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Protein

50S ribosomal protein L36

Gene

rpmJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG11232-MONOMER.
ECOL316407:JW3261-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L36
Alternative name(s):
Ribosomal protein B
Gene namesi
Name:rpmJ
Ordered Locus Names:b3299, JW3261
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11232. rpmJ.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 383850S ribosomal protein L36PRO_0000126183Add
BLAST

Proteomic databases

PaxDbiP0A7Q6.

Expressioni

Gene expression databases

GenevestigatoriP0A7Q6.

Interactioni

Protein-protein interaction databases

IntActiP0A7Q6. 2 interactions.
STRINGi511145.b3299.

Structurei

Secondary structure

1
38
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi11 – 199Combined sources
Beta strandi22 – 298Combined sources
Helixi31 – 333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0041-38[»]
2RDOelectron microscopy9.1041-38[»]
3BBXelectron microscopy10.0041-38[»]
3J5Lelectron microscopy6.6041-38[»]
3J7Zelectron microscopy3.9041-38[»]
4CSUelectron microscopy5.5081-38[»]
4U1UX-ray2.95B4/D41-38[»]
4U1VX-ray3.00B4/D41-38[»]
4U20X-ray2.90B4/D41-38[»]
4U24X-ray2.90B4/D41-38[»]
4U25X-ray2.90B4/D41-38[»]
4U26X-ray2.80B4/D41-38[»]
4U27X-ray2.80B4/D41-38[»]
4UY8electron microscopy3.8041-38[»]
4V47electron microscopy12.30A41-38[»]
4V48electron microscopy11.50A41-38[»]
4V4HX-ray3.46B4/D41-38[»]
4V4QX-ray3.46B4/D41-38[»]
4V50X-ray3.22B4/D41-38[»]
4V52X-ray3.21B4/D41-38[»]
4V53X-ray3.54B4/D41-38[»]
4V54X-ray3.30B4/D41-38[»]
4V55X-ray4.00B4/D41-38[»]
4V56X-ray3.93B4/D41-38[»]
4V57X-ray3.50B4/D41-38[»]
4V5BX-ray3.74A4/C41-38[»]
4V5Helectron microscopy5.80B81-38[»]
4V5YX-ray4.45B4/D41-38[»]
4V64X-ray3.50B4/D41-38[»]
4V65electron microscopy9.00BX1-38[»]
4V66electron microscopy9.00BX1-38[»]
4V69electron microscopy6.70B41-38[»]
4V6CX-ray3.19B4/D41-38[»]
4V6DX-ray3.81B4/D41-38[»]
4V6EX-ray3.71B4/D41-38[»]
4V6Kelectron microscopy8.25Ag1-38[»]
4V6Lelectron microscopy13.20Bg1-38[»]
4V6Melectron microscopy7.10B41-38[»]
4V6Nelectron microscopy12.10A71-38[»]
4V6Oelectron microscopy14.70B71-38[»]
4V6Pelectron microscopy13.50B71-38[»]
4V6Qelectron microscopy11.50B71-38[»]
4V6Relectron microscopy11.50B71-38[»]
4V6Selectron microscopy13.10A71-38[»]
4V6Telectron microscopy8.30B41-38[»]
4V6Velectron microscopy9.8091-38[»]
4V6Yelectron microscopy12.00B41-38[»]
4V6Zelectron microscopy12.00B41-38[»]
4V70electron microscopy17.00B41-38[»]
4V71electron microscopy20.00B41-38[»]
4V72electron microscopy13.00B41-38[»]
4V73electron microscopy15.00B41-38[»]
4V74electron microscopy17.00B41-38[»]
4V75electron microscopy12.00B41-38[»]
4V76electron microscopy17.00B41-38[»]
4V77electron microscopy17.00B41-38[»]
4V78electron microscopy20.00B41-38[»]
4V79electron microscopy15.00B41-38[»]
4V7Aelectron microscopy9.00B41-38[»]
4V7Belectron microscopy6.80B41-38[»]
4V7Celectron microscopy7.60B71-38[»]
4V7Delectron microscopy7.60A81-38[»]
4V7Ielectron microscopy9.60A41-38[»]
4V7SX-ray3.25B4/D41-38[»]
4V7TX-ray3.19B4/D41-38[»]
4V7UX-ray3.10B4/D41-38[»]
4V7VX-ray3.29B4/D41-38[»]
4V85X-ray3.2081-38[»]
4V89X-ray3.70B81-38[»]
4V9CX-ray3.30B4/D41-38[»]
4V9DX-ray3.00C4/D41-38[»]
4V9OX-ray2.90A4/C4/E4/G41-38[»]
4V9PX-ray2.90A4/C4/E4/G41-38[»]
4WF1X-ray3.09B4/D41-38[»]
4WWWX-ray3.10R4/Y41-38[»]
4YBBX-ray2.10C5/D51-38[»]
5AFIelectron microscopy2.9041-38[»]
5AKAelectron microscopy5.7041-38[»]
ProteinModelPortaliP0A7Q6.
SMRiP0A7Q6. Positions 1-38.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Q6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L36P family.Curated

