Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0ADZ4

- RS15_ECOLI

UniProt

P0ADZ4 - RS15_ECOLI

(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)

Protein

30S ribosomal protein S15

Gene

rpsO

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

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations.2 Publications

GO - Molecular functioni

  1. rRNA binding Source: EcoliWiki
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. mRNA polyadenylation Source: EcoliWiki
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10914-MONOMER.
ECOL316407:JW3134-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S15UniRule annotation
Gene namesi
Name:rpsOUniRule annotation
Synonyms:secC
Ordered Locus Names:b3165, JW3134
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10914. rpsO.

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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 898830S ribosomal protein S15PRO_0000115437Add
BLAST

Proteomic databases

PaxDbiP0ADZ4.
PRIDEiP0ADZ4.

Expressioni

Gene expression databases

GenevestigatoriP0ADZ4.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.

Protein-protein interaction databases

DIPiDIP-47909N.
IntActiP0ADZ4. 30 interactions.
MINTiMINT-1299353.
STRINGi511145.b3165.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511
Beta strandi16 – 183
Helixi25 – 4218
Helixi50 – 7324
Helixi75 – 8410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50F1-89[»]
1P6Gelectron microscopy12.30O2-89[»]
1P87electron microscopy11.50O2-89[»]
2AVYX-ray3.46O1-89[»]
2AW7X-ray3.46O1-89[»]
2GY9electron microscopy15.00O3-88[»]
2GYBelectron microscopy15.00O3-88[»]
2QALX-ray3.21O1-89[»]
2QANX-ray3.21O1-89[»]
2QB9X-ray3.54O1-89[»]
2QBBX-ray3.54O1-89[»]
2QBDX-ray3.30O1-89[»]
2QBFX-ray3.30O1-89[»]
2QBHX-ray4.00O1-89[»]
2QBJX-ray4.00O1-89[»]
2QOUX-ray3.93O1-89[»]
2QOWX-ray3.93O1-89[»]
2QOYX-ray3.50O1-89[»]
2QP0X-ray3.50O1-89[»]
2VAZelectron microscopy10.00F2-89[»]
2WWLelectron microscopy5.80O2-89[»]
2YKRelectron microscopy9.80O2-89[»]
2Z4KX-ray4.45O1-89[»]
2Z4MX-ray4.45O1-89[»]
3DF1X-ray3.50O1-89[»]
3DF3X-ray3.50O1-89[»]
3E1Aelectron microscopy9.00H1-89[»]
3E1Celectron microscopy9.00H1-89[»]
3FIHelectron microscopy6.70O2-89[»]
3I1MX-ray3.19O1-89[»]
3I1OX-ray3.19O1-89[»]
3I1QX-ray3.81O1-89[»]
3I1SX-ray3.81O1-89[»]
3I1ZX-ray3.71O1-89[»]
3I21X-ray3.71O1-89[»]
3IZVelectron microscopy-S1-89[»]
3IZWelectron microscopy-S1-89[»]
3J00electron microscopy-O2-89[»]
3J18electron microscopy8.30O2-89[»]
3J36electron microscopy9.80O2-89[»]
3J4Velectron microscopy12.00O1-89[»]
3J4Welectron microscopy12.00O1-89[»]
3J4Yelectron microscopy17.00O1-89[»]
3J4Zelectron microscopy20.00O1-89[»]
3J53electron microscopy13.00O1-89[»]
3J55electron microscopy15.00O1-89[»]
3J57electron microscopy17.00O1-89[»]
3J59electron microscopy12.00O1-89[»]
3J5Belectron microscopy17.00O1-89[»]
3J5Delectron microscopy17.00O1-89[»]
3J5Felectron microscopy20.00O1-89[»]
3J5Helectron microscopy15.00O1-89[»]
3J5Jelectron microscopy9.00O1-89[»]
3J5Nelectron microscopy6.80O1-89[»]
3J5Telectron microscopy7.60O2-89[»]
3J5Xelectron microscopy7.60O2-89[»]
3KC4electron microscopy-O1-89[»]
3OAQX-ray3.25O2-89[»]
3OARX-ray3.25O2-89[»]
3OFAX-ray3.19O2-89[»]
3OFBX-ray3.19O2-89[»]
3OFOX-ray3.10O2-89[»]
3OFPX-ray3.10O2-89[»]
3OFXX-ray3.29O2-89[»]
3OFYX-ray3.29O2-89[»]
3OR9X-ray3.30O1-89[»]
3ORAX-ray3.30O1-89[»]
3SFSX-ray3.20O1-89[»]
3UOQX-ray3.70O1-89[»]
4A2Ielectron microscopy16.50O2-89[»]
4ADVelectron microscopy13.50O1-89[»]
4GAQX-ray3.30O1-89[»]
4GASX-ray3.30O1-89[»]
4GD1X-ray3.00O2-89[»]
4GD2X-ray3.00O2-89[»]
4KIYX-ray2.90O1-89[»]
4KJ0X-ray2.90O1-89[»]
4KJ2X-ray2.90O1-89[»]
4KJ4X-ray2.90O1-89[»]
4KJ6X-ray2.90O1-89[»]
4KJ8X-ray2.90O1-89[»]
4KJAX-ray2.90O1-89[»]
4KJCX-ray2.90O1-89[»]
4PE9X-ray2.95O2-89[»]
4PEAX-ray2.95O2-89[»]
4TOLX-ray3.00O2-89[»]
4TONX-ray3.00O2-89[»]
4TOUX-ray2.90O2-89[»]
4TOWX-ray2.90O2-89[»]
4TP0X-ray2.90O2-89[»]
4TP2X-ray2.90O2-89[»]
4TP4X-ray2.90O2-89[»]
4TP6X-ray2.90O2-89[»]
4TP8X-ray2.80O2-89[»]
4TPAX-ray2.80O2-89[»]
4TPCX-ray2.80O2-89[»]
4TPEX-ray2.80O2-89[»]
ProteinModelPortaliP0ADZ4.
SMRiP0ADZ4. Positions 3-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADZ4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S15P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0184.
HOGENOMiHOG000040097.
InParanoidiP0ADZ4.
KOiK02956.
OMAiNKQDHHS.
OrthoDBiEOG6B368J.
PhylomeDBiP0ADZ4.

