UniProtKB - P0A7L0 (RL1_ECOLI)
Protein
50S ribosomal protein L1
Gene
rplA
Organism
Escherichia coli (strain K12)
Status
Functioni
One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903, PubMed:16272117). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903, PubMed:16272117). Contacts the P and E site tRNAs.2 Publications
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
GO - Molecular functioni
- RNA binding Source: GO_Central
- rRNA binding Source: UniProtKB-UniRule
- structural constituent of ribosome Source: CAFA
- tRNA binding Source: UniProtKB-KW
GO - Biological processi
- maturation of LSU-rRNA Source: GO_Central
- negative regulation of translational initiation Source: EcoCyc
- ribosomal large subunit assembly Source: CAFA
- translation Source: UniProtKB-UniRule
Keywordsi
Molecular function | Repressor, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding |
Biological process | Translation regulation |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10864-MONOMER MetaCyc:EG10864-MONOMER |
Protein family/group databases
MoonProti | P0A7L0 |
Names & Taxonomyi
Protein namesi | Recommended name: 50S ribosomal protein L1Alternative name(s): Large ribosomal subunit protein uL11 Publication |
Gene namesi | Name:rplA Ordered Locus Names:b3984, JW3947 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
- cytosolic large ribosomal subunit Source: CAFA
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000125654 | 2 – 234 | 50S ribosomal protein L1Add BLAST | 233 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 105 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 154 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 186 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 197 | N6-succinyllysine1 Publication | 1 |
Proteomic databases
jPOSTi | P0A7L0 |
PaxDbi | P0A7L0 |
PRIDEi | P0A7L0 |
2D gel databases
SWISS-2DPAGEi | P0A7L0 |
Interactioni
Subunit structurei
Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.
Binary interactionsi
Hide detailsP0A7L0
Protein-protein interaction databases
BioGRIDi | 4259509, 105 interactors |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35746N |
IntActi | P0A7L0, 133 interactors |
STRINGi | 511145.b3984 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A7L0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7L0 |
Family & Domainsi
Sequence similaritiesi
Belongs to the universal ribosomal protein uL1 family.Curated
Phylogenomic databases
eggNOGi | COG0081, Bacteria |
HOGENOMi | CLU_062853_0_0_6 |
InParanoidi | P0A7L0 |
PhylomeDBi | P0A7L0 |
Family and domain databases
CDDi | cd00403, Ribosomal_L1, 1 hit |
Gene3Di | 3.40.50.790, 1 hit |
HAMAPi | MF_01318_B, Ribosomal_L1_B, 1 hit |
InterProi | View protein in InterPro IPR005878, Ribosom_L1_bac-type IPR002143, Ribosomal_L1 IPR023674, Ribosomal_L1-like IPR028364, Ribosomal_L1/biogenesis IPR016095, Ribosomal_L1_3-a/b-sand IPR023673, Ribosomal_L1_CS |
Pfami | View protein in Pfam PF00687, Ribosomal_L1, 1 hit |
PIRSFi | PIRSF002155, Ribosomal_L1, 1 hit |
SUPFAMi | SSF56808, SSF56808, 1 hit |
TIGRFAMsi | TIGR01169, rplA_bact, 1 hit |
PROSITEi | View protein in PROSITE PS01199, RIBOSOMAL_L1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A7L0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAKLTKRMRV IREKVDATKQ YDINEAIALL KELATAKFVE SVDVAVNLGI
60 70 80 90 100
DARKSDQNVR GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAELVGMEDL
110 120 130 140 150
ADQIKKGEMN FDVVIASPDA MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA
160 170 180 190 200
EAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF DADKLKENLE ALLVALKKAK
210 220 230
PTQAKGVYIK KVSISTTMGA GVAVDQAGLS ASVN
