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P0A7T3

- RS16_ECOLI

UniProt

P0A7T3 - RS16_ECOLI

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Protein

30S ribosomal protein S16

Gene

rpsP

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

Functioni

In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity.1 Publication
In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes.1 Publication

GO - Molecular functioni

  1. endodeoxyribonuclease activity Source: EcoCyc
  2. structural constituent of ribosome Source: InterPro
  3. structure-specific DNA binding Source: EcoCyc

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: GOC
  2. ribosomal small subunit assembly Source: EcoCyc
  3. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10915-MONOMER.
ECOL316407:JW2590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S16UniRule annotation
Gene namesi
Name:rpsPUniRule annotation
Ordered Locus Names:b2609, JW2590
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10915. rpsP.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 828230S ribosomal protein S16PRO_0000167184Add
BLAST

Proteomic databases

PaxDbiP0A7T3.
PRIDEiP0A7T3.

Expressioni

Inductioni

Part of the rpsP-rimM-trmD-rplS operon.

Gene expression databases

GenevestigatoriP0A7T3.

Interactioni

Protein-protein interaction databases

DIPiDIP-47829N.
IntActiP0A7T3. 55 interactions.
MINTiMINT-1280042.
STRINGi511145.b2609.

Structurei

Secondary structure

1
82
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi9 – 113Combined sources
Beta strandi12 – 143Combined sources
Beta strandi17 – 237Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 303Combined sources
Beta strandi33 – 353Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi49 – 524Combined sources
Helixi54 – 6310Combined sources
Helixi69 – 757Combined sources
Turni76 – 783Combined sources
Turni79 – 813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-P1-82[»]
1ML5electron microscopy14.00S1-82[»]
1P6Gelectron microscopy12.30P1-82[»]
1P87electron microscopy11.50P1-82[»]
1VS5X-ray3.46P1-82[»]
1VS7X-ray3.46P1-82[»]
2AVYX-ray3.46P1-82[»]
2AW7X-ray3.46P1-82[»]
2GY9electron microscopy15.00P1-78[»]
2GYBelectron microscopy15.00P1-78[»]
2I2PX-ray3.22P1-82[»]
2I2UX-ray3.22P1-82[»]
2QALX-ray3.21P1-82[»]
2QANX-ray3.21P1-82[»]
2QB9X-ray3.54P1-82[»]
2QBBX-ray3.54P1-82[»]
2QBDX-ray3.30P1-82[»]
2QBFX-ray3.30P1-82[»]
2QBHX-ray4.00P1-82[»]
2QBJX-ray4.00P1-82[»]
2QOUX-ray3.93P1-82[»]
2QOWX-ray3.93P1-82[»]
2QOYX-ray3.50P1-82[»]
2QP0X-ray3.50P1-82[»]
2VHOX-ray3.74P1-82[»]
2VHPX-ray3.74P1-82[»]
2WWLelectron microscopy5.80P1-80[»]
2YKRelectron microscopy9.80P1-82[»]
2Z4KX-ray4.45P1-82[»]
2Z4MX-ray4.45P1-82[»]
3DF1X-ray3.50P1-82[»]
3DF3X-ray3.50P1-82[»]
3E1Aelectron microscopy-I1-82[»]
3E1Celectron microscopy-I1-82[»]
3FIHelectron microscopy6.70P1-80[»]
3I1MX-ray3.19P1-82[»]
3I1OX-ray3.19P1-82[»]
3I1QX-ray3.81P1-82[»]
3I1SX-ray3.81P1-82[»]
3I1ZX-ray3.71P1-82[»]
3I21X-ray3.71P1-82[»]
3IZVelectron microscopy-T1-82[»]
3IZWelectron microscopy-T1-82[»]
3J00electron microscopy-P1-82[»]
3J0Uelectron microscopy12.10S1-82[»]
3J0Velectron microscopy14.70S1-82[»]
3J0Xelectron microscopy13.50S1-82[»]
3J0Zelectron microscopy11.50S1-82[»]
3J10electron microscopy11.50S1-82[»]
3J13electron microscopy13.10R1-82[»]
3J18electron microscopy8.30P1-82[»]
3J36electron microscopy9.80P1-82[»]
3J4Velectron microscopy12.00P1-80[»]
3J4Welectron microscopy12.00P1-80[»]
3J4Yelectron microscopy17.00P1-80[»]
3J4Zelectron microscopy20.00P1-80[»]
3J53electron microscopy13.00P1-80[»]
3J55electron microscopy15.00P1-80[»]
3J57electron microscopy17.00P1-80[»]
3J59electron microscopy12.00P1-80[»]
3J5Belectron microscopy17.00P1-80[»]
3J5Delectron microscopy17.00P1-80[»]
3J5Felectron microscopy20.00P1-80[»]
3J5Helectron microscopy15.00P1-80[»]
3J5Jelectron microscopy9.00P1-80[»]
3J5Nelectron microscopy6.80P1-82[»]
3J5Telectron microscopy7.60P1-82[»]
3J5Xelectron microscopy7.60P1-82[»]
3KC4electron microscopy-P1-82[»]
3OAQX-ray3.25P1-82[»]
3OARX-ray3.25P1-80[»]
3OFAX-ray3.19P1-82[»]
3OFBX-ray3.19P1-80[»]
3OFOX-ray3.10P1-82[»]
3OFPX-ray3.10P1-80[»]
3OFXX-ray3.29P1-82[»]
3OFYX-ray3.29P1-80[»]
3OR9X-ray3.30P1-82[»]
3ORAX-ray3.30P1-82[»]
3SFSX-ray3.20P1-82[»]
3UOQX-ray3.70P1-82[»]
4A2Ielectron microscopy16.50P1-82[»]
4ADVelectron microscopy13.50P1-82[»]
4GAQX-ray3.30P1-82[»]
4GASX-ray3.30P1-82[»]
4GD1X-ray3.00P1-82[»]
4GD2X-ray3.00P1-82[»]
4KIYX-ray2.90P1-82[»]
4KJ0X-ray2.90P1-82[»]
4KJ2X-ray2.90P1-82[»]
4KJ4X-ray2.90P1-82[»]
4KJ6X-ray2.90P1-82[»]
4KJ8X-ray2.90P1-82[»]
4KJAX-ray2.90P1-82[»]
4KJCX-ray2.90P1-82[»]
4PE9X-ray2.95P1-82[»]
4PEAX-ray2.95P1-82[»]
4TOLX-ray3.00P1-82[»]
4TONX-ray3.00P1-82[»]
4TOUX-ray2.90P1-82[»]
4TOWX-ray2.90P1-82[»]
4TP0X-ray2.90P1-82[»]
4TP2X-ray2.90P1-82[»]
4TP4X-ray2.90P1-82[»]
4TP6X-ray2.90P1-82[»]
4TP8X-ray2.80P1-82[»]
4TPAX-ray2.80P1-82[»]
4TPCX-ray2.80P1-82[»]
4TPEX-ray2.80P1-82[»]
ProteinModelPortaliP0A7T3.
SMRiP0A7T3. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7T3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S16P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0228.
HOGENOMiHOG000246720.
InParanoidiP0A7T3.
KOiK02959.
OMAiRVEHWVG.
OrthoDBiEOG6CVVKH.
PhylomeDBiP0A7T3.

