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Protein

50S ribosomal protein L13

Gene

rplM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.1 Publication

GO - Molecular functioni

  • structural constituent of ribosome Source: InterPro
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10874-MONOMER.
ECOL316407:JW3200-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L13UniRule annotation
Gene namesi
Name:rplMUniRule annotation
Ordered Locus Names:b3231, JW3200
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10874. rplM.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14214250S ribosomal protein L13PRO_0000133734Add
BLAST

Proteomic databases

PaxDbiP0AA10.
PRIDEiP0AA10.

Expressioni

Gene expression databases

GenevestigatoriP0AA10.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

BioGridi852140. 1 interaction.
DIPiDIP-47837N.
IntActiP0AA10. 112 interactions.
MINTiMINT-1269598.
STRINGi511145.b3231.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Beta strandi15 – 195Combined sources
Beta strandi21 – 233Combined sources
Helixi25 – 3612Combined sources
Turni37 – 404Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 483Combined sources
Beta strandi53 – 575Combined sources
Helixi59 – 613Combined sources
Beta strandi65 – 673Combined sources
Helixi68 – 714Combined sources
Beta strandi73 – 775Combined sources
Beta strandi79 – 824Combined sources
Beta strandi84 – 885Combined sources
Helixi89 – 957Combined sources
Helixi98 – 1069Combined sources
Helixi113 – 1197Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi126 – 1283Combined sources
Helixi133 – 1353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00m1-142[»]
2J28electron microscopy8.00J1-140[»]
2RDOelectron microscopy9.10J1-142[»]
3BBXelectron microscopy10.00J1-142[»]
3IY9electron microscopy14.10J1-140[»]
3J5Lelectron microscopy6.60J1-142[»]
3J7Zelectron microscopy3.90J1-142[»]
4CSUelectron microscopy5.50J1-142[»]
4U1UX-ray2.95BJ/DJ1-142[»]
4U1VX-ray3.00BJ/DJ1-142[»]
4U20X-ray2.90BJ/DJ1-142[»]
4U24X-ray2.90BJ/DJ1-142[»]
4U25X-ray2.90BJ/DJ1-142[»]
4U26X-ray2.80BJ/DJ1-142[»]
4U27X-ray2.80BJ/DJ1-142[»]
4UY8electron microscopy3.80J1-142[»]
4V47electron microscopy12.30AH1-142[»]
4V48electron microscopy11.50AH1-142[»]
4V4HX-ray3.46BJ/DJ1-142[»]
4V4QX-ray3.46BJ/DJ1-142[»]
4V4Velectron microscopy15.00BH1-142[»]
4V4Welectron microscopy15.00BH1-142[»]
4V50X-ray3.22BJ/DJ1-142[»]
4V52X-ray3.21BJ/DJ1-142[»]
4V53X-ray3.54BJ/DJ1-142[»]
4V54X-ray3.30BJ/DJ1-142[»]
4V55X-ray4.00BJ/DJ1-142[»]
4V56X-ray3.93BJ/DJ1-142[»]
4V57X-ray3.50BJ/DJ1-142[»]
4V5BX-ray3.74AJ/CJ1-142[»]
4V5Helectron microscopy5.80BJ1-142[»]
4V5YX-ray4.45BJ/DJ1-142[»]
4V64X-ray3.50BJ/DJ1-142[»]
4V65electron microscopy9.00B61-140[»]
4V66electron microscopy9.00B61-140[»]
4V69electron microscopy6.70BJ1-142[»]
4V6CX-ray3.19BJ/DJ1-142[»]
4V6DX-ray3.81BJ/DJ1-142[»]
4V6EX-ray3.71BJ/DJ1-142[»]
4V6Kelectron microscopy8.25AK1-142[»]
4V6Lelectron microscopy13.20BK1-142[»]
4V6Melectron microscopy7.10BJ1-142[»]
4V6Nelectron microscopy12.10AL1-142[»]
4V6Oelectron microscopy14.70BL1-142[»]
4V6Pelectron microscopy13.50BL1-142[»]
4V6Qelectron microscopy11.50BL1-142[»]
4V6Relectron microscopy11.50BL1-142[»]
4V6Selectron microscopy13.10AL1-142[»]
4V6Telectron microscopy8.30BJ1-142[»]
4V6Yelectron microscopy12.00BJ1-142[»]
4V6Zelectron microscopy12.00BJ1-142[»]
4V70electron microscopy17.00BJ1-142[»]
4V71electron microscopy20.00BJ1-142[»]
4V72electron microscopy13.00BJ1-142[»]
4V73electron microscopy15.00BJ1-142[»]
4V74electron microscopy17.00BJ1-142[»]
4V75electron microscopy12.00BJ1-142[»]
4V76electron microscopy17.00BJ1-142[»]
4V77electron microscopy17.00BJ1-142[»]
4V78electron microscopy20.00BJ1-142[»]
4V79electron microscopy15.00BJ1-142[»]
4V7Aelectron microscopy9.00BJ1-142[»]
4V7Belectron microscopy6.80BJ1-142[»]
4V7Celectron microscopy7.60BL1-142[»]
4V7Delectron microscopy7.60AM1-142[»]
4V7Ielectron microscopy9.60AJ1-142[»]
4V7SX-ray3.25BJ/DJ1-142[»]
4V7TX-ray3.19BJ/DJ1-142[»]
4V7UX-ray3.10BJ/DJ1-142[»]
4V7VX-ray3.29BJ/DJ1-142[»]
4V85X-ray3.20N1-142[»]
4V89X-ray3.70BN1-142[»]
4V9CX-ray3.30BJ/DJ1-142[»]
4V9DX-ray3.00CJ/DJ1-142[»]
4V9OX-ray2.90AJ/CJ/EJ/GJ1-142[»]
4V9PX-ray2.90AJ/CJ/EJ/GJ1-142[»]
4WF1X-ray3.09BJ/DJ1-142[»]
4WWWX-ray3.10RJ/YJ1-142[»]
4YBBX-ray2.10CK/DK1-142[»]
5AFIelectron microscopy2.90J1-142[»]
5AKAelectron microscopy5.70J1-142[»]
ProteinModelPortaliP0AA10.
SMRiP0AA10. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA10.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L13P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0102.
HOGENOMiHOG000225286.
InParanoidiP0AA10.
KOiK02871.
OMAiRNDKIYY.
OrthoDBiEOG628FBD.
PhylomeDBiP0AA10.

