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P0A7R1

- RL9_ECOLI

UniProt

P0A7R1 - RL9_ECOLI

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Protein

50S ribosomal protein L9

Gene

rplI

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

Functioni

One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  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:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L9
Gene namesi
Name:rplI
Ordered Locus Names:b4203, JW4161
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10870. rplI.

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
Chaini1 – 14914950S ribosomal protein L9PRO_0000176636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711N6-succinyllysine1 Publication
Modified residuei83 – 831N6-succinyllysine1 Publication
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei112 – 1121N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7R1.
PRIDEiP0A7R1.

2D gel databases

SWISS-2DPAGEP0A7R1.

Expressioni

Gene expression databases

GenevestigatoriP0A7R1.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

DIPiDIP-35748N.
IntActiP0A7R1. 59 interactions.
MINTiMINT-1228834.
STRINGi511145.b4203.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74
Helixi10 – 123
Beta strandi14 – 163
Helixi23 – 286
Helixi31 – 333
Beta strandi35 – 373
Turni40 – 423
Turni43 – 464
Helixi48 – 514
Turni52 – 554
Helixi56 – 594
Turni60 – 645
Helixi65 – 684
Beta strandi71 – 744
Beta strandi78 – 825
Beta strandi88 – 947
Helixi96 – 1049
Beta strandi106 – 1083
Beta strandi114 – 1163
Beta strandi118 – 1214
Beta strandi122 – 13211
Beta strandi134 – 1374
Beta strandi142 – 1487

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30F1-149[»]
1P86electron microscopy11.50F1-149[»]
1VS6X-ray3.46H1-149[»]
1VS8X-ray3.46H1-149[»]
1VT2X-ray3.30H1-149[»]
2AW4X-ray3.46H1-149[»]
2AWBX-ray3.46H1-149[»]
2GYAelectron microscopy15.00F1-149[»]
2GYCelectron microscopy15.00F1-149[»]
2I2TX-ray3.22H1-149[»]
2I2VX-ray3.22H1-149[»]
2J28electron microscopy8.00H1-149[»]
2QAMX-ray3.21H1-149[»]
2QAOX-ray3.21H1-149[»]
2QBAX-ray3.54H1-149[»]
2QBCX-ray3.54H1-149[»]
2QBEX-ray3.30H1-149[»]
2QBGX-ray3.30H1-149[»]
2QBIX-ray4.00H1-149[»]
2QBKX-ray4.00H1-149[»]
2QOVX-ray3.93H1-149[»]
2QOXX-ray3.93H1-149[»]
2QOZX-ray3.50H1-149[»]
2QP1X-ray3.50H1-149[»]
2RDOelectron microscopy9.10H1-149[»]
2VHMX-ray3.74H1-149[»]
2VHNX-ray3.74H1-149[»]
2WWQelectron microscopy5.80H1-149[»]
2Z4LX-ray4.45H1-149[»]
2Z4NX-ray4.45H1-149[»]
3BBXelectron microscopy10.00H1-149[»]
3DF2X-ray3.50H1-149[»]
3DF4X-ray3.50H1-149[»]
3E1Belectron microscopy-41-149[»]
3E1Delectron microscopy-41-149[»]
3FIKelectron microscopy6.70H1-149[»]
3I1NX-ray3.19H1-149[»]
3I1PX-ray3.19H1-149[»]
3I1RX-ray3.81H1-149[»]
3I1TX-ray3.81H1-149[»]
3I20X-ray3.71H1-149[»]
3I22X-ray3.71H1-149[»]
3IZTelectron microscopy-I1-149[»]
3IZUelectron microscopy-I1-149[»]
3J01electron microscopy-H1-149[»]
3J0Telectron microscopy12.10I1-149[»]
3J0Welectron microscopy14.70I1-149[»]
3J0Yelectron microscopy13.50I1-149[»]
3J11electron microscopy13.10I1-149[»]
3J12electron microscopy11.50I1-149[»]
3J14electron microscopy11.50I1-149[»]
3J19electron microscopy8.30H1-149[»]
3J37electron microscopy9.80L1-149[»]
3J4Xelectron microscopy12.00H1-149[»]
3J50electron microscopy20.00H1-149[»]
3J51electron microscopy17.00H1-149[»]
3J52electron microscopy12.00H1-149[»]
3J54electron microscopy13.00H1-149[»]
3J56electron microscopy15.00H1-149[»]
3J58electron microscopy17.00H1-149[»]
3J5Aelectron microscopy12.00H1-149[»]
3J5Celectron microscopy17.00H1-149[»]
3J5Eelectron microscopy17.00H1-149[»]
3J5Gelectron microscopy20.00H1-149[»]
3J5Ielectron microscopy15.00H1-149[»]
3J5Kelectron microscopy9.00H1-149[»]
3J5Lelectron microscopy6.60H1-56[»]
3J5Oelectron microscopy6.80H1-50[»]
3J5Uelectron microscopy7.60I1-149[»]
3J5Welectron microscopy7.60I1-149[»]
3KCRelectron microscopy-H1-149[»]
3OASX-ray3.25H1-149[»]
3OATX-ray3.25H1-149[»]
3OFCX-ray3.19H1-149[»]
3OFDX-ray3.19H1-149[»]
3OFQX-ray3.10H1-149[»]
3OFRX-ray3.10H1-149[»]
3OFZX-ray3.29H1-149[»]
3OG0X-ray3.29H1-149[»]
3ORBX-ray3.30H1-149[»]
3R8SX-ray3.00H1-149[»]
3R8TX-ray3.00H1-149[»]
487Delectron microscopy7.50K24-123[»]
4CSUelectron microscopy5.50H1-149[»]
4GARX-ray3.30H1-149[»]
4GAUX-ray3.30H1-149[»]
4KIXX-ray2.90H1-50[»]
4KIZX-ray2.90H1-50[»]
4KJ1X-ray2.90H1-50[»]
4KJ3X-ray2.90H1-50[»]
4KJ5X-ray2.90H1-50[»]
4KJ7X-ray2.90H1-50[»]
4KJ9X-ray2.90H1-50[»]
4KJBX-ray2.90H1-50[»]
4PEBX-ray2.95H1-149[»]
4PECX-ray2.95H1-149[»]
4TOMX-ray3.00H1-149[»]
4TOOX-ray3.00H1-149[»]
4TOVX-ray2.90H1-149[»]
4TOXX-ray2.90H1-149[»]
4TP1X-ray2.90H1-149[»]
4TP3X-ray2.90H1-149[»]
4TP5X-ray2.90H1-149[»]
4TP7X-ray2.90H1-148[»]
4TP9X-ray2.80H1-149[»]
4TPBX-ray2.80H1-149[»]
4TPDX-ray2.80H1-149[»]
4TPFX-ray2.80H1-149[»]
ProteinModelPortaliP0A7R1.
SMRiP0A7R1. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7R1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L9P family.Curated

Phylogenomic databases

eggNOGiCOG0359.
HOGENOMiHOG000040337.
InParanoidiP0A7R1.
KOiK02939.
OMAiAKSEVRM.
OrthoDBiEOG6D8BH0.
PhylomeDBiP0A7R1.

Family and domain databases

Gene3Di3.10.430.100. 1 hit.
3.40.5.10. 1 hit.
HAMAPiMF_00503. Ribosomal_L9.
InterProiIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERiPTHR21368. PTHR21368. 1 hit.
PfamiPF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMiSSF55653. SSF55653. 1 hit.
SSF55658. SSF55658. 1 hit.
TIGRFAMsiTIGR00158. L9. 1 hit.
PROSITEiPS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7R1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQVILLDKVA NLGSLGDQVN VKAGYARNFL VPQGKAVPAT KKNIEFFEAR
60 70 80 90 100
RAELEAKLAE VLAAANARAE KINALETVTI ASKAGDEGKL FGSIGTRDIA
110 120 130 140
DAVTAAGVEV AKSEVRLPNG VLRTTGEHEV SFQVHSEVFA KVIVNVVAE
Length:149
Mass (Da):15,769
Last modified:April 1, 1988 - v1
Checksum:iF8FF527DBB9458CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061A → AD AA sequence 1 PublicationCurated
Sequence conflicti125 – 1284TGEH → HGE AA sequence 1 PublicationCurated
Sequence conflicti136 – 1361Missing AA sequence 1 PublicationCurated