Family and domain databases

Gene3Di3.30.1320.10. 1 hit.
HAMAPiMF_00385. Ribosomal_S16.
InterProiIPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view]
PANTHERiPTHR12919. PTHR12919. 1 hit.
PfamiPF00886. Ribosomal_S16. 1 hit.
[Graphical view]
SUPFAMiSSF54565. SSF54565. 1 hit.
TIGRFAMsiTIGR00002. S16. 1 hit.
PROSITEiPS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7T3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVTIRLARHG AKKRPFYQVV VADSRNARNG RFIERVGFFN PIASEKEEGT
60 70 80
RLDLDRIAHW VGQGATISDR VAALIKEVNK AA
Length:82
Mass (Da):9,191
Last modified:July 21, 1986 - v1
Checksum:iF94D07049A6D489D
GO

Mass spectrometryi

Molecular mass is 9190.5 Da from positions 1 - 82. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25958.1.
U00096 Genomic DNA. Translation: AAC75658.1.
AP009048 Genomic DNA. Translation: BAA16494.2.
PIRiS07948. R3EC16.
RefSeqiNP_417100.1. NC_000913.3.
YP_490832.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneIDi12930606.
947103.
KEGGiecj:Y75_p2557.
eco:b2609.
PATRICi32120617. VBIEscCol129921_2707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25958.1 .
U00096 Genomic DNA. Translation: AAC75658.1 .
AP009048 Genomic DNA. Translation: BAA16494.2 .
PIRi S07948. R3EC16.
RefSeqi NP_417100.1. NC_000913.3.
YP_490832.1. 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 - P 1-82 [» ]
1ML5 electron microscopy 14.00 S 1-82 [» ]
1P6G electron microscopy 12.30 P 1-82 [» ]
1P87 electron microscopy 11.50 P 1-82 [» ]
1VS5 X-ray 3.46 P 1-82 [» ]
1VS7 X-ray 3.46 P 1-82 [» ]
2AVY X-ray 3.46 P 1-82 [» ]
2AW7 X-ray 3.46 P 1-82 [» ]
2GY9 electron microscopy 15.00 P 1-78 [» ]
2GYB electron microscopy 15.00 P 1-78 [» ]
2I2P X-ray 3.22 P 1-82 [» ]
2I2U X-ray 3.22 P 1-82 [» ]
2QAL X-ray 3.21 P 1-82 [» ]
2QAN X-ray 3.21 P 1-82 [» ]
2QB9 X-ray 3.54 P 1-82 [» ]
2QBB X-ray 3.54 P 1-82 [» ]
2QBD X-ray 3.30 P 1-82 [» ]
2QBF X-ray 3.30 P 1-82 [» ]
2QBH X-ray 4.00 P 1-82 [» ]
2QBJ X-ray 4.00 P 1-82 [» ]
2QOU X-ray 3.93 P 1-82 [» ]
2QOW X-ray 3.93 P 1-82 [» ]
2QOY X-ray 3.50 P 1-82 [» ]
2QP0 X-ray 3.50 P 1-82 [» ]
2VHO X-ray 3.74 P 1-82 [» ]
2VHP X-ray 3.74 P 1-82 [» ]
2WWL electron microscopy 5.80 P 1-80 [» ]
2YKR electron microscopy 9.80 P 1-82 [» ]
2Z4K X-ray 4.45 P 1-82 [» ]
2Z4M X-ray 4.45 P 1-82 [» ]
3DF1 X-ray 3.50 P 1-82 [» ]
3DF3 X-ray 3.50 P 1-82 [» ]
3E1A electron microscopy - I 1-82 [» ]
3E1C electron microscopy - I 1-82 [» ]
3FIH electron microscopy 6.70 P 1-80 [» ]
3I1M X-ray 3.19 P 1-82 [» ]
3I1O X-ray 3.19 P 1-82 [» ]
3I1Q X-ray 3.81 P 1-82 [» ]
3I1S X-ray 3.81 P 1-82 [» ]
3I1Z X-ray 3.71 P 1-82 [» ]
3I21 X-ray 3.71 P 1-82 [» ]
3IZV electron microscopy - T 1-82 [» ]
3IZW electron microscopy - T 1-82 [» ]
3J00 electron microscopy - P 1-82 [» ]