Family and domain databases

Gene3Di3.90.1180.10. 1 hit.
HAMAPiMF_01366. Ribosomal_L13.
InterProiIPR005822. Ribosomal_L13.
IPR005823. Ribosomal_L13_bac-type.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
[Graphical view]
PANTHERiPTHR11545. PTHR11545. 1 hit.
PfamiPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
PIRSFiPIRSF002181. Ribosomal_L13. 1 hit.
SUPFAMiSSF52161. SSF52161. 1 hit.
TIGRFAMsiTIGR01066. rplM_bact. 1 hit.
PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTFTAKPET VKRDWYVVDA TGKTLGRLAT ELARRLRGKH KAEYTPHVDT
60 70 80 90 100
GDYIIVLNAD KVAVTGNKRT DKVYYHHTGH IGGIKQATFE EMIARRPERV
110 120 130 140
IEIAVKGMLP KGPLGRAMFR KLKVYAGNEH NHAAQQPQVL DI
Length:142
Mass (Da):16,019
Last modified:July 21, 1986 - v1
Checksum:i58B45EF9EB75FDCD
GO

Mass spectrometryi

Molecular mass is 16018.0 Da from positions 1 - 142. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26041.1.
U18997 Genomic DNA. Translation: AAA58033.1.
U00096 Genomic DNA. Translation: AAC76263.1.
AP009048 Genomic DNA. Translation: BAE77274.1.
PIRiA02787. R5EC13.
RefSeqiNP_417698.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76263; AAC76263; b3231.
BAE77274; BAE77274; BAE77274.
GeneIDi947828.
KEGGiecj:Y75_p3151.
eco:b3231.
PATRICi32121888. VBIEscCol129921_3328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26041.1.
U18997 Genomic DNA. Translation: AAA58033.1.
U00096 Genomic DNA. Translation: AAC76263.1.
AP009048 Genomic DNA. Translation: BAE77274.1.
PIRiA02787. R5EC13.
RefSeqiNP_417698.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00m1-142[»]
2J28electron microscopy8.00J1-140[»]
2RDOelectron microscopy9.10J1-142[»]
3BBXelectron microscopy10.00J1-142[»]
3IY9electron microscopy14.10J1-140[»]
3J5Lelectron microscopy6.60J1-142[»]
3J7Zelectron microscopy3.90J1-142[»]
4CSUelectron microscopy5.50J1-142[»]
4U1UX-ray2.95BJ/DJ1-142[»]
4U1VX-ray3.00BJ/DJ1-142[»]
4U20X-ray2.90BJ/DJ1-142[»]
4U24X-ray2.90BJ/DJ1-142[»]
4U25X-ray2.90BJ/DJ1-142[»]
4U26X-ray2.80BJ/DJ1-142[»]
4U27X-ray2.80BJ/DJ1-142[»]
4UY8electron microscopy3.80J1-142[»]
4V47electron microscopy12.30AH1-142[»]
4V48electron microscopy11.50AH1-142[»]
4V4HX-ray3.46BJ/DJ1-142[»]
4V4QX-ray3.46BJ/DJ1-142[»]
4V4Velectron microscopy15.00BH1-142[»]
4V4Welectron microscopy15.00BH1-142[»]
4V50X-ray3.22BJ/DJ1-142[»]
4V52X-ray3.21BJ/DJ1-142[»]
4V53X-ray3.54BJ/DJ1-142[»]
4V54X-ray3.30BJ/DJ1-142[»]
4V55X-ray4.00BJ/DJ1-142[»]
4V56X-ray3.93BJ/DJ1-142[»]
4V57X-ray3.50BJ/DJ1-142[»]
4V5BX-ray3.74AJ/CJ1-142[»]
4V5Helectron microscopy5.80BJ1-142[»]
4V5YX-ray4.45BJ/DJ1-142[»]
4V64X-ray3.50BJ/DJ1-142[»]
4V65electron microscopy9.00B61-140[»]
4V66electron microscopy9.00B61-140[»]
4V69electron microscopy6.70BJ1-142[»]
4V6CX-ray3.19BJ/DJ1-142[»]
4V6DX-ray3.81BJ/DJ1-142[»]
4V6EX-ray3.71BJ/DJ1-142[»]
4V6Kelectron microscopy8.25AK1-142[»]
4V6Lelectron microscopy13.20BK1-142[»]
4V6Melectron microscopy7.10BJ1-142[»]
4V6Nelectron microscopy12.10AL1-142[»]
4V6Oelectron microscopy14.70BL1-142[»]
4V6Pelectron microscopy13.50BL1-142[»]
4V6Qelectron microscopy11.50BL1-142[»]
4V6Relectron microscopy11.50BL1-142[»]
4V6Selectron microscopy13.10AL1-142[»]
4V6Telectron microscopy8.30BJ1-142[»]
4V6Yelectron microscopy12.00BJ1-142[»]
4V6Zelectron microscopy12.00BJ1-142[»]
