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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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 656450S ribosomal protein L35PRO_0000177359Add
BLAST

Proteomic databases

PaxDbiP0A7Q1.
PRIDEiP0A7Q1.

Interactioni

Protein-protein interaction databases

IntActiP0A7Q1. 4 interactions.
STRINGi511145.b1717.

Structurei

Secondary structure

1
65
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 136Combined sources
Beta strandi14 – 163Combined sources
Beta strandi18 – 203Combined sources
Beta strandi22 – 243Combined sources
Beta strandi30 – 323Combined sources
Helixi33 – 353Combined sources
Helixi38 – 425Combined sources
Beta strandi45 – 495Combined sources
Helixi52 – 543Combined sources
Helixi55 – 606Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0032-65[»]
2RDOelectron microscopy9.1032-65[»]
3BBXelectron microscopy10.0032-65[»]
3J5Lelectron microscopy6.6032-65[»]
3J7Zelectron microscopy3.9031-65[»]
3J9Yelectron microscopy3.9031-65[»]
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 microscopy9.8082-65[»]
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[»]
4WWWX-ray3.10R3/Y32-65[»]
4YBBX-ray2.10C4/D42-65[»]
5AFIelectron microscopy2.9031-65[»]
5AKAelectron microscopy5.7032-65[»]
ProteinModelPortaliP0A7Q1.
SMRiP0A7Q1. Positions 2-65.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7Q1.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L35P family.Curated

Phylogenomic databases

eggNOGiCOG0291.
HOGENOMiHOG000040108.
InParanoidiP0A7Q1.
KOiK02916.
OMAiRFKRTAS.
OrthoDBiEOG651T3B.

Family and domain databases

HAMAPiMF_00514. Ribosomal_L35.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → G AA sequence (PubMed:3298224).Curated
Sequence conflicti11 – 111A → S (PubMed:6325158).Curated
Sequence conflicti28 – 281N → D AA sequence (PubMed:3542048).Curated

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.

Genome annotation databases

EnsemblBacteriaiAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneIDi946349.
KEGGiecj:Y75_p1692.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.0032-65[»]
2RDOelectron microscopy9.1032-65[»]
3BBXelectron microscopy10.0032-65[»]
3J5Lelectron microscopy6.6032-65[»]
3J7Zelectron microscopy3.9031-65[»]
3J9Yelectron microscopy3.9031-65[»]
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 microscopy9.8082-65[»]
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[»]
4WWWX-ray3.10R3/Y32-65[»]
4YBBX-ray2.10C4/D42-65[»]
5AFIelectron microscopy2.9031-65[»]
5AKAelectron microscopy5.7032-65[»]
ProteinModelPortaliP0A7Q1.
SMRiP0A7Q1. Positions 2-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A7Q1. 4 interactions.
STRINGi511145.b1717.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7Q1.
PRIDEiP0A7Q1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneIDi946349.
KEGGiecj:Y75_p1692.
eco:b1717.
PATRICi32118738. VBIEscCol129921_1787.

Organism-specific databases

EchoBASEiEB1213.
EcoGeneiEG11231. rpmI.

Phylogenomic databases

eggNOGiCOG0291.
HOGENOMiHOG000040108.
InParanoidiP0A7Q1.
KOiK02916.
OMAiRFKRTAS.
OrthoDBiEOG651T3B.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7Q1.
PROiP0A7Q1.

Family and domain databases

HAMAPiMF_00514. Ribosomal_L35.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon."
    Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J.A., Grunberg-Manago M., Blanquet S.
    EMBO J. 1:311-315(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity."
    Kashiwagi K., Igarashi K.
    Biochim. Biophys. Acta 911:180-190(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-42.
  6. "Primary structures of and genes for new ribosomal proteins A and B in Escherichia coli."
    Wada A., Sako T.
    J. Biochem. 101:817-820(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
  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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  9. "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 2-65 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

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: June 24, 2015
This is version 98 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

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.