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P02413

- RL15_ECOLI

UniProt

P02413 - RL15_ECOLI

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Protein

50S ribosomal protein L15

Gene
rplO, b3301, JW3263
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.UniRule annotation

GO - Molecular functioni

  1. protein binding Source: IntAct
  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:EG10876-MONOMER.
ECOL316407:JW3263-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L15
Gene namesi
Name:rplO
Ordered Locus Names:b3301, JW3263
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10876. rplO.

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 – 14414450S ribosomal protein L15UniRule annotationPRO_0000104721Add
BLAST

Proteomic databases

PaxDbiP02413.
PRIDEiP02413.

Expressioni

Gene expression databases

GenevestigatoriP02413.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts the 5S rRNA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
rlmNP369793EBI-543017,EBI-559071

Protein-protein interaction databases

DIPiDIP-10752N.
IntActiP02413. 78 interactions.
MINTiMINT-1260355.
STRINGi511145.b3301.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53
Beta strandi10 – 134
Helixi22 – 254
Turni29 – 324
Beta strandi35 – 373
Turni38 – 403
Beta strandi41 – 433
Beta strandi47 – 493
Beta strandi52 – 543
Helixi57 – 604
Helixi71 – 733
Beta strandi74 – 763
Turni79 – 824
Helixi83 – 853
Beta strandi86 – 916
Turni92 – 998
Beta strandi103 – 1053
Beta strandi107 – 1093
Beta strandi121 – 1244
Helixi129 – 1368
Turni137 – 1393
Beta strandi141 – 1433

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00o2-144[»]
1P85electron microscopy12.30J1-144[»]
1P86electron microscopy11.50J1-144[»]
1VS6X-ray3.46L1-144[»]
1VS8X-ray3.46L1-144[»]
1VT2X-ray3.30L1-144[»]
2AW4X-ray3.46L1-144[»]
2AWBX-ray3.46L1-144[»]
2GYAelectron microscopy15.00J4-143[»]
2GYCelectron microscopy15.00J4-143[»]
2I2TX-ray3.22L1-144[»]
2I2VX-ray3.22L1-144[»]
2J28electron microscopy8.00L1-144[»]
2QAMX-ray3.21L1-144[»]
2QAOX-ray3.21L1-144[»]
2QBAX-ray3.54L1-144[»]
2QBCX-ray3.54L1-144[»]
2QBEX-ray3.30L1-144[»]
2QBGX-ray3.30L1-144[»]
2QBIX-ray4.00L1-144[»]
2QBKX-ray4.00L1-144[»]
2QOVX-ray3.93L1-144[»]
2QOXX-ray3.93L1-144[»]
2QOZX-ray3.50L1-144[»]
2QP1X-ray3.50L1-144[»]
2RDOelectron microscopy9.10L1-144[»]
2VHMX-ray3.74L1-144[»]
2VHNX-ray3.74L1-144[»]
2WWQelectron microscopy5.80L2-144[»]
2Z4LX-ray4.45L1-144[»]
2Z4NX-ray4.45L1-144[»]
3BBXelectron microscopy10.00L1-144[»]
3DF2X-ray3.50L1-144[»]
3DF4X-ray3.50L1-144[»]
3E1Belectron microscopy-E1-144[»]
3E1Delectron microscopy-E1-144[»]
3FIKelectron microscopy6.70L2-144[»]
3I1NX-ray3.19L1-144[»]
3I1PX-ray3.19L1-144[»]
3I1RX-ray3.81L1-144[»]
3I1TX-ray3.81L1-144[»]
3I20X-ray3.71L1-144[»]
3I22X-ray3.71L1-144[»]
3IY9electron microscopy14.10L2-144[»]
3IZTelectron microscopy-M1-144[»]
3IZUelectron microscopy-M1-144[»]
3J01electron microscopy-L1-144[»]
3J0Telectron microscopy12.10N1-144[»]
3J0Welectron microscopy14.70N1-144[»]
3J0Yelectron microscopy13.50N1-144[»]
3J11electron microscopy13.10N1-144[»]
3J12electron microscopy11.50N1-144[»]
3J14electron microscopy11.50N1-144[»]
3J19electron microscopy8.30L2-144[»]
3J37electron microscopy9.80P1-144[»]
3J4Xelectron microscopy12.00L1-144[»]
3J50electron microscopy20.00L1-144[»]
3J51electron microscopy17.00L1-144[»]
3J52electron microscopy12.00L1-144[»]
3J54electron microscopy13.00L1-144[»]
3J56electron microscopy15.00L1-144[»]
3J58electron microscopy17.00L1-144[»]
3J5Aelectron microscopy12.00L1-144[»]
3J5Celectron microscopy17.00L1-144[»]
3J5Eelectron microscopy17.00L1-144[»]
3J5Gelectron microscopy20.00L1-144[»]
3J5Ielectron microscopy15.00L1-144[»]
3J5Kelectron microscopy9.00L1-144[»]
3J5Lelectron microscopy6.60L2-144[»]
3J5Oelectron microscopy6.80L1-144[»]
3J5Uelectron microscopy7.60N1-144[»]
3J5Welectron microscopy7.60O1-144[»]
3KCRelectron microscopy-L1-144[»]
3OASX-ray3.25L2-144[»]
3OATX-ray3.25L2-144[»]
3OFCX-ray3.19L2-144[»]
3OFDX-ray3.19L2-144[»]
3OFQX-ray3.10L2-144[»]
3OFRX-ray3.10L2-144[»]
3OFZX-ray3.29L2-144[»]
3OG0X-ray3.29L2-144[»]
3ORBX-ray3.30L1-144[»]
3R8SX-ray3.00L2-144[»]
3R8TX-ray3.00L2-144[»]
3SGFX-ray3.20P1-144[»]
3UOSX-ray3.70P1-144[»]
4CSUelectron microscopy5.50L2-144[»]
4GARX-ray3.30L1-144[»]
4GAUX-ray3.30L1-144[»]
4KIXX-ray2.90L1-144[»]
4KIZX-ray2.90L1-144[»]
4KJ1X-ray2.90L1-144[»]
4KJ3X-ray2.90L1-144[»]
4KJ5X-ray2.90L1-144[»]
4KJ7X-ray2.90L1-144[»]
4KJ9X-ray2.90L1-144[»]
4KJBX-ray2.90L1-144[»]
ProteinModelPortaliP02413.
SMRiP02413. Positions 2-144.

