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Protein

50S ribosomal protein L35

Gene

rpmI

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

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG11231-MONOMER.
ECOL316407:JW1707-MONOMER.
MetaCyc:EG11231-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L35
Alternative name(s):
Ribosomal protein A
Gene namesi
Name:rpmI
Ordered Locus Names:b1717, JW1707
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11231. rpmI.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001773592 – 6550S ribosomal protein L35Add BLAST64

Proteomic databases

EPDiP0A7Q1.
PaxDbiP0A7Q1.
PRIDEiP0A7Q1.

Interactioni

Protein-protein interaction databases

BioGridi4262931. 15 interactors.
IntActiP0A7Q1. 4 interactors.
STRINGi511145.b1717.

Structurei

Secondary structure

165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 13Combined sources6
Beta strandi14 – 16Combined sources3
Beta strandi18 – 20Combined sources3
Beta strandi22 – 24Combined sources3
Beta strandi30 – 32Combined sources3
Helixi33 – 35Combined sources3
Helixi38 – 42Combined sources5
Beta strandi45 – 49Combined sources5
Helixi52 – 54Combined sources3
Helixi55 – 60Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0032-65[»]
2RDOelectron microscopy9.1032-65[»]
3BBXelectron microscopy10.0032-65[»]
3J5Lelectron microscopy6.6032-65[»]
3J7Zelectron microscopy3.9031-65[»]
3J8Gelectron microscopy5.0071-65[»]
3J9Yelectron microscopy3.9031-65[»]
3J9Zelectron microscopy3.60L42-65[»]
3JA1electron microscopy3.60L62-65[»]
3JBUelectron microscopy3.6471-65[»]
3JBVelectron microscopy3.3271-65[»]
3JCDelectron microscopy3.7032-65[»]
3JCEelectron microscopy3.2031-65[»]
3JCJelectron microscopy3.70c1-65[»]
3JCNelectron microscopy4.6031-65[»]
4CSUelectron microscopy5.5072-65[»]
4U1UX-ray2.95B3/D32-65[»]
4U1VX-ray3.00B3/D32-65[»]
4U20X-ray2.90B3/D32-65[»]
4U24X-ray2.90B3/D32-65[»]
4U25X-ray2.90B3/D32-65[»]
4U26X-ray2.80B3/D32-65[»]
4U27X-ray2.80B3/D32-65[»]
4UY8electron microscopy3.8032-65[»]
4V4HX-ray3.46B3/D31-65[»]
4V4QX-ray3.46B3/D32-65[»]
4V50X-ray3.22B3/D32-65[»]
4V52X-ray3.21B3/D32-65[»]
4V53X-ray3.54B3/D32-65[»]
4V54X-ray3.30B3/D32-65[»]
4V55X-ray4.00B3/D32-65[»]
4V56X-ray3.93B3/D32-65[»]
4V57X-ray3.50B3/D32-65[»]
4V5BX-ray3.74A3/C32-65[»]
4V5Helectron microscopy5.80B72-65[»]
4V5YX-ray4.45B3/D32-65[»]
4V64X-ray3.50B3/D32-65[»]
4V65electron microscopy9.00BW2-65[»]
4V66electron microscopy9.00BW2-65[»]
4V69electron microscopy6.70B32-65[»]
4V6CX-ray3.19B3/D31-65[»]
4V6DX-ray3.81B3/D31-65[»]
4V6EX-ray3.71B3/D31-65[»]
4V6Kelectron microscopy8.25Af1-65[»]
4V6Lelectron microscopy13.20Bf1-65[»]
4V6Melectron microscopy7.10B32-65[»]
4V6Nelectron microscopy12.10A62-65[»]
4V6Oelectron microscopy14.70B62-65[»]
4V6Pelectron microscopy13.50B62-65[»]
4V6Qelectron microscopy11.50B62-65[»]
4V6Relectron microscopy11.50B62-65[»]
4V6Selectron microscopy13.10A62-65[»]
4V6Telectron microscopy8.30B32-65[»]
4V6Velectron microscopy9.80B82-65[»]
4V6Yelectron microscopy12.00B31-65[»]
4V6Zelectron microscopy12.00B31-65[»]
4V70electron microscopy17.00B31-65[»]
4V71electron microscopy20.00B31-65[»]
4V72electron microscopy13.00B31-65[»]
4V73electron microscopy15.00B31-65[»]
4V74electron microscopy17.00B31-65[»]
4V75electron microscopy12.00B31-65[»]
4V76electron microscopy17.00B31-65[»]
4V77electron microscopy17.00B31-65[»]
4V78electron microscopy20.00B31-65[»]
4V79electron microscopy15.00B31-65[»]
4V7Aelectron microscopy9.00B31-65[»]
4V7Belectron microscopy6.80B31-65[»]
4V7Celectron microscopy7.60B62-65[»]
4V7Delectron microscopy7.60A72-65[»]
4V7Ielectron microscopy9.60A31-65[»]
4V7SX-ray3.25B3/D32-65[»]
4V7TX-ray3.19B3/D32-65[»]
4V7UX-ray3.10B3/D32-65[»]
4V7VX-ray3.29B3/D32-65[»]
4V85X-ray3.2071-65[»]
4V89X-ray3.70B71-65[»]
4V9CX-ray3.30B3/D31-65[»]
4V9DX-ray3.00C3/D32-65[»]
4V9OX-ray2.90A3/C3/E3/G31-65[»]
4V9PX-ray2.90A3/C3/E3/G31-65[»]
4WF1X-ray3.09B3/D32-65[»]
4WOIX-ray3.00B3/C31-65[»]
4WWWX-ray3.10R3/Y32-65[»]
4YBBX-ray2.10C4/D42-65[»]
5ADYelectron microscopy4.5031-65[»]
5AFIelectron microscopy2.9031-65[»]
5AKAelectron microscopy5.7032-65[»]
5GADelectron microscopy3.70e1-65[»]
5GAEelectron microscopy3.33e1-65[»]
5GAFelectron microscopy4.30e2-65[»]
5GAGelectron microscopy3.80e1-65[»]
5GAHelectron microscopy3.80e1-65[»]
5IQRelectron microscopy3.00e1-65[»]
5IT8X-ray3.12C4/D42-65[»]
5J5BX-ray2.80C4/D42-65[»]
5J7LX-ray3.00C4/D42-65[»]
5J88X-ray3.32C4/D42-65[»]
5J8AX-ray3.10C4/D42-65[»]
5J91X-ray2.96C4/D42-65[»]
5JC9X-ray3.03C4/D42-65[»]
5JTEelectron microscopy3.60B31-65[»]
5JU8electron microscopy3.60B31-65[»]
5KCRelectron microscopy3.60181-65[»]
5KCSelectron microscopy3.90181-65[»]
5KPSelectron microscopy3.9051-65[»]
5KPVelectron microscopy4.1041-65[»]
5KPWelectron microscopy3.9041-65[»]
5KPXelectron microscopy3.9041-65[»]
5L3Pelectron microscopy3.7081-65[»]
ProteinModelPortaliP0A7Q1.
SMRiP0A7Q1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Q1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L35P family.Curated

