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P0A7Q1 (RL35_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L35
Alternative name(s):
Ribosomal protein A
Gene names
Name:rpmI
Ordered Locus Names:b1717, JW1707
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length65 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L35P family.

Mass spectrometry

Molecular mass is 7158.0 Da from positions 2 - 65. Determined by MALDI. Ref.7

Sequence caution

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 656450S ribosomal protein L35 HAMAP-Rule MF_00514
PRO_0000177359

Experimental info

Sequence conflict111A → G AA sequence Ref.6
Sequence conflict111A → S Ref.1
Sequence conflict281N → D AA sequence Ref.5

Secondary structure

.................... 65
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7Q1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 98A72C0AD6CE0A07

FASTA657,289
        10         20         30         40         50         60 
MPKIKTVRGA AKRFKKTGKG GFKHKHANLR HILTKKATKR KRHLRPKAMV SKGDLGLVIA 


CLPYA 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00291 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC74787.1.
AP009048 Genomic DNA. Translation: BAA15484.1.
PIRR5EC35. E64930.
RefSeqNP_416232.3. NC_000913.3.
YP_489979.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
ProteinModelPortalP0A7Q1.
SMRP0A7Q1. Positions 2-65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A7Q1. 4 interactions.
STRING511145.b1717.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7Q1.
PRIDEP0A7Q1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74787; AAC74787; b1717.
BAA15484; BAA15484; BAA15484.
GeneID12933937.
946349.
KEGGecj:Y75_p1692.
eco:b1717.
PATRIC32118738. VBIEscCol129921_1787.

Organism-specific databases

EchoBASEEB1213.
EcoGeneEG11231. rpmI.

Phylogenomic databases

eggNOGCOG0291.
HOGENOMHOG000040108.
KOK02916.
OMASHHNHIL.
OrthoDBEOG651T3B.

Enzyme and pathway databases

BioCycEcoCyc:EG11231-MONOMER.
ECOL316407:JW1707-MONOMER.

Gene expression databases

GenevestigatorP0A7Q1.

Family and domain databases

HAMAPMF_00514. Ribosomal_L35.
InterProIPR021137. Ribosomal_L35.
IPR018265. Ribosomal_L35_CS.
IPR001706. Ribosomal_L35_non-mt.
[Graphical view]
PfamPF01632. Ribosomal_L35p. 1 hit.
[Graphical view]
PRINTSPR00064. RIBOSOMALL35.
TIGRFAMsTIGR00001. rpmI_bact. 1 hit.
PROSITEPS00936. RIBOSOMAL_L35. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7Q1.
PROP0A7Q1.

Entry information

Entry nameRL35_ECOLI
AccessionPrimary (citable) accession number: P0A7Q1
Secondary accession number(s): P07085, P78275
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene