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P0A7K6

- RL19_ECOLI

UniProt

P0A7K6 - RL19_ECOLI

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Protein

50S ribosomal protein L19

Gene

rplS

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

Functioni

This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.2 Publications

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10880-MONOMER.
ECOL316407:JW2587-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L19
Gene namesi
Name:rplS
Ordered Locus Names:b2606, JW2587
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10880. rplS.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11511450S ribosomal protein L19PRO_0000163451Add
BLAST

Proteomic databases

PaxDbiP0A7K6.
PRIDEiP0A7K6.

PTM databases

PhosSiteiP0810432.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriP0A7K6.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L14 (PubMed:2665813 and PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA.

Binary interactionsi

WithEntry#Exp.IntActNotes
nanEP0A7611EBI-543891,EBI-561432

Protein-protein interaction databases

DIPiDIP-35793N.
IntActiP0A7K6. 101 interactions.
MINTiMINT-1245288.
STRINGi511145.b2606.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107
Beta strandi27 – 337
Turni34 – 363
Beta strandi38 – 447
Beta strandi46 – 505
Helixi54 – 563
Beta strandi58 – 625
Beta strandi66 – 683
Beta strandi70 – 756
Beta strandi76 – 783
Helixi79 – 813
Beta strandi83 – 853
Beta strandi86 – 883
Beta strandi93 – 953
Helixi98 – 1025
Helixi105 – 1073

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30N2-115[»]
1P86electron microscopy11.50N2-115[»]
1VS6X-ray3.46P1-115[»]
1VS8X-ray3.46P1-115[»]
1VT2X-ray3.30P1-115[»]
2AW4X-ray3.46P2-115[»]
2AWBX-ray3.46P2-115[»]
2GYAelectron microscopy15.00N2-115[»]
2GYCelectron microscopy15.00N2-115[»]
2I2TX-ray3.22P2-115[»]
2I2VX-ray3.22P2-115[»]
2J28electron microscopy8.00P2-115[»]
2QAMX-ray3.21P2-115[»]
2QAOX-ray3.21P2-115[»]
2QBAX-ray3.54P2-115[»]
2QBCX-ray3.54P2-115[»]
2QBEX-ray3.30P2-115[»]
2QBGX-ray3.30P2-115[»]
2QBIX-ray4.00P2-115[»]
2QBKX-ray4.00P2-115[»]
2QOVX-ray3.93P2-115[»]
2QOXX-ray3.93P2-115[»]
2QOZX-ray3.50P2-115[»]
2QP1X-ray3.50P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
2VHMX-ray3.74P2-115[»]
2VHNX-ray3.74P2-115[»]
2WWQelectron microscopy5.80P2-115[»]
2Z4LX-ray4.45P2-115[»]
2Z4NX-ray4.45P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3DF2X-ray3.50P2-114[»]
3DF4X-ray3.50P2-114[»]
3E1Belectron microscopy-I1-115[»]
3E1Delectron microscopy-I1-115[»]
3FIKelectron microscopy6.70P2-115[»]
3I1NX-ray3.19P1-115[»]
3I1PX-ray3.19P1-115[»]
3I1RX-ray3.81P1-115[»]
3I1TX-ray3.81P1-115[»]
3I20X-ray3.71P1-115[»]
3I22X-ray3.71P1-115[»]
3IZTelectron microscopy-Q1-115[»]
3IZUelectron microscopy-Q1-115[»]
3J01electron microscopy-P2-115[»]
3J0Telectron microscopy12.10R2-115[»]
3J0Welectron microscopy14.70R2-115[»]
3J0Yelectron microscopy13.50R2-115[»]
3J11electron microscopy13.10R2-115[»]
3J12electron microscopy11.50R2-115[»]
3J14electron microscopy11.50R2-115[»]
3J19electron microscopy8.30P2-115[»]
3J37electron microscopy9.80T2-115[»]
3J4Xelectron microscopy12.00P1-115[»]
3J50electron microscopy20.00P1-115[»]
3J51electron microscopy17.00P1-115[»]
3J52electron microscopy12.00P1-115[»]
3J54electron microscopy13.00P1-115[»]
3J56electron microscopy15.00P1-115[»]
3J58electron microscopy17.00P1-115[»]
3J5Aelectron microscopy12.00P1-115[»]
3J5Celectron microscopy17.00P1-115[»]
3J5Eelectron microscopy17.00P1-115[»]
3J5Gelectron microscopy20.00P1-115[»]
3J5Ielectron microscopy15.00P1-115[»]
3J5Kelectron microscopy9.00P1-115[»]
3J5Lelectron microscopy6.60P2-115[»]
3J5Oelectron microscopy6.80P1-115[»]
3J5Uelectron microscopy7.60R2-115[»]
3J5Welectron microscopy7.60S2-115[»]
3KCRelectron microscopy-P1-115[»]
3OASX-ray3.25P2-115[»]
3OATX-ray3.25P2-115[»]
3OFCX-ray3.19P2-115[»]
3OFDX-ray3.19P2-115[»]
3OFQX-ray3.10P2-115[»]
3OFRX-ray3.10P2-115[»]
3OFZX-ray3.29P2-115[»]
3OG0X-ray3.29P2-115[»]
3ORBX-ray3.30P1-115[»]
3R8SX-ray3.00P2-115[»]
3R8TX-ray3.00P2-115[»]
3SGFX-ray3.20T1-115[»]
3UOSX-ray3.70T1-115[»]
4CSUelectron microscopy5.50P2-115[»]
4GARX-ray3.30P1-115[»]
4GAUX-ray3.30P1-115[»]
4KIXX-ray2.90P1-115[»]
4KIZX-ray2.90P1-115[»]
4KJ1X-ray2.90P1-115[»]
4KJ3X-ray2.90P1-115[»]
4KJ5X-ray2.90P1-115[»]
4KJ7X-ray2.90P1-115[»]
4KJ9X-ray2.90P1-115[»]
4KJBX-ray2.90P1-115[»]
4PEBX-ray2.95P2-115[»]
4PECX-ray2.95P2-115[»]
4TOMX-ray3.00P2-115[»]
4TOOX-ray3.00P2-115[»]
4TOVX-ray2.90P2-115[»]
4TOXX-ray2.90P2-115[»]
4TP1X-ray2.90P2-115[»]
4TP3X-ray2.90P2-115[»]
4TP5X-ray2.90P2-115[»]
4TP7X-ray2.90P2-115[»]
4TP9X-ray2.80P2-115[»]
4TPBX-ray2.80P2-115[»]
4TPDX-ray2.80P2-115[»]
4TPFX-ray2.80P2-115[»]
ProteinModelPortaliP0A7K6.
SMRiP0A7K6. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7K6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19P family.Curated

