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P0A7Q1

- RL35_ECOLI

UniProt

P0A7Q1 - RL35_ECOLI

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Protein
50S ribosomal protein L35
Gene
rpmI, b1717, JW1707
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: EcoCyc

GO - Biological processi

  1. translation Source: InterPro
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11231. rpmI.

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
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 656450S ribosomal protein L35UniRule annotation
PRO_0000177359Add
BLAST

Proteomic databases

PaxDbiP0A7Q1.
PRIDEiP0A7Q1.

Expressioni

Gene expression databases

GenevestigatoriP0A7Q1.

Interactioni

Protein-protein interaction databases

IntActiP0A7Q1. 4 interactions.
STRINGi511145.b1717.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114
Beta strandi14 – 163
Beta strandi18 – 203
Beta strandi22 – 254
Beta strandi30 – 323
Beta strandi34 – 363
Helixi38 – 436
Beta strandi45 – 495
Turni52 – 543
Helixi55 – 617

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.4631-65[»]
1VS8X-ray3.4631-65[»]
1VT2X-ray3.3031-65[»]
2AW4X-ray3.4632-65[»]
2AWBX-ray3.4632-65[»]
2I2TX-ray3.2232-65[»]
2I2VX-ray3.2232-65[»]
2J28electron microscopy8.0032-65[»]
2QAMX-ray3.2132-65[»]
2QAOX-ray3.2132-65[»]
2QBAX-ray3.5432-65[»]
2QBCX-ray3.5432-65[»]
2QBEX-ray3.3032-65[»]
2QBGX-ray3.3032-65[»]
2QBIX-ray4.0032-65[»]
2QBKX-ray4.0032-65[»]
2QOVX-ray3.9332-65[»]
2QOXX-ray3.9332-65[»]
2QOZX-ray3.5032-65[»]
2QP1X-ray3.5032-65[»]
2RDOelectron microscopy9.1032-65[»]
2VHMX-ray3.7432-65[»]
2VHNX-ray3.7432-65[»]
2WWQelectron microscopy5.8072-65[»]
2Z4LX-ray4.4532-65[»]
2Z4NX-ray4.4532-65[»]
3BBXelectron microscopy10.0032-65[»]
3DF2X-ray3.5032-64[»]
3DF4X-ray3.5032-64[»]
3E1Belectron microscopy-W2-65[»]
3E1Delectron microscopy-W2-65[»]
3FIKelectron microscopy6.7032-65[»]
3I1NX-ray3.1931-65[»]
3I1PX-ray3.1931-65[»]
3I1RX-ray3.8131-65[»]
3I1TX-ray3.8131-65[»]
3I20X-ray3.7131-65[»]
3I22X-ray3.7131-65[»]
3IZTelectron microscopy-f1-65[»]
3IZUelectron microscopy-f1-65[»]
3J01electron microscopy-32-65[»]
3J0Telectron microscopy12.1062-65[»]
3J0Welectron microscopy14.7062-65[»]
3J0Yelectron microscopy13.5062-65[»]
3J11electron microscopy13.1062-65[»]
3J12electron microscopy11.5062-65[»]
3J14electron microscopy11.5062-65[»]
3J19electron microscopy8.3032-65[»]
3J37electron microscopy9.8082-65[»]
3J4Xelectron microscopy12.0031-65[»]
3J50electron microscopy20.0031-65[»]
3J51electron microscopy17.0031-65[»]
3J52electron microscopy12.0031-65[»]
3J54electron microscopy13.0031-65[»]
3J56electron microscopy15.0031-65[»]
3J58electron microscopy17.0031-65[»]
3J5Aelectron microscopy12.0031-65[»]
3J5Celectron microscopy17.0031-65[»]
3J5Eelectron microscopy17.0031-65[»]
3J5Gelectron microscopy20.0031-65[»]
3J5Ielectron microscopy15.0031-65[»]
3J5Kelectron microscopy9.0031-65[»]
3J5Lelectron microscopy6.6032-65[»]
3J5Oelectron microscopy6.8031-65[»]
3J5Uelectron microscopy7.6062-65[»]
3J5Welectron microscopy7.6072-65[»]
3KCRelectron microscopy-31-65[»]
3OASX-ray3.2532-65[»]
3OATX-ray3.2532-65[»]
3OFCX-ray3.1932-65[»]
3OFDX-ray3.1932-65[»]
3OFQX-ray3.1032-65[»]
3OFRX-ray3.1032-65[»]
3OFZX-ray3.2932-65[»]
3OG0X-ray3.2932-65[»]
3ORBX-ray3.3031-65[»]
3R8SX-ray3.0032-65[»]
3R8TX-ray3.0032-65[»]
3SGFX-ray3.2071-65[»]
3UOSX-ray3.7071-65[»]
4CSUelectron microscopy5.5072-65[»]
4GARX-ray3.3031-65[»]
4GAUX-ray3.3031-65[»]
4KIXX-ray2.9031-65[»]
4KIZX-ray2.9031-65[»]
4KJ1X-ray2.9031-65[»]
4KJ3X-ray2.9031-65[»]
4KJ5X-ray2.9031-65[»]
4KJ7X-ray2.9031-65[»]
4KJ9X-ray2.9031-65[»]
4KJBX-ray2.9031-65[»]
ProteinModelPortaliP0A7Q1.
SMRiP0A7Q1. Positions 2-65.

