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P0A7Q1 (RL35_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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
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)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosolic large ribosomal subunit

Inferred from direct assay Ref.6. Source: EcoCyc

   Molecular functionstructural constituent of ribosome

Inferred from direct assay Ref.6. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 656450S ribosomal protein L35 HAMAP 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

1 ....... 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: 6325158] [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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 3542048] [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: 3298224] [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: 10094780] [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: 16272117] [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_000913.2.

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-ray3.2232-64[»]
2I2VX-ray3.2232-64[»]
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[»]
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[»]
ProteinModelPortalP0A7Q1.
SMRP0A7Q1. Positions 2-65.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A7Q1. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000706; EBESCP00000000706; EBESCG00000000590.
EBESCT00000000707; EBESCP00000000707; EBESCG00000000590.
EBESCT00000000708; EBESCP00000000708; EBESCG00000000590.
EBESCT00000018199; EBESCP00000017490; EBESCG00000017254.
GeneID946349.
GenomeReviewsGene locus JW1707 in contig AP009048_GR.
Gene locus b1717 in contig U00096_GR.
KEGGecj:JW1707.
eco:b1717.
PATRIC32118738. VBIEscCol129921_1787.

Organism-specific databases

EchoBASEEB1213.
EcoGeneEG11231. rpmI.

Phylogenomic databases

eggNOGCOG0291.
GeneTreeEBGT00050000008998.
HOGENOMHBG734125.
OMAIKTNRGA.
PhylomeDBP0A7Q1.
ProtClustDBPRK00172.

Enzyme and pathway databases

BioCycEcoCyc:EG11231-MONOMER.

Gene expression databases

GenevestigatorP0A7Q1.

Family and domain databases

HAMAPMF_00514. Ribosomal_L35.
[Tree]
InterProIPR021137. Ribosomal_L35.
IPR018265. Ribosomal_L35_CS.
IPR001706. Ribosomal_L35_non-mt.
[Graphical view]
KOK02916.
PfamPF01632. Ribosomal_L35p. 1 hit.
[Graphical view]
PRINTSPR00064. RIBOSOMALL35.
TIGRFAMsTIGR00001. RpmI_bact. 1 hit.
PROSITEPS00936. RIBOSOMAL_L35. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents