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P0ADZ0

- RL23_ECOLI

UniProt

P0ADZ0 - RL23_ECOLI

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Protein

50S ribosomal protein L23

Gene

rplW

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

Functioni

One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).2 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. rRNA binding Source: UniProtKB-HAMAP
  3. 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:EG10883-MONOMER.
ECOL316407:JW3280-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L23UniRule annotation
Gene namesi
Name:rplWUniRule annotation
Ordered Locus Names:b3318, JW3280
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10883. rplW.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 183VSE → AAA: Strongly reduces trigger factor binding. 1 Publication
Mutagenesisi18 – 181E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. 1 Publication
Mutagenesisi18 – 181E → Q: Strongly reduces trigger factor binding. 1 Publication
Mutagenesisi51 – 533FEV → AAA: No effect on trigger factor binding. 1 Publication
Mutagenesisi52 – 521E → K: No effect on trigger factor binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10010050S ribosomal protein L23PRO_0000129407Add
BLAST

Proteomic databases

PaxDbiP0ADZ0.
PRIDEiP0ADZ0.

Expressioni

Gene expression databases

GenevestigatoriP0ADZ0.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Might also contact SecE and probably does contact SecG and SecY when the SecYEG translocation complex is docked with the ribosome.

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsEP0A7W12EBI-542264,EBI-543949

Protein-protein interaction databases

DIPiDIP-35972N.
IntActiP0ADZ0. 73 interactions.
MINTiMINT-1225825.
STRINGi511145.b3318.