Phylogenomic databases

eggNOGiCOG0257.
HOGENOMiHOG000111584.
InParanoidiP0A7Q6.
KOiK02919.
OrthoDBiEOG676ZC2.
PhylomeDBiP0A7Q6.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 1 hit.
PROSITEiPS00828. RIBOSOMAL_L36. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
MKVRASVKKL CRNCKIVKRD GVIRVICSAE PKHKQRQG
Length:38
Mass (Da):4,364
Last modified:June 7, 2005 - v1
Checksum:iC4785CEC0578EB24
GO

Mass spectrometryi

Molecular mass is 4364.2 Da from positions 1 - 38. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12432 Genomic DNA. Translation: AAA83902.1.
X01563 Genomic DNA. Translation: CAA25726.1.
U18997 Genomic DNA. Translation: AAA58096.1.
U00096 Genomic DNA. Translation: AAC76324.1.
AP009048 Genomic DNA. Translation: BAE77992.1.
PIRiS14057. R5EC36.
RefSeqiNP_417758.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76324; AAC76324; b3299.
BAE77992; BAE77992; BAE77992.
GeneIDi947805.
KEGGiecj:Y75_p3877.
eco:b3299.
PATRICi32122030. VBIEscCol129921_3392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12432 Genomic DNA. Translation: AAA83902.1.
X01563 Genomic DNA. Translation: CAA25726.1.
U18997 Genomic DNA. Translation: AAA58096.1.
U00096 Genomic DNA. Translation: AAC76324.1.
AP009048 Genomic DNA. Translation: BAE77992.1.
PIRiS14057. R5EC36.
RefSeqiNP_417758.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0041-38[»]
2RDOelectron microscopy9.1041-38[»]
3BBXelectron microscopy10.0041-38[»]
3J5Lelectron microscopy6.6041-38[»]
3J7Zelectron microscopy3.9041-38[»]
4CSUelectron microscopy5.5081-38[»]
4U1UX-ray2.95B4/D41-38[»]
4U1VX-ray3.00B4/D41-38[»]
4U20X-ray2.90B4/D41-38[»]
4U24X-ray2.90B4/D41-38[»]
4U25X-ray2.90B4/D41-38[»]
4U26X-ray2.80B4/D41-38[»]
4U27X-ray2.80B4/D41-38[»]
4UY8electron microscopy3.8041-38[»]
4V47electron microscopy12.30A41-38[»]
4V48electron microscopy11.50A41-38[»]
4V4HX-ray3.46B4/D41-38[»]
4V4QX-ray3.46B4/D41-38[»]
4V50X-ray3.22B4/D41-38[»]
4V52X-ray3.21B4/D41-38[»]
4V53X-ray3.54B4/D41-38[»]
4V54X-ray3.30B4/D41-38[»]
4V55X-ray4.00B4/D41-38[»]
4V56X-ray3.93B4/D41-38[»]
4V57X-ray3.50B4/D41-38[»]
4V5BX-ray3.74A4/C41-38[»]
4V5Helectron microscopy5.80B81-38[»]
4V5YX-ray4.45B4/D41-38[»]
4V64X-ray3.50B4/D41-38[»]
4V65electron microscopy9.00BX1-38[»]
4V66electron microscopy9.00BX1-38[»]
4V69electron microscopy6.70B41-38[»]
4V6CX-ray3.19B4/D41-38[»]
4V6DX-ray3.81B4/D41-38[»]
4V6EX-ray3.71B4/D41-38[»]
4V6Kelectron microscopy8.25Ag1-38[»]
4V6Lelectron microscopy13.20Bg1-38[»]
4V6Melectron microscopy7.10B41-38[»]
4V6Nelectron microscopy12.10A71-38[»]
4V6Oelectron microscopy14.70B71-38[»]
4V6Pelectron microscopy13.50B71-38[»]
4V6Qelectron microscopy11.50B71-38[»]
4V6Relectron microscopy11.50B71-38[»]
4V6Selectron microscopy13.10A71-38[»]
4V6Telectron microscopy8.30B41-38[»]
4V6Velectron microscopy9.8091-38[»]
4V6Yelectron microscopy12.00B41-38[»]
4V6Zelectron microscopy12.00B41-38[»]
4V70electron microscopy17.00B41-38[»]
4V71electron microscopy20.00B41-38[»]
4V72electron microscopy13.00B41-38[»]
4V73electron microscopy15.00B41-38[»]
4V74electron microscopy17.00B41-38[»]
4V75electron microscopy12.00B41-38[»]
4V76electron microscopy17.00B41-38[»]
4V77electron microscopy17.00B41-38[»]
4V78electron microscopy20.00B41-38[»]
4V79electron microscopy15.00B41-38[»]
4V7Aelectron microscopy9.00B41-38[»]
4V7Belectron microscopy6.80B41-38[»]
4V7Celectron microscopy7.60B71-38[»]
4V7Delectron microscopy7.60A81-38[»]
4V7Ielectron microscopy9.60A41-38[»]
4V7SX-ray3.25B4/D41-38[»]
4V7TX-ray3.19B4/D41-38[»]
4V7UX-ray3.10B4/D41-38[»]
4V7VX-ray3.29B4/D41-38[»]
4V85X-ray3.2081-38[»]
4V89X-ray3.70B81-38[»]
4V9CX-ray3.30B4/D41-38[»]
4V9DX-ray3.00C4/D41-38[»]
4V9OX-ray2.90A4/C4/E4/G41-38[»]
4V9PX-ray2.90A4/C4/E4/G41-38[»]
4WF1X-ray3.09B4/D41-38[»]
4WWWX-ray3.10R4/Y41-38[»]
4YBBX-ray2.10C5/D51-38[»]
5AFIelectron microscopy2.9041-38[»]
5AKAelectron microscopy5.7041-38[»]
ProteinModelPortaliP0A7Q6.
SMRiP0A7Q6. Positions 1-38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A7Q6. 2 interactions.
STRINGi511145.b3299.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76324; AAC76324; b3299.
BAE77992; BAE77992; BAE77992.
GeneIDi947805.
KEGGiecj:Y75_p3877.
eco:b3299.
PATRICi32122030. VBIEscCol129921_3392.