Family and domain databases

Gene3Di1.10.287.10. 1 hit.
HAMAPiMF_01343_B. Ribosomal_S15_B.
InterProiIPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
TIGRFAMsiTIGR00952. S15_bact. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0ADZ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLSTEATAK IVSEFGRDAN DTGSTEVQVA LLTAQINHLQ GHFAEHKKDH
60 70 80
HSRRGLLRMV SQRRKLLDYL KRKDVARYTQ LIERLGLRR
Length:89
Mass (Da):10,269
Last modified:January 23, 2007 - v2
Checksum:iAABDDA6674B99B1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661Missing(PubMed:3005122)Curated

Mass spectrometryi

Molecular mass is 10137.6 Da from positions 2 - 89. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01073 Genomic DNA. Translation: CAA25536.1.
X00761 Genomic DNA. Translation: CAA25331.1.
M14425 Genomic DNA. Translation: AAA24595.1.
J02638 Genomic DNA. Translation: AAA83904.1.
U18997 Genomic DNA. Translation: AAA57968.1.
U00096 Genomic DNA. Translation: AAC76199.1.
AP009048 Genomic DNA. Translation: BAE77211.1.
X13775 Genomic DNA. Translation: CAA32022.1.
PIRiB26118. R3EC15.
RefSeqiNP_417634.1. NC_000913.3.
YP_491352.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76199; AAC76199; b3165.
BAE77211; BAE77211; BAE77211.
GeneIDi12933439.
947686.
KEGGiecj:Y75_p3087.
eco:b3165.
PATRICi32121748. VBIEscCol129921_3260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01073 Genomic DNA. Translation: CAA25536.1 .
X00761 Genomic DNA. Translation: CAA25331.1 .
M14425 Genomic DNA. Translation: AAA24595.1 .
J02638 Genomic DNA. Translation: AAA83904.1 .
U18997 Genomic DNA. Translation: AAA57968.1 .
U00096 Genomic DNA. Translation: AAC76199.1 .
AP009048 Genomic DNA. Translation: BAE77211.1 .
X13775 Genomic DNA. Translation: CAA32022.1 .
PIRi B26118. R3EC15.
RefSeqi NP_417634.1. NC_000913.3.
YP_491352.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 F 1-89 [» ]
1P6G electron microscopy 12.30 O 2-89 [» ]
1P87 electron microscopy 11.50 O 2-89 [» ]
2AVY X-ray 3.46 O 1-89 [» ]
2AW7 X-ray 3.46 O 1-89 [» ]
2GY9 electron microscopy 15.00 O 3-88 [» ]
2GYB electron microscopy 15.00 O 3-88 [» ]
2QAL X-ray 3.21 O 1-89 [» ]
2QAN X-ray 3.21 O 1-89 [» ]
2QB9 X-ray 3.54 O 1-89 [» ]
2QBB X-ray 3.54 O 1-89 [» ]
2QBD X-ray 3.30 O 1-89 [» ]
2QBF X-ray 3.30 O 1-89 [» ]
2QBH X-ray 4.00 O 1-89 [» ]
2QBJ X-ray 4.00 O 1-89 [» ]
2QOU X-ray 3.93 O 1-89 [» ]
2QOW X-ray 3.93 O 1-89 [» ]
2QOY X-ray 3.50 O 1-89 [» ]
2QP0 X-ray 3.50 O 1-89 [» ]
2VAZ electron microscopy 10.00 F 2-89 [» ]
2WWL electron microscopy 5.80 O 2-89 [» ]
2YKR electron microscopy 9.80 O 2-89 [» ]
2Z4K X-ray 4.45 O 1-89 [» ]
2Z4M X-ray 4.45 O 1-89 [» ]
3DF1 X-ray 3.50 O 1-89 [» ]
3DF3 X-ray 3.50 O 1-89 [» ]
3E1A electron microscopy 9.00 H 1-89 [» ]
3E1C electron microscopy 9.00 H 1-89 [» ]
