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Protein

50S ribosomal protein L11

Gene

rplK

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

Functioni

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.

GO - Molecular functioni

  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • ribosomal large subunit assembly Source: CAFA
  • stringent response Source: EcoCyc
  • translational termination Source: EcoCyc

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10872-MONOMER.
MetaCyc:EG10872-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L11UniRule annotation
Alternative name(s):
Large ribosomal subunit protein uL111 Publication
Gene namesi
Name:rplKUniRule annotation
Synonyms:relC
Ordered Locus Names:b3983, JW3946
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10872. rplK.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: CAFA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001042832 – 14250S ribosomal protein L11Add BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N,N,N-trimethylalanine1 Publication1
Modified residuei4N6,N6,N6-trimethyllysine1 Publication1
Modified residuei40N6,N6,N6-trimethyllysine1 Publication1
Modified residuei72N6-succinyllysine1 Publication1
Modified residuei81N6-succinyllysine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

EPDiP0A7J7.
PaxDbiP0A7J7.
PRIDEiP0A7J7.

Interactioni

Subunit structurei

Part of the ribosomal stalk of the 50S ribosomal subunit (PubMed:15923259). Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex (PubMed:15923259).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
prmAP0A8T13EBI-547288,EBI-556300

Protein-protein interaction databases

BioGridi852778. 1 interactor.
DIPiDIP-35882N.
IntActiP0A7J7. 46 interactors.
MINTiMINT-1232893.
STRINGi316385.ECDH10B_4171.

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi76 – 83Combined sources8
Turni93 – 95Combined sources3
Helixi103 – 116Combined sources14
Helixi122 – 135Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50K1-140[»]
1MJ1electron microscopy13.00L1-141[»]
1ML5electron microscopy14.00l1-141[»]
2J28electron microscopy8.00I2-142[»]
2RDOelectron microscopy9.10I2-142[»]
3DEGelectron microscopy-H2-142[»]
3EP2electron microscopy-I2-142[»]
3EQ3electron microscopy-I2-142[»]
3EQ4electron microscopy-I2-142[»]
3J0Delectron microscopy11.10G2-142[»]
3J5Lelectron microscopy6.60I2-142[»]
3J7Zelectron microscopy3.90I1-142[»]
3J8Gelectron microscopy5.00I1-142[»]
3J9Yelectron microscopy3.90I1-142[»]
3J9Zelectron microscopy3.60LE2-142[»]
3JA1electron microscopy3.60LK2-142[»]
3JBVelectron microscopy3.32i1-142[»]
3JCDelectron microscopy3.70I1-142[»]
3JCEelectron microscopy3.20I1-142[»]
3JCJelectron microscopy3.70H1-142[»]
3JCNelectron microscopy4.60I1-142[»]
487Delectron microscopy7.50L10-86[»]
4CSUelectron microscopy5.50I2-142[»]
4U1UX-ray2.95BI/DI2-142[»]
4U1VX-ray3.00BI/DI2-142[»]
4U20X-ray2.90BI/DI2-142[»]
4U24X-ray2.90BI/DI2-142[»]
4U25X-ray2.90BI/DI2-142[»]
4U26X-ray2.80BI/DI2-142[»]
4U27X-ray2.80BI/DI2-142[»]
4UY8electron microscopy3.80I2-142[»]
4V47electron microscopy12.30AG2-142[»]
4V48electron microscopy11.50AG2-142[»]
4V4HX-ray3.46BI/DI1-142[»]
4V4QX-ray3.46BI/DI2-142[»]
4V4Velectron microscopy15.00BG3-141[»]
4V4Welectron microscopy15.00BG3-141[»]
4V50X-ray3.22BI/DI2-142[»]
4V52X-ray3.21BI/DI2-142[»]
4V53X-ray3.54BI/DI2-142[»]
4V54X-ray3.30BI/DI2-142[»]
4V55X-ray4.00BI/DI2-142[»]
4V56X-ray3.93BI/DI2-142[»]
4V57X-ray3.50BI/DI2-142[»]
4V5BX-ray3.74AI/CI2-142[»]
4V5Helectron microscopy5.80BI2-142[»]
4V5YX-ray4.45BI/DI2-142[»]
4V64X-ray3.50BI/DI2-142[»]
4V65electron microscopy9.00B51-142[»]
4V66electron microscopy9.00B51-142[»]
4V69electron microscopy6.70BI2-142[»]
4V6CX-ray3.19BI/DI1-142[»]
4V6DX-ray3.81BI/DI1-142[»]
4V6EX-ray3.71BI/DI1-142[»]
4V6Kelectron microscopy8.25AJ1-142[»]
4V6Lelectron microscopy13.20BJ1-142[»]
4V6Melectron microscopy7.10BI2-142[»]
4V6Nelectron microscopy12.10AK2-142[»]
4V6Oelectron microscopy14.70BK2-142[»]
4V6Pelectron microscopy13.50BK2-142[»]
4V6Qelectron microscopy11.50BK2-142[»]
4V6Relectron microscopy11.50BK2-142[»]
4V6Selectron microscopy13.10AK2-142[»]
4V6Telectron microscopy8.30BI2-142[»]
4V6Velectron microscopy9.80BK2-142[»]
4V6Yelectron microscopy12.00BI1-142[»]
4V6Zelectron microscopy12.00BI1-142[»]
4V70electron microscopy17.00BI1-142[»]
4V71electron microscopy20.00BI1-142[»]
4V72electron microscopy13.00BI1-142[»]
4V73electron microscopy15.00BI1-142[»]
4V74electron microscopy17.00BI1-142[»]
4V75electron microscopy12.00BI1-142[»]
4V76electron microscopy17.00BI1-142[»]
4V77electron microscopy17.00BI1-142[»]
4V78electron microscopy20.00BI1-142[»]
4V79electron microscopy15.00BI1-142[»]
4V7Aelectron microscopy9.00BI1-142[»]
4V7Belectron microscopy6.80BI1-142[»]
4V7Celectron microscopy7.60BK2-142[»]
4V7Delectron microscopy7.60AK2-142[»]
4V7Ielectron microscopy9.60AI1-142[»]
4V7SX-ray3.25BI/DI2-142[»]
4V7TX-ray3.19BI/DI2-142[»]
4V7UX-ray3.10BI/DI2-142[»]
4V7VX-ray3.29BI/DI2-142[»]
4V85X-ray3.20I1-142[»]
4V89X-ray3.70BI1-142[»]
4V9CX-ray3.30BI/DI1-142[»]
4V9DX-ray3.00CI/DI2-142[»]
4V9OX-ray2.90AI/CI/EI/GI1-142[»]
4V9PX-ray2.90AI/CI/EI/GI1-142[»]
4WF1X-ray3.09BI/DI2-142[»]
4WOIX-ray3.00BI/CI1-142[»]
4WWWX-ray3.10RI/YI2-142[»]
4YBBX-ray2.10CJ/DJ8-141[»]
5ADYelectron microscopy4.50I1-142[»]
5AFIelectron microscopy2.90I1-142[»]
5AKAelectron microscopy5.70I2-142[»]
5GADelectron microscopy3.70J1-142[»]
5GAEelectron microscopy3.33J1-142[»]
5GAFelectron microscopy4.30J8-141[»]
5GAGelectron microscopy3.80J1-142[»]
5GAHelectron microscopy3.80J1-142[»]
5H5Uelectron microscopy3.00J2-142[»]
5IQRelectron microscopy3.00I1-142[»]
5IT8X-ray3.12CJ/DJ8-141[»]
5J5BX-ray2.80CJ/DJ8-141[»]
5J7LX-ray3.00CJ/DJ8-141[»]
5J88X-ray3.32CJ/DJ8-142[»]
5J8AX-ray3.10CJ/DJ8-142[»]
5J91X-ray2.96CJ/DJ8-141[»]
5JC9X-ray3.03CJ/DJ8-141[»]
5JTEelectron microscopy3.60BI1-142[»]
5JU8electron microscopy3.60BI1-142[»]
5KCRelectron microscopy3.601K1-142[»]
5KCSelectron microscopy3.901K1-142[»]
5KPSelectron microscopy3.90I1-142[»]
5KPVelectron microscopy4.10H1-142[»]
5KPWelectron microscopy3.90H1-142[»]
5KPXelectron microscopy3.90H1-142[»]
5L3Pelectron microscopy3.70K1-142[»]
5LZAelectron microscopy3.60I2-142[»]
5LZBelectron microscopy5.30I2-142[»]
5LZCelectron microscopy4.80I2-142[»]
5LZDelectron microscopy3.40I2-142[»]
5LZEelectron microscopy3.50I2-142[»]
5LZFelectron microscopy4.60I2-142[»]
5MDVelectron microscopy2.97I1-142[»]
5MDWelectron microscopy3.06I1-142[»]
5MDYelectron microscopy3.35I1-142[»]
5MDZelectron microscopy3.10I1-142[»]
5U4Ielectron microscopy3.50J1-142[»]
5U9Felectron microscopy3.20111-142[»]
5U9Gelectron microscopy3.20111-142[»]
ProteinModelPortaliP0A7J7.
SMRiP0A7J7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7J7.