Phylogenomic databases

eggNOGiCOG0335.
HOGENOMiHOG000016264.
InParanoidiP0A7K6.
KOiK02884.
OMAiGGRERIQ.
OrthoDBiEOG6DZF5W.
PhylomeDBiP0A7K6.

Family and domain databases

HAMAPiMF_00402. Ribosomal_L19.
InterProiIPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR15680. PTHR15680. 1 hit.
PfamiPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PIRSFiPIRSF002191. Ribosomal_L19. 1 hit.
PRINTSiPR00061. RIBOSOMALL19.
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01024. rplS_bact. 1 hit.
PROSITEiPS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7K6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI
60 70 80 90 100
RNRGLHSAFT VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL
110
RERTGKAARI KERLN
Length:115
Mass (Da):13,133
Last modified:January 23, 2007 - v2
Checksum:i7BD9F2EFB9DDB06B
GO

Mass spectrometryi

Molecular mass is 13001.7 Da from positions 2 - 115. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01818 Genomic DNA. Translation: CAA25960.1.
U00096 Genomic DNA. Translation: AAC75655.1.
AP009048 Genomic DNA. Translation: BAA16491.1.
PIRiS07951. R5EC19.
RefSeqiNP_417097.1. NC_000913.3.
YP_490829.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneIDi12931612.
947096.
KEGGiecj:Y75_p2554.
eco:b2606.
PATRICi32120611. VBIEscCol129921_2704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01818 Genomic DNA. Translation: CAA25960.1 .
U00096 Genomic DNA. Translation: AAC75655.1 .
AP009048 Genomic DNA. Translation: BAA16491.1 .
PIRi S07951. R5EC19.
RefSeqi NP_417097.1. NC_000913.3.
YP_490829.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P85 electron microscopy 12.30 N 2-115 [» ]
1P86 electron microscopy 11.50 N 2-115 [» ]
1VS6 X-ray 3.46 P 1-115 [» ]
1VS8 X-ray 3.46 P 1-115 [» ]
1VT2 X-ray 3.30 P 1-115 [» ]
2AW4 X-ray 3.46 P 2-115 [» ]
2AWB X-ray 3.46 P 2-115 [» ]
2GYA electron microscopy 15.00 N 2-115 [» ]
2GYC electron microscopy 15.00 N 2-115 [» ]
2I2T X-ray 3.22 P 2-115 [» ]
2I2V X-ray 3.22 P 2-115 [» ]
2J28 electron microscopy 8.00 P 2-115 [» ]
2QAM X-ray 3.21 P 2-115 [» ]
2QAO X-ray 3.21 P 2-115 [» ]
2QBA X-ray 3.54 P 2-115 [» ]
2QBC X-ray 3.54 P 2-115 [» ]
2QBE X-ray 3.30 P 2-115 [» ]
2QBG X-ray 3.30 P 2-115 [» ]
2QBI X-ray 4.00 P 2-115 [» ]
2QBK X-ray 4.00 P 2-115 [» ]
2QOV X-ray 3.93 P 2-115 [» ]
2QOX X-ray 3.93 P 2-115 [» ]
2QOZ X-ray 3.50 P 2-115 [» ]
2QP1 X-ray 3.50 P 2-115 [» ]
2RDO electron microscopy 9.10 P 2-115 [» ]
2VHM X-ray 3.74 P 2-115 [» ]
2VHN X-ray 3.74 P 2-115 [» ]
2WWQ electron microscopy 5.80 P 2-115 [» ]
2Z4L X-ray 4.45 P 2-115 [» ]
2Z4N X-ray 4.45 P 2-115 [» ]
3BBX electron microscopy 10.00 P 2-115 [» ]
3DF2 X-ray 3.50 P 2-114 [» ]
3DF4 X-ray 3.50 P 2-114 [» ]
3E1B electron microscopy - I 1-115 [» ]
3E1D electron microscopy - I 1-115 [» ]