3FIH electron microscopy 6.70 O 2-89 [» ]
3I1M X-ray 3.19 O 1-89 [» ]
3I1O X-ray 3.19 O 1-89 [» ]
3I1Q X-ray 3.81 O 1-89 [» ]
3I1S X-ray 3.81 O 1-89 [» ]
3I1Z X-ray 3.71 O 1-89 [» ]
3I21 X-ray 3.71 O 1-89 [» ]
3IZV electron microscopy - S 1-89 [» ]
3IZW electron microscopy - S 1-89 [» ]
3J00 electron microscopy - O 2-89 [» ]
3J18 electron microscopy 8.30 O 2-89 [» ]
3J36 electron microscopy 9.80 O 2-89 [» ]
3J4V electron microscopy 12.00 O 1-89 [» ]
3J4W electron microscopy 12.00 O 1-89 [» ]
3J4Y electron microscopy 17.00 O 1-89 [» ]
3J4Z electron microscopy 20.00 O 1-89 [» ]
3J53 electron microscopy 13.00 O 1-89 [» ]
3J55 electron microscopy 15.00 O 1-89 [» ]
3J57 electron microscopy 17.00 O 1-89 [» ]
3J59 electron microscopy 12.00 O 1-89 [» ]
3J5B electron microscopy 17.00 O 1-89 [» ]
3J5D electron microscopy 17.00 O 1-89 [» ]
3J5F electron microscopy 20.00 O 1-89 [» ]
3J5H electron microscopy 15.00 O 1-89 [» ]
3J5J electron microscopy 9.00 O 1-89 [» ]
3J5N electron microscopy 6.80 O 1-89 [» ]
3J5T electron microscopy 7.60 O 2-89 [» ]
3J5X electron microscopy 7.60 O 2-89 [» ]
3KC4 electron microscopy - O 1-89 [» ]
3OAQ X-ray 3.25 O 2-89 [» ]
3OAR X-ray 3.25 O 2-89 [» ]
3OFA X-ray 3.19 O 2-89 [» ]
3OFB X-ray 3.19 O 2-89 [» ]
3OFO X-ray 3.10 O 2-89 [» ]
3OFP X-ray 3.10 O 2-89 [» ]
3OFX X-ray 3.29 O 2-89 [» ]
3OFY X-ray 3.29 O 2-89 [» ]
3OR9 X-ray 3.30 O 1-89 [» ]
3ORA X-ray 3.30 O 1-89 [» ]
3SFS X-ray 3.20 O 1-89 [» ]
3UOQ X-ray 3.70 O 1-89 [» ]
4A2I electron microscopy 16.50 O 2-89 [» ]
4ADV electron microscopy 13.50 O 1-89 [» ]
4GAQ X-ray 3.30 O 1-89 [» ]
4GAS X-ray 3.30 O 1-89 [» ]
4GD1 X-ray 3.00 O 2-89 [» ]
4GD2 X-ray 3.00 O 2-89 [» ]
4KIY X-ray 2.90 O 1-89 [» ]
4KJ0 X-ray 2.90 O 1-89 [» ]
4KJ2 X-ray 2.90 O 1-89 [» ]
4KJ4 X-ray 2.90 O 1-89 [» ]
4KJ6 X-ray 2.90 O 1-89 [» ]
4KJ8 X-ray 2.90 O 1-89 [» ]
4KJA X-ray 2.90 O 1-89 [» ]
4KJC X-ray 2.90 O 1-89 [» ]
4PE9 X-ray 2.95 O 2-89 [» ]
4PEA X-ray 2.95 O 2-89 [» ]
4TOL X-ray 3.00 O 2-89 [» ]
4TON X-ray 3.00 O 2-89 [» ]
4TOU X-ray 2.90 O 2-89 [» ]
4TOW X-ray 2.90 O 2-89 [» ]
4TP0 X-ray 2.90 O 2-89 [» ]
4TP2 X-ray 2.90 O 2-89 [» ]
4TP4 X-ray 2.90 O 2-89 [» ]
4TP6 X-ray 2.90 O 2-89 [» ]
4TP8 X-ray 2.80 O 2-89 [» ]
4TPA X-ray 2.80 O 2-89 [» ]
4TPC X-ray 2.80 O 2-89 [» ]
4TPE X-ray 2.80 O 2-89 [» ]
ProteinModelPortali P0ADZ4.
SMRi P0ADZ4. Positions 3-88.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47909N.
IntActi P0ADZ4. 30 interactions.
MINTi MINT-1299353.
STRINGi 511145.b3165.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0ADZ4.
PRIDEi P0ADZ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76199 ; AAC76199 ; b3165 .
BAE77211 ; BAE77211 ; BAE77211 .
GeneIDi 12933439.
947686.
KEGGi ecj:Y75_p3087.
eco:b3165.
PATRICi 32121748. VBIEscCol129921_3260.