Phylogenomic databases

eggNOGiCOG0291. LUCA.
HOGENOMiHOG000040108.
InParanoidiP0A7Q1.
KOiK02916.
OMAiFKCKQSH.

Family and domain databases

HAMAPiMF_00514. Ribosomal_L35. 1 hit.
InterProiIPR021137. Ribosomal_L35.
IPR018265. Ribosomal_L35_CS.
IPR001706. Ribosomal_L35_non-mt.
[Graphical view]
PfamiPF01632. Ribosomal_L35p. 1 hit.
[Graphical view]
PRINTSiPR00064. RIBOSOMALL35.
TIGRFAMsiTIGR00001. rpmI_bact. 1 hit.
PROSITEiPS00936. RIBOSOMAL_L35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKIKTVRGA AKRFKKTGKG GFKHKHANLR HILTKKATKR KRHLRPKAMV
60
SKGDLGLVIA CLPYA
Length:65
Mass (Da):7,289
Last modified:January 23, 2007 - v2
Checksum:i98A72C0AD6CE0A07
GO

Sequence cautioni

The sequence V00291 differs from that shown. Reason: Frameshift at position 6.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11A → G AA sequence (PubMed:3298224).Curated1
Sequence conflicti11A → S (PubMed:6325158).Curated1
Sequence conflicti28N → D AA sequence (PubMed:3542048).Curated1