Miscellaneous databases

EvolutionaryTraceiP02413.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0200.
HOGENOMiHOG000231262.
KOiK02876.
OMAiRGHKGLK.
OrthoDBiEOG6CGCM5.
PhylomeDBiP02413.

Family and domain databases

HAMAPiMF_01341_B. Ribosomal_L15_B.
InterProiIPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PANTHERiPTHR12934. PTHR12934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02413-1 [UniParc]FASTAAdd to Basket

« Hide

MRLNTLSPAE GSKKAGKRLG RGIGSGLGKT GGRGHKGQKS RSGGGVRRGF    50
EGGQMPLYRR LPKFGFTSRK AAITAEIRLS DLAKVEGGVV DLNTLKAANI 100
IGIQIEFAKV ILAGEVTTPV TVRGLRVTKG ARAAIEAAGG KIEE 144
Length:144
Mass (Da):14,980
Last modified:July 21, 1986 - v1
Checksum:i53D14CD948815FD9
GO

Mass spectrometryi

Molecular mass is 14980.1 Da from positions 1 - 144. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25724.1.
U18997 Genomic DNA. Translation: AAA58098.1.
U00096 Genomic DNA. Translation: AAC76326.1.
AP009048 Genomic DNA. Translation: BAE77990.1.
PIRiA02794. R5EC15.
RefSeqiNP_417760.1. NC_000913.3.
YP_492131.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76326; AAC76326; b3301.
BAE77990; BAE77990; BAE77990.
GeneIDi12934400.
947798.
KEGGiecj:Y75_p3875.
eco:b3301.
PATRICi32122034. VBIEscCol129921_3394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25724.1 .
U18997 Genomic DNA. Translation: AAA58098.1 .
U00096 Genomic DNA. Translation: AAC76326.1 .
AP009048 Genomic DNA. Translation: BAE77990.1 .
PIRi A02794. R5EC15.
RefSeqi NP_417760.1. NC_000913.3.
YP_492131.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 o 2-144 [» ]
1P85 electron microscopy 12.30 J 1-144 [» ]
1P86 electron microscopy 11.50 J 1-144 [» ]
1VS6 X-ray 3.46 L 1-144 [» ]
1VS8 X-ray 3.46 L 1-144 [» ]
1VT2 X-ray 3.30 L 1-144 [» ]
2AW4 X-ray 3.46 L 1-144 [» ]
2AWB X-ray 3.46 L 1-144 [» ]
2GYA electron microscopy 15.00 J 4-143 [» ]
2GYC electron microscopy 15.00 J 4-143 [» ]
2I2T X-ray 3.22 L 1-144 [» ]
2I2V X-ray 3.22 L 1-144 [» ]
2J28 electron microscopy 8.00 L 1-144 [» ]
2QAM X-ray 3.21 L 1-144 [» ]
2QAO X-ray 3.21 L 1-144 [» ]
2QBA X-ray 3.54 L 1-144 [» ]
2QBC X-ray 3.54 L 1-144 [» ]
2QBE X-ray 3.30 L 1-144 [» ]
2QBG X-ray 3.30 L 1-144 [» ]
2QBI X-ray 4.00 L 1-144 [» ]
2QBK X-ray 4.00 L 1-144 [» ]
2QOV X-ray 3.93 L 1-144 [» ]
2QOX X-ray 3.93 L 1-144 [» ]
2QOZ X-ray 3.50 L 1-144 [» ]
2QP1 X-ray 3.50 L 1-144 [» ]
2RDO electron microscopy 9.10 L 1-144 [» ]
2VHM X-ray 3.74 L 1-144 [» ]
2VHN X-ray 3.74 L 1-144 [» ]
2WWQ electron microscopy 5.80 L 2-144 [» ]
2Z4L X-ray 4.45 L 1-144 [» ]
2Z4N X-ray 4.45 L 1-144 [» ]
3BBX electron microscopy 10.00 L 1-144 [» ]
3DF2 X-ray 3.50 L 1-144 [» ]
3DF4 X-ray 3.50 L 1-144 [» ]
3E1B electron microscopy - E 1-144 [» ]
3E1D electron microscopy - E 1-144 [» ]