3FIK electron microscopy 6.70 P 2-115 [» ]
3I1N X-ray 3.19 P 1-115 [» ]
3I1P X-ray 3.19 P 1-115 [» ]
3I1R X-ray 3.81 P 1-115 [» ]
3I1T X-ray 3.81 P 1-115 [» ]
3I20 X-ray 3.71 P 1-115 [» ]
3I22 X-ray 3.71 P 1-115 [» ]
3IZT electron microscopy - Q 1-115 [» ]
3IZU electron microscopy - Q 1-115 [» ]
3J01 electron microscopy - P 2-115 [» ]
3J0T electron microscopy 12.10 R 2-115 [» ]
3J0W electron microscopy 14.70 R 2-115 [» ]
3J0Y electron microscopy 13.50 R 2-115 [» ]
3J11 electron microscopy 13.10 R 2-115 [» ]
3J12 electron microscopy 11.50 R 2-115 [» ]
3J14 electron microscopy 11.50 R 2-115 [» ]
3J19 electron microscopy 8.30 P 2-115 [» ]
3J37 electron microscopy 9.80 T 2-115 [» ]
3J4X electron microscopy 12.00 P 1-115 [» ]
3J50 electron microscopy 20.00 P 1-115 [» ]
3J51 electron microscopy 17.00 P 1-115 [» ]
3J52 electron microscopy 12.00 P 1-115 [» ]
3J54 electron microscopy 13.00 P 1-115 [» ]
3J56 electron microscopy 15.00 P 1-115 [» ]
3J58 electron microscopy 17.00 P 1-115 [» ]
3J5A electron microscopy 12.00 P 1-115 [» ]
3J5C electron microscopy 17.00 P 1-115 [» ]
3J5E electron microscopy 17.00 P 1-115 [» ]
3J5G electron microscopy 20.00 P 1-115 [» ]
3J5I electron microscopy 15.00 P 1-115 [» ]
3J5K electron microscopy 9.00 P 1-115 [» ]
3J5L electron microscopy 6.60 P 2-115 [» ]
3J5O electron microscopy 6.80 P 1-115 [» ]
3J5U electron microscopy 7.60 R 2-115 [» ]
3J5W electron microscopy 7.60 S 2-115 [» ]
3KCR electron microscopy - P 1-115 [» ]
3OAS X-ray 3.25 P 2-115 [» ]
3OAT X-ray 3.25 P 2-115 [» ]
3OFC X-ray 3.19 P 2-115 [» ]
3OFD X-ray 3.19 P 2-115 [» ]
3OFQ X-ray 3.10 P 2-115 [» ]
3OFR X-ray 3.10 P 2-115 [» ]
3OFZ X-ray 3.29 P 2-115 [» ]
3OG0 X-ray 3.29 P 2-115 [» ]
3ORB X-ray 3.30 P 1-115 [» ]
3R8S X-ray 3.00 P 2-115 [» ]
3R8T X-ray 3.00 P 2-115 [» ]
3SGF X-ray 3.20 T 1-115 [» ]
3UOS X-ray 3.70 T 1-115 [» ]
4CSU electron microscopy 5.50 P 2-115 [» ]
4GAR X-ray 3.30 P 1-115 [» ]
4GAU X-ray 3.30 P 1-115 [» ]
4KIX X-ray 2.90 P 1-115 [» ]
4KIZ X-ray 2.90 P 1-115 [» ]
4KJ1 X-ray 2.90 P 1-115 [» ]
4KJ3 X-ray 2.90 P 1-115 [» ]
4KJ5 X-ray 2.90 P 1-115 [» ]
4KJ7 X-ray 2.90 P 1-115 [» ]
4KJ9 X-ray 2.90 P 1-115 [» ]
4KJB X-ray 2.90 P 1-115 [» ]
4PEB X-ray 2.95 P 2-115 [» ]
4PEC X-ray 2.95 P 2-115 [» ]
4TOM X-ray 3.00 P 2-115 [» ]
4TOO X-ray 3.00 P 2-115 [» ]
4TOV X-ray 2.90 P 2-115 [» ]
4TOX X-ray 2.90 P 2-115 [» ]
4TP1 X-ray 2.90 P 2-115 [» ]
4TP3 X-ray 2.90 P 2-115 [» ]
4TP5 X-ray 2.90 P 2-115 [» ]
4TP7 X-ray 2.90 P 2-115 [» ]
4TP9 X-ray 2.80 P 2-115 [» ]
4TPB X-ray 2.80 P 2-115 [» ]
4TPD X-ray 2.80 P 2-115 [» ]
4TPF X-ray 2.80 P 2-115 [» ]
ProteinModelPortali P0A7K6.
SMRi P0A7K6. Positions 2-115.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35793N.
IntActi P0A7K6. 101 interactions.
MINTi MINT-1245288.
STRINGi 511145.b2606.