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 12 | R → I AA sequence (PubMed:9298646).Curated | 1 |
Mass spectrometryi
Molecular mass is 24598.9 Da. Determined by MALDI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23622.1 U00006 Genomic DNA Translation: AAC43082.1 U00096 Genomic DNA Translation: AAC76958.1 AP009048 Genomic DNA Translation: BAE77336.1 |
PIRi | S12573, R5EC1 |
RefSeqi | NP_418411.1, NC_000913.3 WP_001096684.1, NZ_STEB01000045.1 |
Genome annotation databases
EnsemblBacteriai | AAC76958; AAC76958; b3984 BAE77336; BAE77336; BAE77336 |
GeneIDi | 58462388 948483 |
KEGGi | ecj:JW3947 eco:b3984 |
PATRICi | fig|1411691.4.peg.2728 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23622.1 U00006 Genomic DNA Translation: AAC43082.1 U00096 Genomic DNA Translation: AAC76958.1 AP009048 Genomic DNA Translation: BAE77336.1 |
PIRi | S12573, R5EC1 |
RefSeqi | NP_418411.1, NC_000913.3 WP_001096684.1, NZ_STEB01000045.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EG0 | electron microscopy | 11.50 | N | 1-229 | [»] | |
1ML5 | electron microscopy | 14.00 | c | 2-229 | [»] | |
2RDO | electron microscopy | 9.10 | 9 | 2-234 | [»] | |
3J46 | electron microscopy | 10.10 | 5 | 1-234 | [»] | |
3J5S | electron microscopy | 7.50 | F | 1-234 | [»] | |
3J8G | electron microscopy | 5.00 | 5 | 1-234 | [»] | |
3J9Z | electron microscopy | 3.60 | LC | 1-234 | [»] | |
3JA1 | electron microscopy | 3.60 | LC | 1-234 | [»] | |
3JCD | electron microscopy | 3.70 | 5 | 1-234 | [»] | |
3JCE | electron microscopy | 3.20 | 5 | 1-234 | [»] | |
487D | electron microscopy | 7.50 | H | 29-201 | [»] | |
4CSU | electron microscopy | 5.50 | 5 | 1-234 | [»] | |
4U1U | X-ray | 2.95 | B5 | 2-229 | [»] | |
4U1V | X-ray | 3.00 | B5 | 2-229 | [»] | |
4U20 | X-ray | 2.90 | B5 | 2-229 | [»] | |
4U24 | X-ray | 2.90 | B5 | 2-229 | [»] | |
4U25 | X-ray | 2.90 | B5 | 2-229 | [»] | |
4U26 | X-ray | 2.80 | B5 | 2-229 | [»] | |
4U27 | X-ray | 2.80 | B5 | 2-229 | [»] | |
4V4V | electron microscopy | 15.00 | B2 | 6-227 | [»] | |
4V4W | electron microscopy | 15.00 | B2 | 6-227 | [»] | |
4V5H | electron microscopy | 5.80 | B5 | 1-234 | [»] | |
4V65 | electron microscopy | 9.00 | BZ | 5-220 | [»] | |
4V66 | electron microscopy | 9.00 | BZ | 5-220 | [»] | |
4V69 | electron microscopy | 6.70 | B5 | 1-234 | [»] | |
4V6K | electron microscopy | 8.25 | AC | 1-234 | [»] | |
4V6L | electron microscopy | 13.20 | BC | 1-234 | [»] | |
4V6M | electron microscopy | 7.10 | B5 | 1-234 | [»] | |
4V6N | electron microscopy | 12.10 | AC | 1-234 | [»] | |
4V6O | electron microscopy | 14.70 | BC | 1-234 | [»] | |
4V6P | electron microscopy | 13.50 | BC | 1-234 | [»] | |
4V6Q | electron microscopy | 11.50 | BC | 1-234 | [»] | |
4V6R | electron microscopy | 11.50 | BC | 1-234 | [»] | |
4V6S | electron microscopy | 13.10 | AC | 1-234 | [»] | |
4V6V | electron microscopy | 9.80 | BC | 1-234 | [»] | |
4V6Y | electron microscopy | 12.00 | B5 | 1-234 | [»] | |
4V6Z | electron microscopy | 12.00 | B5 | 1-234 | [»] | |
4V70 | electron microscopy | 17.00 | B5 | 1-234 | [»] | |
4V71 | electron microscopy | 20.00 | B5 | 1-234 | [»] | |
4V72 | electron microscopy | 13.00 | B5 | 1-234 | [»] | |
4V73 | electron microscopy | 15.00 | B5 | 1-234 | [»] | |
4V74 | electron microscopy | 17.00 | B5 | 1-234 | [»] | |
4V75 | electron microscopy | 12.00 | B5 | 1-234 | [»] | |
4V76 | electron microscopy | 17.00 | B5 | 1-234 | [»] | |
4V77 | electron microscopy | 17.00 | B5 | 1-234 | [»] | |
4V78 | electron microscopy | 20.00 | B5 | 1-234 | [»] | |
4V79 | electron microscopy | 15.00 | B5 | 1-234 | [»] | |
4V7A | electron microscopy | 9.00 | B5 | 1-234 | [»] | |
4V7C | electron microscopy | 7.60 | BC | 2-234 | [»] | |