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Beta strandi11 – 144Combined sources
Helixi18 – 258Combined sources
Beta strandi26 – 283Combined sources
Beta strandi29 – 346Combined sources
Turni35 – 373Combined sources
Helixi40 – 5011Combined sources
Beta strandi55 – 639Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 733Combined sources
Beta strandi74 – 763Combined sources
Beta strandi80 – 878Combined sources
Beta strandi88 – 903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00t2-85[»]
1P85electron microscopy12.30R1-100[»]
1P86electron microscopy11.50R1-100[»]
1VS6X-ray3.46T1-100[»]
1VS8X-ray3.46T1-100[»]
1VT2X-ray3.30T1-100[»]
2AW4X-ray3.46T1-100[»]
2AWBX-ray3.46T1-100[»]
2GYAelectron microscopy15.00R7-98[»]
2GYCelectron microscopy15.00R7-98[»]
2I2TX-ray3.22T1-100[»]
2I2VX-ray3.22T1-100[»]
2J28electron microscopy8.00T1-99[»]
2QAMX-ray3.21T1-100[»]
2QAOX-ray3.21T1-100[»]
2QBAX-ray3.54T1-100[»]
2QBCX-ray3.54T1-100[»]
2QBEX-ray3.30T1-100[»]
2QBGX-ray3.30T1-100[»]
2QBIX-ray4.00T1-100[»]
2QBKX-ray4.00T1-100[»]
2QOVX-ray3.93T1-100[»]
2QOXX-ray3.93T1-100[»]
2QOZX-ray3.50T1-100[»]
2QP1X-ray3.50T1-100[»]
2RDOelectron microscopy9.10T1-100[»]
2VRHelectron microscopy19.00B1-100[»]
2WWQelectron microscopy5.80T1-93[»]
2Z4LX-ray4.45T1-100[»]
2Z4NX-ray4.45T1-100[»]
3BBXelectron microscopy10.00T1-100[»]
3E1Belectron microscopy-M1-99[»]
3E1Delectron microscopy-M1-99[»]
3FIKelectron microscopy6.70T1-93[»]
3I1NX-ray3.19T1-100[»]
3I1PX-ray3.19T1-100[»]
3I1RX-ray3.81T1-100[»]
3I1TX-ray3.81T1-100[»]
3I20X-ray3.71T1-100[»]
3I22X-ray3.71T1-100[»]
3IY9electron microscopy14.10T1-99[»]
3IZTelectron microscopy-U1-100[»]
3IZUelectron microscopy-U1-100[»]
3J01electron microscopy-T1-100[»]
3J0Telectron microscopy12.10V1-100[»]
3J0Welectron microscopy14.70V1-100[»]
3J0Yelectron microscopy13.50V1-100[»]
3J11electron microscopy13.10V1-100[»]
3J12electron microscopy11.50V1-100[»]
3J14electron microscopy11.50V1-100[»]
3J19electron microscopy8.30T1-93[»]
3J37electron microscopy9.80X1-100[»]
3J45electron microscopy9.50T1-100[»]
3J46electron microscopy10.10T1-100[»]
3J4Xelectron microscopy12.00T1-93[»]
3J50electron microscopy20.00T1-93[»]
3J51electron microscopy17.00T1-93[»]
3J52electron microscopy12.00T1-93[»]
3J54electron microscopy13.00T1-93[»]
3J56electron microscopy15.00T1-93[»]
3J58electron microscopy17.00T1-93[»]
3J5Aelectron microscopy12.00T1-93[»]
3J5Celectron microscopy17.00T1-93[»]
3J5Eelectron microscopy17.00T1-93[»]
3J5Gelectron microscopy20.00T1-93[»]
3J5Ielectron microscopy15.00T1-93[»]
3J5Kelectron microscopy9.00T1-93[»]
3J5Lelectron microscopy6.60T1-93[»]
3J5Oelectron microscopy6.80T1-100[»]
3J5Uelectron microscopy7.60V1-100[»]
3J5Welectron microscopy7.60W1-100[»]
3KCRelectron microscopy-T1-100[»]
3OASX-ray3.25T1-93[»]
3OATX-ray3.25T1-93[»]
3OFCX-ray3.19T1-93[»]
3OFDX-ray3.19T1-93[»]
3OFQX-ray3.10T1-93[»]
3OFRX-ray3.10T1-93[»]
3OFZX-ray3.29T1-93[»]
3OG0X-ray3.29T1-93[»]
3ORBX-ray3.30T1-100[»]
3R8SX-ray3.00T1-93[»]
3R8TX-ray3.00T1-93[»]
3SGFX-ray3.20X1-100[»]
3UOSX-ray3.70X1-100[»]
4CSUelectron microscopy5.50T1-100[»]
4GARX-ray3.30T1-100[»]
4GAUX-ray3.30T1-100[»]
4KIXX-ray2.90T1-100[»]
4KIZX-ray2.90T1-100[»]
4KJ1X-ray2.90T1-100[»]
4KJ3X-ray2.90T1-100[»]
4KJ5X-ray2.90T1-100[»]
4KJ7X-ray2.90T1-100[»]
4KJ9X-ray2.90T1-100[»]
4KJBX-ray2.90T1-100[»]
4PEBX-ray2.95T1-93[»]
4PECX-ray2.95T1-93[»]
4TOMX-ray3.00T1-93[»]
4TOOX-ray3.00T1-93[»]
4TOVX-ray2.90T1-93[»]
4TOXX-ray2.90T1-93[»]
4TP1X-ray2.90T1-93[»]
4TP3X-ray2.90T1-93[»]
4TP5X-ray2.90T1-93[»]
4TP7X-ray2.90T1-93[»]
4TP9X-ray2.80T1-93[»]
4TPBX-ray2.80T1-93[»]
4TPDX-ray2.80T1-93[»]
4TPFX-ray2.80T1-93[»]
ProteinModelPortaliP0ADZ0.
SMRiP0ADZ0. Positions 7-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADZ0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L23P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0089.
HOGENOMiHOG000231364.
InParanoidiP0ADZ0.
KOiK02892.
OMAiFGRRSDW.
OrthoDBiEOG6HTP4P.
PhylomeDBiP0ADZ0.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_01369_B. Ribosomal_L23_B.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
PfamiPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ADZ0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL
60 70 80 90 100
FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE
Length:100
Mass (Da):11,199
Last modified:December 6, 2005 - v1
Checksum:i30CD1D77CC7CF9EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801Missing AA sequence (PubMed:391594)Curated