Mass spectrometryi

Molecular mass is 7158.0 Da from positions 2 - 65. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74787.1.
AP009048 Genomic DNA. Translation: BAA15484.1.
PIRiE64930. R5EC35.
RefSeqiNP_416232.3. NC_000913.3.
WP_001124225.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneIDi5552405.
946349.
KEGGiecj:JW1707.
eco:b1717.
PATRICi32118738. VBIEscCol129921_1787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74787.1.
AP009048 Genomic DNA. Translation: BAA15484.1.
PIRiE64930. R5EC35.
RefSeqiNP_416232.3. NC_000913.3.
WP_001124225.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0032-65[»]
2RDOelectron microscopy9.1032-65[»]
3BBXelectron microscopy10.0032-65[»]
3J5Lelectron microscopy6.6032-65[»]
3J7Zelectron microscopy3.9031-65[»]
3J8Gelectron microscopy5.0071-65[»]
3J9Yelectron microscopy3.9031-65[»]
3J9Zelectron microscopy3.60L42-65[»]
3JA1electron microscopy3.60L62-65[»]
3JBUelectron microscopy3.6471-65[»]
3JBVelectron microscopy3.3271-65[»]
3JCDelectron microscopy3.7032-65[»]
3JCEelectron microscopy3.2031-65[»]
3JCJelectron microscopy3.70c1-65[»]
3JCNelectron microscopy4.6031-65[»]
4CSUelectron microscopy5.5072-65[»]
4U1UX-ray2.95B3/D32-65[»]
4U1VX-ray3.00B3/D32-65[»]
4U20X-ray2.90B3/D32-65[»]
4U24X-ray2.90B3/D32-65[»]
4U25X-ray2.90B3/D32-65[»]
4U26X-ray2.80B3/D32-65[»]
4U27X-ray2.80B3/D32-65[»]
4UY8electron microscopy3.8032-65[»]
4V4HX-ray3.46B3/D31-65[»]
4V4QX-ray3.46B3/D32-65[»]
4V50X-ray3.22B3/D32-65[»]
4V52X-ray3.21B3/D32-65[»]
4V53X-ray3.54B3/D32-65[»]
4V54X-ray3.30B3/D32-65[»]
4V55X-ray4.00B3/D32-65[»]
4V56X-ray3.93B3/D32-65[»]
4V57X-ray3.50B3/D32-65[»]
4V5BX-ray3.74A3/C32-65[»]
4V5Helectron microscopy5.80B72-65[»]
4V5YX-ray4.45B3/D32-65[»]
4V64X-ray3.50B3/D32-65[»]
4V65electron microscopy9.00BW2-65[»]
4V66electron microscopy9.00BW2-65[»]
4V69electron microscopy6.70B32-65[»]
4V6CX-ray3.19B3/D31-65[»]
4V6DX-ray3.81B3/D31-65[»]
4V6EX-ray3.71B3/D31-65[»]
4V6Kelectron microscopy8.25Af1-65[»]
4V6Lelectron microscopy13.20Bf1-65[»]
4V6Melectron microscopy7.10B32-65[»]
4V6Nelectron microscopy12.10A62-65[»]
4V6Oelectron microscopy14.70B62-65[»]
4V6Pelectron microscopy13.50B62-65[»]
4V6Qelectron microscopy11.50B62-65[»]
4V6Relectron microscopy11.50B62-65[»]
4V6Selectron microscopy13.10A62-65[»]
4V6Telectron microscopy8.30B32-65[»]
4V6Velectron microscopy9.80B82-65[»]
4V6Yelectron microscopy12.00B31-65[»]
4V6Zelectron microscopy12.00B31-65[»]
4V70electron microscopy17.00B31-65[»]
4V71electron microscopy20.00B31-65[»]
4V72electron microscopy13.00B31-65[»]
4V73electron microscopy15.00B31-65[»]
4V74electron microscopy17.00B31-65[»]
4V75electron microscopy12.00B31-65[»]
4V76electron microscopy17.00B31-65[»]
4V77electron microscopy17.00B31-65[»]
4V78electron microscopy20.00B31-65[»]
4V79electron microscopy15.00B31-65[»]
4V7Aelectron microscopy9.00B31-65[»]
4V7Belectron microscopy6.80B31-65[»]
4V7Celectron microscopy7.60B62-65[»]
4V7Delectron microscopy7.60A72-65[»]
4V7Ielectron microscopy9.60A31-65[»]
4V7SX-ray3.25B3/D32-65[»]
4V7TX-ray3.19B3/D32-65[»]
4V7UX-ray3.10B3/D32-65[»]
4V7VX-ray3.29B3/D32-65[»]
4V85X-ray3.2071-65[»]
4V89X-ray3.70B71-65[»]
4V9CX-ray3.30B3/D31-65[»]
4V9DX-ray3.00C3/D32-65[»]
4V9OX-ray2.90A3/C3/E3/G31-65[»]
4V9PX-ray2.90A3/C3/E3/G31-65[»]
4WF1X-ray3.09B3/D32-65[»]
4WOIX-ray3.00B3/C31-65[»]
4WWWX-ray3.10R3/Y32-65[»]
4YBBX-ray2.10C4/D42-65[»]
5ADYelectron microscopy4.5031-65[»]
5AFIelectron microscopy2.9031-65[»]
5AKAelectron microscopy5.7032-65[»]
5GADelectron microscopy3.70e1-65[»]
5GAEelectron microscopy3.33e1-65[»]
5GAFelectron microscopy4.30e2-65[»]
5GAGelectron microscopy3.80e1-65[»]
5GAHelectron microscopy3.80e1-65[»]
5IQRelectron microscopy3.00e1-65[»]
5IT8X-ray3.12C4/D42-65[»]
5J5BX-ray2.80C4/D42-65[»]
5J7LX-ray3.00C4/D42-65[»]
5J88X-ray3.32C4/D42-65[»]
5J8AX-ray3.10C4/D42-65[»]
5J91X-ray2.96C4/D42-65[»]
5JC9X-ray3.03C4/D42-65[»]
5JTEelectron microscopy3.60B31-65[»]
5JU8electron microscopy3.60B31-65[»]
5KCRelectron microscopy3.60181-65[»]
5KCSelectron microscopy3.90181-65[»]
5KPSelectron microscopy3.9051-65[»]
5KPVelectron microscopy4.1041-65[»]
5KPWelectron microscopy3.9041-65[»]
5KPXelectron microscopy3.9041-65[»]
5L3Pelectron microscopy3.7081-65[»]
ProteinModelPortaliP0A7Q1.
SMRiP0A7Q1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262931. 15 interactors.
IntActiP0A7Q1. 4 interactors.
STRINGi511145.b1717.