4V7D | electron microscopy | 7.60 | AC | 2-234 | [»] | |
4V7I | electron microscopy | 9.60 | A5 | 1-234 | [»] | |
4WOI | X-ray | 3.00 | B5 | 2-229 | [»] | |
5ADY | electron microscopy | 4.50 | 5 | 1-234 | [»] | |
5U9F | electron microscopy | 3.20 | 03 | 1-234 | [»] | |
5U9G | electron microscopy | 3.20 | 03 | 1-234 | [»] | |
5UYK | electron microscopy | 3.90 | 03 | 3-225 | [»] | |
5UYL | electron microscopy | 3.60 | 03 | 1-234 | [»] | |
5UYM | electron microscopy | 3.20 | 03 | 3-225 | [»] | |
5UYN | electron microscopy | 4.00 | 03 | 3-225 | [»] | |
5UYP | electron microscopy | 3.90 | 03 | 3-225 | [»] | |
5UYQ | electron microscopy | 3.80 | 03 | 3-225 | [»] | |
6BU8 | electron microscopy | 3.50 | 03 | 3-225 | [»] | |
6ENJ | electron microscopy | 3.70 | 7 | 6-229 | [»] | |
6ENU | electron microscopy | 3.10 | 7 | 6-229 | [»] | |
6OFX | electron microscopy | 3.30 | a | 3-225 | [»] | |
6OG7 | electron microscopy | 3.30 | a | 3-225 | [»] | |
6WD6 | electron microscopy | 3.70 | a | 3-225 | [»] | |
6WDB | electron microscopy | 4.00 | a | 3-225 | [»] | |
6WDC | electron microscopy | 4.20 | a | 3-225 | [»] | |
6WDD | electron microscopy | 3.20 | a | 3-225 | [»] | |
6WDE | electron microscopy | 3.00 | a | 3-225 | [»] | |
6WDF | electron microscopy | 3.30 | a | 3-225 | [»] | |
6WDG | electron microscopy | 3.30 | a | 3-225 | [»] | |
6WDH | electron microscopy | 4.30 | a | 3-225 | [»] | |
6WDI | electron microscopy | 4.00 | a | 3-225 | [»] | |
6WDJ | electron microscopy | 3.70 | a | 3-225 | [»] | |
6WDK | electron microscopy | 3.60 | a | 3-225 | [»] | |
6WDL | electron microscopy | 3.70 | a | 3-225 | [»] | |
6WDM | electron microscopy | 3.60 | a | 3-225 | [»] | |
6WNT | electron microscopy | 3.10 | a | 3-225 | [»] | |
6WNV | electron microscopy | 3.50 | a | 3-225 | [»] | |
6WNW | electron microscopy | 3.20 | a | 3-225 | [»] | |
SMRi | P0A7L0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259509, 105 interactors |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35746N |
IntActi | P0A7L0, 133 interactors |
STRINGi | 511145.b3984 |
Protein family/group databases
MoonProti | P0A7L0 |
2D gel databases
SWISS-2DPAGEi | P0A7L0 |
Proteomic databases
jPOSTi | P0A7L0 |
PaxDbi | P0A7L0 |
PRIDEi | P0A7L0 |
Genome annotation databases
EnsemblBacteriai | AAC76958; AAC76958; b3984 BAE77336; BAE77336; BAE77336 |
GeneIDi | 58462388 948483 |
KEGGi | ecj:JW3947 eco:b3984 |
PATRICi | fig|1411691.4.peg.2728 |
Organism-specific databases
EchoBASEi | EB0857 |
Phylogenomic databases
eggNOGi | COG0081, Bacteria |
HOGENOMi | CLU_062853_0_0_6 |
InParanoidi | P0A7L0 |
PhylomeDBi | P0A7L0 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10864-MONOMER MetaCyc:EG10864-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A7L0 |
PROi | PR:P0A7L0 |
Family and domain databases
CDDi | cd00403, Ribosomal_L1, 1 hit |
Gene3Di | 3.40.50.790, 1 hit |
HAMAPi | MF_01318_B, Ribosomal_L1_B, 1 hit |
InterProi | View protein in InterPro IPR005878, Ribosom_L1_bac-type IPR002143, Ribosomal_L1 IPR023674, Ribosomal_L1-like IPR028364, Ribosomal_L1/biogenesis IPR016095, Ribosomal_L1_3-a/b-sand IPR023673, Ribosomal_L1_CS |
Pfami | View protein in Pfam PF00687, Ribosomal_L1, 1 hit |
PIRSFi | PIRSF002155, Ribosomal_L1, 1 hit |
SUPFAMi | SSF56808, SSF56808, 1 hit |
TIGRFAMsi | TIGR01169, rplA_bact, 1 hit |
PROSITEi | View protein in PROSITE PS01199, RIBOSOMAL_L1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RL1_ECOLI | |
Accessioni | P0A7L0Primary (citable) accession number: P0A7L0 Secondary accession number(s): P02384, Q2M8S0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 144 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Ribosomal proteins
Ribosomal proteins families and list of entries