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL11 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0080. LUCA.
HOGENOMiHOG000082123.
InParanoidiP0A7J7.
KOiK02867.
PhylomeDBiP0A7J7.

Family and domain databases

CDDicd00349. Ribosomal_L11. 1 hit.
Gene3Di1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPiMF_00736. Ribosomal_L11. 1 hit.
InterProiView protein in InterPro
IPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
PANTHERiPTHR11661. PTHR11661. 1 hit.
PfamiView protein in Pfam
PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
SMARTiView protein in SMART
SM00649. RL11. 1 hit.
SUPFAMiSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsiTIGR01632. L11_bact. 1 hit.
PROSITEiView protein in PROSITE
PS00359. RIBOSOMAL_L11. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE
60 70 80 90 100
KGLPIPVVIT VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK
110 120 130 140
ISRAQLQEIA QTKAADMTGA DIEAMTRSIE GTARSMGLVV ED
Length:142
Mass (Da):14,875
Last modified:January 23, 2007 - v2
Checksum:iC49226BB2462BE0F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132T → S in CAA23621 (PubMed:377281).Curated1

Mass spectrometryi

Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23621.1.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.
PIRiS12572. R5EC11.
RefSeqiNP_418410.1. NC_000913.3.
WP_001085926.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.
GeneIDi948484.
KEGGiecj:JW3946.
eco:b3983.
PATRICifig|1411691.4.peg.2729.

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 one 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.

Entry informationi

Entry nameiRL11_ECOLI
AccessioniPrimary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 128 of the entry and version 2 of the sequence. See 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