3J0U electron microscopy 12.10 S 1-82 [» ]
3J0V electron microscopy 14.70 S 1-82 [» ]
3J0X electron microscopy 13.50 S 1-82 [» ]
3J0Z electron microscopy 11.50 S 1-82 [» ]
3J10 electron microscopy 11.50 S 1-82 [» ]
3J13 electron microscopy 13.10 R 1-82 [» ]
3J18 electron microscopy 8.30 P 1-82 [» ]
3J36 electron microscopy 9.80 P 1-82 [» ]
3J4V electron microscopy 12.00 P 1-80 [» ]
3J4W electron microscopy 12.00 P 1-80 [» ]
3J4Y electron microscopy 17.00 P 1-80 [» ]
3J4Z electron microscopy 20.00 P 1-80 [» ]
3J53 electron microscopy 13.00 P 1-80 [» ]
3J55 electron microscopy 15.00 P 1-80 [» ]
3J57 electron microscopy 17.00 P 1-80 [» ]
3J59 electron microscopy 12.00 P 1-80 [» ]
3J5B electron microscopy 17.00 P 1-80 [» ]
3J5D electron microscopy 17.00 P 1-80 [» ]
3J5F electron microscopy 20.00 P 1-80 [» ]
3J5H electron microscopy 15.00 P 1-80 [» ]
3J5J electron microscopy 9.00 P 1-80 [» ]
3J5N electron microscopy 6.80 P 1-82 [» ]
3J5T electron microscopy 7.60 P 1-82 [» ]
3J5X electron microscopy 7.60 P 1-82 [» ]
3KC4 electron microscopy - P 1-82 [» ]
3OAQ X-ray 3.25 P 1-82 [» ]
3OAR X-ray 3.25 P 1-80 [» ]
3OFA X-ray 3.19 P 1-82 [» ]
3OFB X-ray 3.19 P 1-80 [» ]
3OFO X-ray 3.10 P 1-82 [» ]
3OFP X-ray 3.10 P 1-80 [» ]
3OFX X-ray 3.29 P 1-82 [» ]
3OFY X-ray 3.29 P 1-80 [» ]
3OR9 X-ray 3.30 P 1-82 [» ]
3ORA X-ray 3.30 P 1-82 [» ]
3SFS X-ray 3.20 P 1-82 [» ]
3UOQ X-ray 3.70 P 1-82 [» ]
4A2I electron microscopy 16.50 P 1-82 [» ]
4ADV electron microscopy 13.50 P 1-82 [» ]
4GAQ X-ray 3.30 P 1-82 [» ]
4GAS X-ray 3.30 P 1-82 [» ]
4GD1 X-ray 3.00 P 1-82 [» ]
4GD2 X-ray 3.00 P 1-82 [» ]
4KIY X-ray 2.90 P 1-82 [» ]
4KJ0 X-ray 2.90 P 1-82 [» ]
4KJ2 X-ray 2.90 P 1-82 [» ]
4KJ4 X-ray 2.90 P 1-82 [» ]
4KJ6 X-ray 2.90 P 1-82 [» ]
4KJ8 X-ray 2.90 P 1-82 [» ]
4KJA X-ray 2.90 P 1-82 [» ]
4KJC X-ray 2.90 P 1-82 [» ]
4PE9 X-ray 2.95 P 1-82 [» ]
4PEA X-ray 2.95 P 1-82 [» ]
4TOL X-ray 3.00 P 1-82 [» ]
4TON X-ray 3.00 P 1-82 [» ]
4TOU X-ray 2.90 P 1-82 [» ]
4TOW X-ray 2.90 P 1-82 [» ]
4TP0 X-ray 2.90 P 1-82 [» ]
4TP2 X-ray 2.90 P 1-82 [» ]
4TP4 X-ray 2.90 P 1-82 [» ]
4TP6 X-ray 2.90 P 1-82 [» ]
4TP8 X-ray 2.80 P 1-82 [» ]
4TPA X-ray 2.80 P 1-82 [» ]
4TPC X-ray 2.80 P 1-82 [» ]
4TPE X-ray 2.80 P 1-82 [» ]
ProteinModelPortali P0A7T3.
SMRi P0A7T3. Positions 1-82.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47829N.
IntActi P0A7T3. 55 interactions.
MINTi MINT-1280042.
STRINGi 511145.b2609.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7T3.
PRIDEi P0A7T3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75658 ; AAC75658 ; b2609 .
BAA16494 ; BAA16494 ; BAA16494 .
GeneIDi 12930606.
947103.
KEGGi ecj:Y75_p2557.
eco:b2609.
PATRICi 32120617. VBIEscCol129921_2707.