3FIK electron microscopy 6.70 L 2-144 [» ]
3I1N X-ray 3.19 L 1-144 [» ]
3I1P X-ray 3.19 L 1-144 [» ]
3I1R X-ray 3.81 L 1-144 [» ]
3I1T X-ray 3.81 L 1-144 [» ]
3I20 X-ray 3.71 L 1-144 [» ]
3I22 X-ray 3.71 L 1-144 [» ]
3IY9 electron microscopy 14.10 L 2-144 [» ]
3IZT electron microscopy - M 1-144 [» ]
3IZU electron microscopy - M 1-144 [» ]
3J01 electron microscopy - L 1-144 [» ]
3J0T electron microscopy 12.10 N 1-144 [» ]
3J0W electron microscopy 14.70 N 1-144 [» ]
3J0Y electron microscopy 13.50 N 1-144 [» ]
3J11 electron microscopy 13.10 N 1-144 [» ]
3J12 electron microscopy 11.50 N 1-144 [» ]
3J14 electron microscopy 11.50 N 1-144 [» ]
3J19 electron microscopy 8.30 L 2-144 [» ]
3J37 electron microscopy 9.80 P 1-144 [» ]
3J4X electron microscopy 12.00 L 1-144 [» ]
3J50 electron microscopy 20.00 L 1-144 [» ]
3J51 electron microscopy 17.00 L 1-144 [» ]
3J52 electron microscopy 12.00 L 1-144 [» ]
3J54 electron microscopy 13.00 L 1-144 [» ]
3J56 electron microscopy 15.00 L 1-144 [» ]
3J58 electron microscopy 17.00 L 1-144 [» ]
3J5A electron microscopy 12.00 L 1-144 [» ]
3J5C electron microscopy 17.00 L 1-144 [» ]
3J5E electron microscopy 17.00 L 1-144 [» ]
3J5G electron microscopy 20.00 L 1-144 [» ]
3J5I electron microscopy 15.00 L 1-144 [» ]
3J5K electron microscopy 9.00 L 1-144 [» ]
3J5L electron microscopy 6.60 L 2-144 [» ]
3J5O electron microscopy 6.80 L 1-144 [» ]
3J5U electron microscopy 7.60 N 1-144 [» ]
3J5W electron microscopy 7.60 O 1-144 [» ]
3KCR electron microscopy - L 1-144 [» ]
3OAS X-ray 3.25 L 2-144 [» ]
3OAT X-ray 3.25 L 2-144 [» ]
3OFC X-ray 3.19 L 2-144 [» ]
3OFD X-ray 3.19 L 2-144 [» ]
3OFQ X-ray 3.10 L 2-144 [» ]
3OFR X-ray 3.10 L 2-144 [» ]
3OFZ X-ray 3.29 L 2-144 [» ]
3OG0 X-ray 3.29 L 2-144 [» ]
3ORB X-ray 3.30 L 1-144 [» ]
3R8S X-ray 3.00 L 2-144 [» ]
3R8T X-ray 3.00 L 2-144 [» ]
3SGF X-ray 3.20 P 1-144 [» ]
3UOS X-ray 3.70 P 1-144 [» ]
4CSU electron microscopy 5.50 L 2-144 [» ]
4GAR X-ray 3.30 L 1-144 [» ]
4GAU X-ray 3.30 L 1-144 [» ]
4KIX X-ray 2.90 L 1-144 [» ]
4KIZ X-ray 2.90 L 1-144 [» ]
4KJ1 X-ray 2.90 L 1-144 [» ]
4KJ3 X-ray 2.90 L 1-144 [» ]
4KJ5 X-ray 2.90 L 1-144 [» ]
4KJ7 X-ray 2.90 L 1-144 [» ]
4KJ9 X-ray 2.90 L 1-144 [» ]
4KJB X-ray 2.90 L 1-144 [» ]
ProteinModelPortali P02413.
SMRi P02413. Positions 2-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10752N.
IntActi P02413. 78 interactions.
MINTi MINT-1260355.
STRINGi 511145.b3301.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P02413.
PRIDEi P02413.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76326 ; AAC76326 ; b3301 .
BAE77990 ; BAE77990 ; BAE77990 .
GeneIDi 12934400.
947798.
KEGGi ecj:Y75_p3875.
eco:b3301.
PATRICi 32122034. VBIEscCol129921_3394.