Proteomic databases

EPDiP0A7Q1.
PaxDbiP0A7Q1.
PRIDEiP0A7Q1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneIDi5552405.
946349.
KEGGiecj:JW1707.
eco:b1717.
PATRICi32118738. VBIEscCol129921_1787.

Organism-specific databases

EchoBASEiEB1213.
EcoGeneiEG11231. rpmI.

Phylogenomic databases

eggNOGiCOG0291. LUCA.
HOGENOMiHOG000040108.
InParanoidiP0A7Q1.
KOiK02916.
OMAiFKCKQSH.

Enzyme and pathway databases

BioCyciEcoCyc:EG11231-MONOMER.
ECOL316407:JW1707-MONOMER.
MetaCyc:EG11231-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7Q1.
PROiP0A7Q1.

Family and domain databases

HAMAPiMF_00514. Ribosomal_L35. 1 hit.
InterProiIPR021137. Ribosomal_L35.
IPR018265. Ribosomal_L35_CS.
IPR001706. Ribosomal_L35_non-mt.
[Graphical view]
PfamiPF01632. Ribosomal_L35p. 1 hit.
[Graphical view]
PRINTSiPR00064. RIBOSOMALL35.
TIGRFAMsiTIGR00001. rpmI_bact. 1 hit.
PROSITEiPS00936. RIBOSOMAL_L35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL35_ECOLI
AccessioniPrimary (citable) accession number: P0A7Q1
Secondary accession number(s): P07085, P78275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 111 of the entry and version 2 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

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.