Mass spectrometryi

Molecular mass is 15769.7 Da from positions 1 - 149. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04022 Genomic DNA. Translation: CAA27655.1.
U14003 Genomic DNA. Translation: AAA97099.1.
U00096 Genomic DNA. Translation: AAC77160.1.
AP009048 Genomic DNA. Translation: BAE78204.1.
PIRiF65231. R5EC9.
RefSeqiNP_418624.1. NC_000913.3.
YP_492345.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77160; AAC77160; b4203.
BAE78204; BAE78204; BAE78204.
GeneIDi12930641.
948720.
KEGGiecj:Y75_p4089.
eco:b4203.
PATRICi32123981. VBIEscCol129921_4335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04022 Genomic DNA. Translation: CAA27655.1 .
U14003 Genomic DNA. Translation: AAA97099.1 .
U00096 Genomic DNA. Translation: AAC77160.1 .
AP009048 Genomic DNA. Translation: BAE78204.1 .
PIRi F65231. R5EC9.
RefSeqi NP_418624.1. NC_000913.3.
YP_492345.1. 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 F 1-149 [» ]
1P86 electron microscopy 11.50 F 1-149 [» ]
1VS6 X-ray 3.46 H 1-149 [» ]
1VS8 X-ray 3.46 H 1-149 [» ]
1VT2 X-ray 3.30 H 1-149 [» ]
2AW4 X-ray 3.46 H 1-149 [» ]
2AWB X-ray 3.46 H 1-149 [» ]
2GYA electron microscopy 15.00 F 1-149 [» ]
2GYC electron microscopy 15.00 F 1-149 [» ]
2I2T X-ray 3.22 H 1-149 [» ]
2I2V X-ray 3.22 H 1-149 [» ]
2J28 electron microscopy 8.00 H 1-149 [» ]
2QAM X-ray 3.21 H 1-149 [» ]
2QAO X-ray 3.21 H 1-149 [» ]
2QBA X-ray 3.54 H 1-149 [» ]
2QBC X-ray 3.54 H 1-149 [» ]
2QBE X-ray 3.30 H 1-149 [» ]
2QBG X-ray 3.30 H 1-149 [» ]
2QBI X-ray 4.00 H 1-149 [» ]
2QBK X-ray 4.00 H 1-149 [» ]
2QOV X-ray 3.93 H 1-149 [» ]
2QOX X-ray 3.93 H 1-149 [» ]
2QOZ X-ray 3.50 H 1-149 [» ]
2QP1 X-ray 3.50 H 1-149 [» ]
2RDO electron microscopy 9.10 H 1-149 [» ]
2VHM X-ray 3.74 H 1-149 [» ]
2VHN X-ray 3.74 H 1-149 [» ]
2WWQ electron microscopy 5.80 H 1-149 [» ]
2Z4L X-ray 4.45 H 1-149 [» ]
2Z4N X-ray 4.45 H 1-149 [» ]
3BBX electron microscopy 10.00 H 1-149 [» ]
3DF2 X-ray 3.50 H 1-149 [» ]
3DF4 X-ray 3.50 H 1-149 [» ]
3E1B electron microscopy - 4 1-149 [» ]
3E1D electron microscopy - 4 1-149 [» ]
3FIK electron microscopy 6.70 H 1-149 [» ]
3I1N X-ray 3.19 H 1-149 [» ]
3I1P X-ray 3.19 H 1-149 [» ]
3I1R X-ray 3.81 H 1-149 [» ]
3I1T X-ray 3.81 H 1-149 [» ]
3I20 X-ray 3.71 H 1-149 [» ]
3I22 X-ray 3.71 H 1-149 [» ]
3IZT electron microscopy - I 1-149 [» ]
3IZU electron microscopy - I 1-149 [» ]
3J01 electron microscopy - H 1-149 [» ]
3J0T electron microscopy 12.10 I 1-149 [» ]
3J0W electron microscopy 14.70 I 1-149 [» ]
3J0Y electron microscopy 13.50 I 1-149 [» ]
3J11 electron microscopy 13.10 I 1-149 [» ]
3J12 electron microscopy 11.50 I 1-149 [» ]
3J14 electron microscopy 11.50 I 1-149 [» ]
3J19 electron microscopy 8.30 H 1-149 [» ]
3J37 electron microscopy 9.80 L 1-149 [» ]
3J4X electron microscopy 12.00 H 1-149 [» ]
3J50 electron microscopy 20.00 H 1-149 [» ]
3J51 electron microscopy 17.00 H 1-149 [» ]
3J52 electron microscopy 12.00 H 1-149 [» ]
3J54 electron microscopy 13.00 H 1-149 [» ]
3J56 electron microscopy 15.00 H 1-149 [» ]
3J58 electron microscopy 17.00 H 1-149 [» ]
3J5A electron microscopy 12.00 H 1-149 [» ]
3J5C electron microscopy 17.00 H 1-149 [» ]
3J5E electron microscopy 17.00 H 1-149 [» ]
3J5G electron microscopy 20.00 H 1-149 [» ]
3J5I electron microscopy 15.00 H 1-149 [» ]
3J5K electron microscopy 9.00 H 1-149 [» ]
3J5L electron microscopy 6.60 H 1-56 [» ]
3J5O electron microscopy 6.80 H 1-50 [» ]
3J5U electron microscopy 7.60 I 1-149 [» ]
3J5W electron microscopy 7.60 I 1-149 [» ]
3KCR electron microscopy - H 1-149 [» ]
3OAS X-ray 3.25 H 1-149 [» ]
3OAT X-ray 3.25 H 1-149 [» ]
3OFC X-ray 3.19 H 1-149 [» ]
3OFD X-ray 3.19 H 1-149 [» ]
3OFQ X-ray 3.10 H 1-149 [» ]
3OFR X-ray 3.10 H 1-149 [» ]
3OFZ X-ray 3.29 H 1-149 [» ]
3OG0 X-ray 3.29 H 1-149 [» ]
3ORB X-ray 3.30 H 1-149 [» ]
3R8S X-ray 3.00 H 1-149 [» ]
3R8T X-ray 3.00 H 1-149 [» ]
487D electron microscopy 7.50 K 24-123 [» ]
4CSU electron microscopy 5.50 H 1-149 [» ]
4GAR X-ray 3.30 H 1-149 [» ]
4GAU X-ray 3.30 H 1-149 [» ]
4KIX X-ray 2.90 H 1-50 [» ]
4KIZ X-ray 2.90 H 1-50 [» ]
4KJ1 X-ray 2.90 H 1-50 [» ]
4KJ3 X-ray 2.90 H 1-50 [» ]
4KJ5 X-ray 2.90 H 1-50 [» ]
4KJ7 X-ray 2.90 H 1-50 [» ]
4KJ9 X-ray 2.90 H 1-50 [» ]
4KJB X-ray 2.90 H 1-50 [» ]
4PEB X-ray 2.95 H 1-149 [» ]
4PEC X-ray 2.95 H 1-149 [» ]
4TOM X-ray 3.00 H 1-149 [» ]
4TOO X-ray 3.00 H 1-149 [» ]
4TOV X-ray 2.90 H 1-149 [» ]
4TOX X-ray 2.90 H 1-149 [» ]
4TP1 X-ray 2.90 H 1-149 [» ]
4TP3 X-ray 2.90 H 1-149 [» ]
4TP5 X-ray 2.90 H 1-149 [» ]
4TP7 X-ray 2.90 H 1-148 [» ]
4TP9 X-ray 2.80 H 1-149 [» ]
4TPB X-ray 2.80 H 1-149 [» ]
4TPD X-ray 2.80 H 1-149 [» ]
4TPF X-ray 2.80 H 1-149 [» ]
ProteinModelPortali P0A7R1.
SMRi P0A7R1. Positions 1-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35748N.
IntActi P0A7R1. 59 interactions.
MINTi MINT-1228834.
STRINGi 511145.b4203.