Organism-specific databases

EchoBASEi EB0908.
EcoGenei EG10915. rpsP.

Phylogenomic databases

eggNOGi COG0228.
HOGENOMi HOG000246720.
InParanoidi P0A7T3.
KOi K02959.
OMAi RVEHWVG.
OrthoDBi EOG6CVVKH.
PhylomeDBi P0A7T3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10915-MONOMER.
ECOL316407:JW2590-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7T3.
PROi P0A7T3.

Gene expression databases

Genevestigatori P0A7T3.

Family and domain databases

Gene3Di 3.30.1320.10. 1 hit.
HAMAPi MF_00385. Ribosomal_S16.
InterProi IPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view ]
PANTHERi PTHR12919. PTHR12919. 1 hit.
Pfami PF00886. Ribosomal_S16. 1 hit.
[Graphical view ]
SUPFAMi SSF54565. SSF54565. 1 hit.
TIGRFAMsi TIGR00002. S16. 1 hit.
PROSITEi PS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete amino acid sequence of protein S16 from Escherichia coli."
    Vandekerckhove J., Rombauts W., Wittmann-Liebold B.
    Hoppe-Seyler's Z. Physiol. Chem. 358:989-1002(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
    Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
    EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
    Strain: K12.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION AS AN ENDONUCLEASE.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Hybrid protein between ribosomal protein S16 and RimM of Escherichia coli retains the ribosome maturation function of both proteins."
    Loevgren J.M., Wikstroem P.M.
    J. Bacteriol. 183:5352-5357(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUSION WITH RIBOSOME MATURATION FACTOR RIMM.
    Strain: MW100.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS16_ECOLI
AccessioniPrimary (citable) accession number: P0A7T3
Secondary accession number(s): P02372, P77006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 94 of the entry and version 1 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