Organism-specific databases

EchoBASEi EB0907.
EcoGenei EG10914. rpsO.

Phylogenomic databases

eggNOGi COG0184.
HOGENOMi HOG000040097.
InParanoidi P0ADZ4.
KOi K02956.
OMAi NKQDHHS.
OrthoDBi EOG6B368J.
PhylomeDBi P0ADZ4.

Enzyme and pathway databases

BioCyci EcoCyc:EG10914-MONOMER.
ECOL316407:JW3134-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ADZ4.
PROi P0ADZ4.

Gene expression databases

Genevestigatori P0ADZ4.

Family and domain databases

Gene3Di 1.10.287.10. 1 hit.
HAMAPi MF_01343_B. Ribosomal_S15_B.
InterProi IPR000589. Ribosomal_S15.
IPR005290. Ribosomal_S15_bac-type.
IPR009068. S15_NS1_RNA-bd.
[Graphical view ]
Pfami PF00312. Ribosomal_S15. 1 hit.
[Graphical view ]
SUPFAMi SSF47060. SSF47060. 1 hit.
TIGRFAMsi TIGR00952. S15_bact. 1 hit.
PROSITEi PS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO)."
    Takata R., Mukai T., Aoyagi M., Hori K.
    Mol. Gen. Genet. 197:225-229(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions."
    Portier C., Regnier P.
    Nucleic Acids Res. 12:6091-6102(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli."
    Evans S., Dennis P.P.
    Gene 40:15-22(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1."
    Regnier P., Grunberg-Manago M., Portier C.
    J. Biol. Chem. 262:63-68(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "Primary structure of the 16S rRNA binding protein S15 from Escherichia coli ribosomes."
    Morinaga T., Funatsu G., Funatsu M., Wittmann H.G.
    FEBS Lett. 64:307-309(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-89.
    Strain: K.
  8. "The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping."
    Sands J.F., Regnier P., Cummings H.S., Grunberg-Manago M., Hershey J.W.B.
    Nucleic Acids Res. 16:10803-10816(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  9. "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.
  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), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE.
    Strain: MRE-600.

Entry informationi

Entry nameiRS15_ECOLI
AccessioniPrimary (citable) accession number: P0ADZ4
Secondary accession number(s): P02371, Q2M945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 89 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