2D gel databases

SWISS-2DPAGE P0A7R1.

Proteomic databases

PaxDbi P0A7R1.
PRIDEi P0A7R1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77160 ; AAC77160 ; b4203 .
BAE78204 ; BAE78204 ; BAE78204 .
GeneIDi 12930641.
948720.
KEGGi ecj:Y75_p4089.
eco:b4203.
PATRICi 32123981. VBIEscCol129921_4335.

Organism-specific databases

EchoBASEi EB0863.
EcoGenei EG10870. rplI.

Phylogenomic databases

eggNOGi COG0359.
HOGENOMi HOG000040337.
InParanoidi P0A7R1.
KOi K02939.
OMAi AKSEVRM.
OrthoDBi EOG6D8BH0.
PhylomeDBi P0A7R1.

Enzyme and pathway databases

BioCyci EcoCyc:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7R1.
PROi P0A7R1.

Gene expression databases

Genevestigatori P0A7R1.

Family and domain databases

Gene3Di 3.10.430.100. 1 hit.
3.40.5.10. 1 hit.
HAMAPi MF_00503. Ribosomal_L9.
InterProi IPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view ]
PANTHERi PTHR21368. PTHR21368. 1 hit.
Pfami PF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view ]
SUPFAMi SSF55653. SSF55653. 1 hit.
SSF55658. SSF55658. 1 hit.
TIGRFAMsi TIGR00158. L9. 1 hit.
PROSITEi PS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L9 from the Escherichia coli ribosome."
    Kamp R.M., Wittmann-Liebold B.
    FEBS Lett. 149:313-319(1982)
    Cited for: PROTEIN SEQUENCE.
  2. "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
    Schnier J., Kitakawa M., Isono K.
    Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: PROTEIN SEQUENCE OF 1-13.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. Cited for: PROTEIN SEQUENCE OF 1-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  10. "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.
  11. "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.
  12. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  13. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-71; LYS-83 AND LYS-112.
    Strain: K12.
  14. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
    Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
    J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  15. "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.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL9_ECOLI
AccessioniPrimary (citable) accession number: P0A7R1
Secondary accession number(s): P02418, Q2M6A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: October 29, 2014
This is version 99 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