Miscellaneous databases

EvolutionaryTraceiP0A7Q1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0291.
HOGENOMiHOG000040108.
KOiK02916.
OMAiSHHNHIL.
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

MPKIKTVRGA AKRFKKTGKG GFKHKHANLR HILTKKATKR KRHLRPKAMV   50
SKGDLGLVIA CLPYA 65
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.

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → G AA sequence 1 Publication
Sequence conflicti11 – 111A → S1 Publication
Sequence conflicti28 – 281N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489979.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneIDi12933937.
946349.
KEGGiecj:Y75_p1692.
eco:b1717.
PATRICi32118738. VBIEscCol129921_1787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00291 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74787.1 .
AP009048 Genomic DNA. Translation: BAA15484.1 .
PIRi E64930. R5EC35.
RefSeqi NP_416232.3. NC_000913.3.
YP_489979.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VS6 X-ray 3.46 3 1-65 [» ]
1VS8 X-ray 3.46 3 1-65 [» ]
1VT2 X-ray 3.30 3 1-65 [» ]
2AW4 X-ray 3.46 3 2-65 [» ]
2AWB X-ray 3.46 3 2-65 [» ]
2I2T X-ray 3.22 3 2-65 [» ]
2I2V X-ray 3.22 3 2-65 [» ]
2J28 electron microscopy 8.00 3 2-65 [» ]
2QAM X-ray 3.21 3 2-65 [» ]
2QAO X-ray 3.21 3 2-65 [» ]
2QBA X-ray 3.54 3 2-65 [» ]
2QBC X-ray 3.54 3 2-65 [» ]
2QBE X-ray 3.30 3 2-65 [» ]
2QBG X-ray 3.30 3 2-65 [» ]
2QBI X-ray 4.00 3 2-65 [» ]
2QBK X-ray 4.00 3 2-65 [» ]
2QOV X-ray 3.93 3 2-65 [» ]
2QOX X-ray 3.93 3 2-65 [» ]
2QOZ X-ray 3.50 3 2-65 [» ]
2QP1 X-ray 3.50 3 2-65 [» ]
2RDO electron microscopy 9.10 3 2-65 [» ]
2VHM X-ray 3.74 3 2-65 [» ]
2VHN X-ray 3.74 3 2-65 [» ]
2WWQ electron microscopy 5.80 7 2-65 [» ]
2Z4L X-ray 4.45 3 2-65 [» ]
2Z4N X-ray 4.45 3 2-65 [» ]
3BBX electron microscopy 10.00 3 2-65 [» ]
3DF2 X-ray 3.50 3 2-64 [» ]
3DF4 X-ray 3.50 3 2-64 [» ]
3E1B electron microscopy - W 2-65 [» ]
3E1D electron microscopy - W 2-65 [» ]
3FIK electron microscopy 6.70 3 2-65 [» ]
3I1N X-ray 3.19 3 1-65 [» ]
3I1P X-ray 3.19 3 1-65 [» ]
3I1R X-ray 3.81 3 1-65 [» ]
3I1T X-ray 3.81 3 1-65 [» ]
3I20 X-ray 3.71 3 1-65 [» ]
3I22 X-ray 3.71 3 1-65 [» ]
3IZT electron microscopy - f 1-65 [» ]
3IZU electron microscopy - f 1-65 [» ]
3J01 electron microscopy - 3 2-65 [» ]
3J0T electron microscopy 12.10 6 2-65 [» ]
3J0W electron microscopy 14.70 6 2-65 [» ]
3J0Y electron microscopy 13.50 6 2-65 [» ]
3J11 electron microscopy 13.10 6 2-65 [» ]
3J12 electron microscopy 11.50 6 2-65 [» ]
3J14 electron microscopy 11.50 6 2-65 [» ]
3J19 electron microscopy 8.30 3 2-65 [» ]
3J37 electron microscopy 9.80 8 2-65 [» ]
3J4X electron microscopy 12.00 3 1-65 [» ]
3J50 electron microscopy 20.00 3 1-65 [» ]