4V70electron microscopy17.00BJ1-142[»]
4V71electron microscopy20.00BJ1-142[»]
4V72electron microscopy13.00BJ1-142[»]
4V73electron microscopy15.00BJ1-142[»]
4V74electron microscopy17.00BJ1-142[»]
4V75electron microscopy12.00BJ1-142[»]
4V76electron microscopy17.00BJ1-142[»]
4V77electron microscopy17.00BJ1-142[»]
4V78electron microscopy20.00BJ1-142[»]
4V79electron microscopy15.00BJ1-142[»]
4V7Aelectron microscopy9.00BJ1-142[»]
4V7Belectron microscopy6.80BJ1-142[»]
4V7Celectron microscopy7.60BL1-142[»]
4V7Delectron microscopy7.60AM1-142[»]
4V7Ielectron microscopy9.60AJ1-142[»]
4V7SX-ray3.25BJ/DJ1-142[»]
4V7TX-ray3.19BJ/DJ1-142[»]
4V7UX-ray3.10BJ/DJ1-142[»]
4V7VX-ray3.29BJ/DJ1-142[»]
4V85X-ray3.20N1-142[»]
4V89X-ray3.70BN1-142[»]
4V9CX-ray3.30BJ/DJ1-142[»]
4V9DX-ray3.00CJ/DJ1-142[»]
4V9OX-ray2.90AJ/CJ/EJ/GJ1-142[»]
4V9PX-ray2.90AJ/CJ/EJ/GJ1-142[»]
4WF1X-ray3.09BJ/DJ1-142[»]
4WWWX-ray3.10RJ/YJ1-142[»]
4YBBX-ray2.10CK/DK1-142[»]
5AFIelectron microscopy2.90J1-142[»]
5AKAelectron microscopy5.70J1-142[»]
ProteinModelPortaliP0AA10.
SMRiP0AA10. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852140. 1 interaction.
DIPiDIP-47837N.
IntActiP0AA10. 112 interactions.
MINTiMINT-1269598.
STRINGi511145.b3231.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0AA10.
PRIDEiP0AA10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76263; AAC76263; b3231.
BAE77274; BAE77274; BAE77274.
GeneIDi947828.
KEGGiecj:Y75_p3151.
eco:b3231.
PATRICi32121888. VBIEscCol129921_3328.

Organism-specific databases

EchoBASEiEB0867.
EcoGeneiEG10874. rplM.

Phylogenomic databases

eggNOGiCOG0102.
HOGENOMiHOG000225286.
InParanoidiP0AA10.
KOiK02871.
OMAiRNDKIYY.
OrthoDBiEOG628FBD.
PhylomeDBiP0AA10.

Enzyme and pathway databases

BioCyciEcoCyc:EG10874-MONOMER.
ECOL316407:JW3200-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AA10.
PROiP0AA10.

Gene expression databases

GenevestigatoriP0AA10.

Family and domain databases

Gene3Di3.90.1180.10. 1 hit.
HAMAPiMF_01366. Ribosomal_L13.
InterProiIPR005822. Ribosomal_L13.
IPR005823. Ribosomal_L13_bac-type.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
[Graphical view]
PANTHERiPTHR11545. PTHR11545. 1 hit.
PfamiPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
PIRSFiPIRSF002181. Ribosomal_L13. 1 hit.
SUPFAMiSSF52161. SSF52161. 1 hit.
TIGRFAMsiTIGR01066. rplM_bact. 1 hit.
PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L13 from the large subunit of Escherichia coli ribosomes."
    Mende L.
    FEBS Lett. 96:313-316(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli."
    Isono S., Thamm S., Kitakawa M., Isono K.
    Mol. Gen. Genet. 198:279-282(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. "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 34-46.
    Strain: K12 / EMG2.
  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. "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).
    Strain: MRE-600.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  10. "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 nameiRL13_ECOLI
AccessioniPrimary (citable) accession number: P0AA10
Secondary accession number(s): P02410, Q2M8Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 27, 2015
This is version 98 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.