Mass spectrometryi

Molecular mass is 11198.0 Da from positions 1 - 100. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26462.1.
U18997 Genomic DNA. Translation: AAA58115.1.
U00096 Genomic DNA. Translation: AAC76343.1.
AP009048 Genomic DNA. Translation: BAE77973.1.
PIRiA65125. R5EC23.
RefSeqiNP_417777.1. NC_000913.3.
YP_492114.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76343; AAC76343; b3318.
BAE77973; BAE77973; BAE77973.
GeneIDi12932296.
947819.
KEGGiecj:Y75_p3858.
eco:b3318.
PATRICi32122068. VBIEscCol129921_3411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26462.1 .
U18997 Genomic DNA. Translation: AAA58115.1 .
U00096 Genomic DNA. Translation: AAC76343.1 .
AP009048 Genomic DNA. Translation: BAE77973.1 .
PIRi A65125. R5EC23.
RefSeqi NP_417777.1. NC_000913.3.
YP_492114.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 t 2-85 [» ]
1P85 electron microscopy 12.30 R 1-100 [» ]
1P86 electron microscopy 11.50 R 1-100 [» ]
1VS6 X-ray 3.46 T 1-100 [» ]
1VS8 X-ray 3.46 T 1-100 [» ]
1VT2 X-ray 3.30 T 1-100 [» ]
2AW4 X-ray 3.46 T 1-100 [» ]
2AWB X-ray 3.46 T 1-100 [» ]
2GYA electron microscopy 15.00 R 7-98 [» ]
2GYC electron microscopy 15.00 R 7-98 [» ]
2I2T X-ray 3.22 T 1-100 [» ]
2I2V X-ray 3.22 T 1-100 [» ]
2J28 electron microscopy 8.00 T 1-99 [» ]
2QAM X-ray 3.21 T 1-100 [» ]
2QAO X-ray 3.21 T 1-100 [» ]
2QBA X-ray 3.54 T 1-100 [» ]
2QBC X-ray 3.54 T 1-100 [» ]
2QBE X-ray 3.30 T 1-100 [» ]
2QBG X-ray 3.30 T 1-100 [» ]
2QBI X-ray 4.00 T 1-100 [» ]
2QBK X-ray 4.00 T 1-100 [» ]
2QOV X-ray 3.93 T 1-100 [» ]
2QOX X-ray 3.93 T 1-100 [» ]
2QOZ X-ray 3.50 T 1-100 [» ]
2QP1 X-ray 3.50 T 1-100 [» ]
2RDO electron microscopy 9.10 T 1-100 [» ]
2VRH electron microscopy 19.00 B 1-100 [» ]
2WWQ electron microscopy 5.80 T 1-93 [» ]
2Z4L X-ray 4.45 T 1-100 [» ]
2Z4N X-ray 4.45 T 1-100 [» ]
3BBX electron microscopy 10.00 T 1-100 [» ]
3E1B electron microscopy - M 1-99 [» ]
3E1D electron microscopy - M 1-99 [» ]
3FIK electron microscopy 6.70 T 1-93 [» ]
3I1N X-ray 3.19 T 1-100 [» ]
3I1P X-ray 3.19 T 1-100 [» ]
3I1R X-ray 3.81 T 1-100 [» ]
3I1T X-ray 3.81 T 1-100 [» ]
3I20 X-ray 3.71 T 1-100 [» ]
3I22 X-ray 3.71 T 1-100 [» ]
3IY9 electron microscopy 14.10 T 1-99 [» ]
3IZT electron microscopy - U 1-100 [» ]
3IZU electron microscopy - U 1-100 [» ]
3J01 electron microscopy - T 1-100 [» ]
3J0T electron microscopy 12.10 V 1-100 [» ]
3J0W electron microscopy 14.70 V 1-100 [» ]
3J0Y electron microscopy 13.50 V 1-100 [» ]
3J11 electron microscopy 13.10 V 1-100 [» ]
3J12 electron microscopy 11.50 V 1-100 [» ]
3J14 electron microscopy 11.50 V 1-100 [» ]
3J19 electron microscopy 8.30 T 1-93 [» ]
3J37 electron microscopy 9.80 X 1-100 [» ]
3J45 electron microscopy 9.50 T 1-100 [» ]
3J46 electron microscopy 10.10 T 1-100 [» ]
3J4X electron microscopy 12.00 T 1-93 [» ]
3J50 electron microscopy 20.00 T 1-93 [» ]
3J51 electron microscopy 17.00 T 1-93 [» ]
3J52 electron microscopy 12.00 T 1-93 [» ]
3J54 electron microscopy 13.00 T 1-93 [» ]
3J56 electron microscopy 15.00 T 1-93 [» ]
3J58 electron microscopy 17.00 T 1-93 [» ]
3J5A electron microscopy 12.00 T 1-93 [» ]
3J5C electron microscopy 17.00 T 1-93 [» ]
3J5E electron microscopy 17.00 T 1-93 [» ]
3J5G electron microscopy 20.00 T 1-93 [» ]
3J5I electron microscopy 15.00 T 1-93 [» ]
3J5K electron microscopy 9.00 T 1-93 [» ]
3J5L electron microscopy 6.60 T 1-93 [» ]
3J5O electron microscopy 6.80 T 1-100 [» ]
3J5U electron microscopy 7.60 V 1-100 [» ]
3J5W electron microscopy 7.60 W 1-100 [» ]
3KCR electron microscopy - T 1-100 [» ]
3OAS X-ray 3.25 T 1-93 [» ]
3OAT X-ray 3.25 T 1-93 [» ]
3OFC X-ray 3.19 T 1-93 [» ]
3OFD X-ray 3.19 T 1-93 [» ]
3OFQ X-ray 3.10 T 1-93 [» ]
3OFR X-ray 3.10 T 1-93 [» ]
3OFZ X-ray 3.29 T 1-93 [» ]
3OG0 X-ray 3.29 T 1-93 [» ]
3ORB X-ray 3.30 T 1-100 [» ]
3R8S X-ray 3.00 T 1-93 [» ]
3R8T X-ray 3.00 T 1-93 [» ]
3SGF X-ray 3.20 X 1-100 [» ]
3UOS X-ray 3.70 X 1-100 [» ]
4CSU electron microscopy 5.50 T 1-100 [» ]
4GAR X-ray 3.30 T 1-100 [» ]
4GAU X-ray 3.30 T 1-100 [» ]
4KIX X-ray 2.90 T 1-100 [» ]
4KIZ X-ray 2.90 T 1-100 [» ]
4KJ1 X-ray 2.90 T 1-100 [» ]
4KJ3 X-ray 2.90 T 1-100 [» ]
4KJ5 X-ray 2.90 T 1-100 [» ]
4KJ7 X-ray 2.90 T 1-100 [» ]
4KJ9 X-ray 2.90 T 1-100 [» ]
4KJB X-ray 2.90 T 1-100 [» ]
4PEB X-ray 2.95 T 1-93 [» ]
4PEC X-ray 2.95 T 1-93 [» ]
4TOM X-ray 3.00 T 1-93 [» ]
4TOO X-ray 3.00 T 1-93 [» ]
4TOV X-ray 2.90 T 1-93 [» ]
4TOX X-ray 2.90 T 1-93 [» ]
4TP1 X-ray 2.90 T 1-93 [» ]
4TP3 X-ray 2.90 T 1-93 [» ]
4TP5 X-ray 2.90 T 1-93 [» ]
4TP7 X-ray 2.90 T 1-93 [» ]
4TP9 X-ray 2.80 T 1-93 [» ]
4TPB X-ray 2.80 T 1-93 [» ]
4TPD X-ray 2.80 T 1-93 [» ]
4TPF X-ray 2.80 T 1-93 [» ]
ProteinModelPortali P0ADZ0.
SMRi P0ADZ0. Positions 7-98.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35972N.
IntActi P0ADZ0. 73 interactions.
MINTi MINT-1225825.
STRINGi 511145.b3318.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0ADZ0.
PRIDEi P0ADZ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76343 ; AAC76343 ; b3318 .
BAE77973 ; BAE77973 ; BAE77973 .
GeneIDi 12932296.
947819.
KEGGi ecj:Y75_p3858.
eco:b3318.
PATRICi 32122068. VBIEscCol129921_3411.