3J51 electron microscopy 17.00 3 1-65 [» ]
3J52 electron microscopy 12.00 3 1-65 [» ]
3J54 electron microscopy 13.00 3 1-65 [» ]
3J56 electron microscopy 15.00 3 1-65 [» ]
3J58 electron microscopy 17.00 3 1-65 [» ]
3J5A electron microscopy 12.00 3 1-65 [» ]
3J5C electron microscopy 17.00 3 1-65 [» ]
3J5E electron microscopy 17.00 3 1-65 [» ]
3J5G electron microscopy 20.00 3 1-65 [» ]
3J5I electron microscopy 15.00 3 1-65 [» ]
3J5K electron microscopy 9.00 3 1-65 [» ]
3J5L electron microscopy 6.60 3 2-65 [» ]
3J5O electron microscopy 6.80 3 1-65 [» ]
3J5U electron microscopy 7.60 6 2-65 [» ]
3J5W electron microscopy 7.60 7 2-65 [» ]
3KCR electron microscopy - 3 1-65 [» ]
3OAS X-ray 3.25 3 2-65 [» ]
3OAT X-ray 3.25 3 2-65 [» ]
3OFC X-ray 3.19 3 2-65 [» ]
3OFD X-ray 3.19 3 2-65 [» ]
3OFQ X-ray 3.10 3 2-65 [» ]
3OFR X-ray 3.10 3 2-65 [» ]
3OFZ X-ray 3.29 3 2-65 [» ]
3OG0 X-ray 3.29 3 2-65 [» ]
3ORB X-ray 3.30 3 1-65 [» ]
3R8S X-ray 3.00 3 2-65 [» ]
3R8T X-ray 3.00 3 2-65 [» ]
3SGF X-ray 3.20 7 1-65 [» ]
3UOS X-ray 3.70 7 1-65 [» ]
4CSU electron microscopy 5.50 7 2-65 [» ]
4GAR X-ray 3.30 3 1-65 [» ]
4GAU X-ray 3.30 3 1-65 [» ]
4KIX X-ray 2.90 3 1-65 [» ]
4KIZ X-ray 2.90 3 1-65 [» ]
4KJ1 X-ray 2.90 3 1-65 [» ]
4KJ3 X-ray 2.90 3 1-65 [» ]
4KJ5 X-ray 2.90 3 1-65 [» ]
4KJ7 X-ray 2.90 3 1-65 [» ]
4KJ9 X-ray 2.90 3 1-65 [» ]
4KJB X-ray 2.90 3 1-65 [» ]
ProteinModelPortali P0A7Q1.
SMRi P0A7Q1. Positions 2-65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A7Q1. 4 interactions.
STRINGi 511145.b1717.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7Q1.
PRIDEi P0A7Q1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74787 ; AAC74787 ; b1717 .
BAA15484 ; BAA15484 ; BAA15484 .
GeneIDi 12933937.
946349.
KEGGi ecj:Y75_p1692.
eco:b1717.
PATRICi 32118738. VBIEscCol129921_1787.

Organism-specific databases

EchoBASEi EB1213.
EcoGenei EG11231. rpmI.

Phylogenomic databases

eggNOGi COG0291.
HOGENOMi HOG000040108.
KOi K02916.
OMAi SHHNHIL.
OrthoDBi EOG651T3B.

Enzyme and pathway databases

BioCyci EcoCyc:EG11231-MONOMER.
ECOL316407:JW1707-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7Q1.
PROi P0A7Q1.

Gene expression databases

Genevestigatori P0A7Q1.

Family and domain databases

HAMAPi MF_00514. Ribosomal_L35.
InterProi IPR021137. Ribosomal_L35.
IPR018265. Ribosomal_L35_CS.
IPR001706. Ribosomal_L35_non-mt.
[Graphical view ]
Pfami PF01632. Ribosomal_L35p. 1 hit.
[Graphical view ]
PRINTSi PR00064. RIBOSOMALL35.
TIGRFAMsi TIGR00001. rpmI_bact. 1 hit.
PROSITEi PS00936. RIBOSOMAL_L35. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 88 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

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