Organism-specific databases

EchoBASEi EB0869.
EcoGenei EG10876. rplO.

Phylogenomic databases

eggNOGi COG0200.
HOGENOMi HOG000231262.
KOi K02876.
OMAi RGHKGLK.
OrthoDBi EOG6CGCM5.
PhylomeDBi P02413.

Enzyme and pathway databases

BioCyci EcoCyc:EG10876-MONOMER.
ECOL316407:JW3263-MONOMER.

Miscellaneous databases

EvolutionaryTracei P02413.
PROi P02413.

Gene expression databases

Genevestigatori P02413.

Family and domain databases

HAMAPi MF_01341_B. Ribosomal_L15_B.
InterProi IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view ]
PANTHERi PTHR12934. PTHR12934. 1 hit.
Pfami PF00828. Ribosomal_L18e. 1 hit.
[Graphical view ]
SUPFAMi SSF52080. SSF52080. 1 hit.
TIGRFAMsi TIGR01071. rplO_bact. 1 hit.
PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L15 located at the peptidyltransferase center of Escherichia coli ribosomes."
    Giorginis S., Chen R.
    FEBS Lett. 84:347-350(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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. "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.
  6. "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.
  7. "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.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL15_ECOLI
AccessioniPrimary (citable) accession number: P02413
Secondary accession number(s): Q2M6W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 147 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