Organism-specific databases

EchoBASEi EB0876.
EcoGenei EG10883. rplW.

Phylogenomic databases

eggNOGi COG0089.
HOGENOMi HOG000231364.
InParanoidi P0ADZ0.
KOi K02892.
OMAi FGRRSDW.
OrthoDBi EOG6HTP4P.
PhylomeDBi P0ADZ0.

Enzyme and pathway databases

BioCyci EcoCyc:EG10883-MONOMER.
ECOL316407:JW3280-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ADZ0.
PROi P0ADZ0.

Gene expression databases

Genevestigatori P0ADZ0.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
HAMAPi MF_01369_B. Ribosomal_L23_B.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view ]
Pfami PF00276. Ribosomal_L23. 1 hit.
[Graphical view ]
SUPFAMi SSF54189. SSF54189. 1 hit.
PROSITEi PS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of protein L23 from the Escherichia coli ribosome."
    Wittmann-Liebold B., Greuer B.
    FEBS Lett. 108:69-74(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K12.
  2. "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].
  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. "The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
    Wower I., Wower J., Meinke M., Brimacombe R.
    Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO 23S RRNA.
    Strain: MRE-600.
  6. "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.
  7. "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 L29.
  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. Cited for: BINDING TO TRIGGER FACTOR, MUTAGENESIS OF 16-VAL--GLU-18; GLU-18; 51-PHE--VAL-53 AND GLU-52.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  10. "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
    Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
    J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  11. "The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
    Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
    RNA 9:566-573(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE.
    Strain: MRE-600.
  12. "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.
  13. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
    Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
    Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
    Strain: MRE-600.
  14. "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.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  16. Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.

Entry informationi

Entry nameiRL23_ECOLI
AccessioniPrimary (citable) accession number: P0ADZ0
Secondary accession number(s): P02424, Q2M6Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 6, 2005
Last modified: November 26, 2014
This is version 92 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