Organism-specific databases

EchoBASEiEB1214.
EcoGeneiEG11232. rpmJ.

Phylogenomic databases

eggNOGiCOG0257.
HOGENOMiHOG000111584.
InParanoidiP0A7Q6.
KOiK02919.
OrthoDBiEOG676ZC2.
PhylomeDBiP0A7Q6.

Enzyme and pathway databases

BioCyciEcoCyc:EG11232-MONOMER.
ECOL316407:JW3261-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7Q6.
PROiP0A7Q6.

Gene expression databases

GenevestigatoriP0A7Q6.

Family and domain databases

HAMAPiMF_00251. Ribosomal_L36.
InterProiIPR000473. Ribosomal_L36.
[Graphical view]
PANTHERiPTHR18804. PTHR18804. 1 hit.
PfamiPF00444. Ribosomal_L36. 1 hit.
[Graphical view]
SUPFAMiSSF57840. SSF57840. 1 hit.
TIGRFAMsiTIGR01022. rpmJ_bact. 1 hit.
PROSITEiPS00828. RIBOSOMAL_L36. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli."
    Post L.E., Arfsten A.E., Davis G.R., Nomura M.
    J. Biol. Chem. 255:4653-4659(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Primary structures of and genes for new ribosomal proteins A and B in Escherichia coli."
    Wada A., Sako T.
    J. Biochem. 101:817-820(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17.
  5. "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.
  6. "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.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  8. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL36_ECOLI
AccessioniPrimary (citable) accession number: P0A7Q6
Secondary accession number(s): P21194, Q2M6W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 27, 2015
This is version 96 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.