Chemistry

ChEMBLi CHEMBL2363135.

PTM databases

PhosSitei P0810432.

Proteomic databases

PaxDbi P0A7K6.
PRIDEi P0A7K6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75655 ; AAC75655 ; b2606 .
BAA16491 ; BAA16491 ; BAA16491 .
GeneIDi 12931612.
947096.
KEGGi ecj:Y75_p2554.
eco:b2606.
PATRICi 32120611. VBIEscCol129921_2704.

Organism-specific databases

EchoBASEi EB0873.
EcoGenei EG10880. rplS.

Phylogenomic databases

eggNOGi COG0335.
HOGENOMi HOG000016264.
InParanoidi P0A7K6.
KOi K02884.
OMAi GGRERIQ.
OrthoDBi EOG6DZF5W.
PhylomeDBi P0A7K6.

Enzyme and pathway databases

BioCyci EcoCyc:EG10880-MONOMER.
ECOL316407:JW2587-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7K6.
PROi P0A7K6.

Gene expression databases

Genevestigatori P0A7K6.

Family and domain databases

HAMAPi MF_00402. Ribosomal_L19.
InterProi IPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
PANTHERi PTHR15680. PTHR15680. 1 hit.
Pfami PF01245. Ribosomal_L19. 1 hit.
[Graphical view ]
PIRSFi PIRSF002191. Ribosomal_L19. 1 hit.
PRINTSi PR00061. RIBOSOMALL19.
SUPFAMi SSF50104. SSF50104. 1 hit.
TIGRFAMsi TIGR01024. rplS_bact. 1 hit.
PROSITEi PS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes."
    Brosius J., Arfsten U.
    Biochemistry 17:508-516(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-115.
  6. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
    Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
    Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L14.
  7. "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.
  8. "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.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL19_ECOLI
AccessioniPrimary (citable) accession number: P0A7K6
Secondary accession number(s): P02420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 98 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

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