribosomal subunit of Escherichia coli."
    Yaguchi M., Wittmann H.G.
    FEBS Lett. 88:227-230(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-92.
    Strain: K.
  5. "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 66-70, CROSS-LINKING TO S13.
    Strain: K12 / A19.
  6. "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.
  7. "The PRC-barrel domain of the ribosome maturation protein RimM mediates binding to ribosomal protein S19 in the 30S ribosomal subunits."
    Loevgren J.M., Bylund G.O., Srivastava M.K., Lundberg L.A.C., Persson O.P., Wingsle G., Wikstroem P.M.
    RNA 10:1798-1812(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABILITY OF VARIANT MW145 TO SUPPRESS A RIMM DELETION.
    Strain: MW100.
  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), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  11. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE B1B.
    Strain: MRE-600.

Entry informationi

Entry nameiRS19_ECOLI
AccessioniPrimary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 103 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