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P0A7L8 (RL27_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 93. 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 L27
Gene names
Name:rpmA
Ordered Locus Names:b3185, JW3152
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length85 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Part of the 50S ribosomal subunit, cross-links to the 23S rRNA. Cross-links to the A and P site tRNAs.

Sequence similarities

Belongs to the ribosomal protein L27P family.

Mass spectrometry

Molecular mass is 8993.5 Da from positions 2 - 85. Determined by MALDI. Ref.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 858450S ribosomal protein L27 HAMAP-Rule MF_00539
PRO_0000181085

Secondary structure

............... 85
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7L8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B43AAE180ABC23EA

FASTA859,124
        10         20         30         40         50         60 
MAHKKAGGST RNGRDSEAKR LGVKRFGGES VLAGSIIVRQ RGTKFHAGAN VGCGRDHTLF 

        70         80 
AKADGKVKFE VKGPKNRKFI SIEAE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli."
Jeong J.H., Kitakawa M.S., Isono S., Isono K.
DNA Seq. 4:59-67(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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.
[3]"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.
[4]"The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes."
Chen R., Mende L., Arfsten U.
FEBS Lett. 59:96-99(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-85.
Strain: K12.
[5]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 67-78, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[6]"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
Wower I., Wower J., Meinke M., Brimacombe R.
Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO 23S RRNA.
Strain: MRE-600.
[7]"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
Osswald M., Doering T., Brimacombe R.
Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
Strain: MRE-600.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"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.
[10]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[11]"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
D13267 Genomic DNA. Translation: BAA02526.1.
U18997 Genomic DNA. Translation: AAA57986.1.
U00096 Genomic DNA. Translation: AAC76217.1.
AP009048 Genomic DNA. Translation: BAE77229.1.
PIRR5EC27. JS0767.
RefSeqNP_417652.1. NC_000913.3.
YP_491370.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30U2-85[»]
1P86electron microscopy11.50U2-85[»]
1VS6X-ray3.46W1-85[»]
1VS8X-ray3.46W1-85[»]
1VT2X-ray3.30W1-85[»]
2AW4X-ray3.46W2-85[»]
2AWBX-ray3.46W2-85[»]
2GYAelectron microscopy15.00U2-84[»]
2GYCelectron microscopy15.00U2-85[»]
2I2TX-ray3.22W2-84[»]
2I2VX-ray3.22W2-84[»]
2J28electron microscopy8.00W2-85[»]
2QAMX-ray3.21W2-85[»]
2QAOX-ray3.21W2-85[»]
2QBAX-ray3.54W2-85[»]
2QBCX-ray3.54W2-85[»]
2QBEX-ray3.30W2-85[»]
2QBGX-ray3.30W2-85[»]
2QBIX-ray4.00W2-85[»]
2QBKX-ray4.00W2-85[»]
2QOVX-ray3.93W2-85[»]
2QOXX-ray3.93W2-85[»]
2QOZX-ray3.50W2-85[»]
2QP1X-ray3.50W2-85[»]
2RDOelectron microscopy9.10W2-85[»]
2VHMX-ray3.74W2-85[»]
2VHNX-ray3.74W2-85[»]
2WWQelectron microscopy5.80Y7-85[»]
2Z4LX-ray4.45W2-85[»]
2Z4NX-ray4.45W2-85[»]
3BBXelectron microscopy10.00W2-85[»]
3DF2X-ray3.50W2-84[»]
3DF4X-ray3.50W2-84[»]
3E1Belectron microscopy-P1-85[»]
3E1Delectron microscopy-P1-85[»]
3FIKelectron microscopy6.70W7-85[»]
3I1NX-ray3.19W1-85[»]
3I1PX-ray3.19W1-85[»]
3I1RX-ray3.81W1-85[»]
3I1TX-ray3.81W1-85[»]
3I20X-ray3.71W1-85[»]
3I22X-ray3.71W1-85[»]
3IZTelectron microscopy-X1-85[»]
3IZUelectron microscopy-X1-85[»]
3J01electron microscopy-W2-85[»]
3J0Telectron microscopy12.10Y2-84[»]
3J0Welectron microscopy14.70Y2-84[»]
3J0Yelectron microscopy13.50Y2-84[»]
3J11electron microscopy13.10Y2-84[»]
3J12electron microscopy11.50Y2-84[»]
3J14electron microscopy11.50Y2-84[»]
3J19electron microscopy8.30W10-85[»]
3J37electron microscopy9.8002-85[»]
3J4Xelectron microscopy12.00W7-85[»]
3J50electron microscopy20.00W7-85[»]
3J51electron microscopy17.00W7-85[»]
3J52electron microscopy12.00W7-85[»]
3J54electron microscopy13.00W7-85[»]
3J56electron microscopy15.00W7-85[»]
3J58electron microscopy17.00W7-85[»]
3J5Aelectron microscopy12.00W7-85[»]
3J5Celectron microscopy17.00W7-85[»]
3J5Eelectron microscopy17.00W7-85[»]
3J5Gelectron microscopy20.00W7-85[»]
3J5Ielectron microscopy15.00W7-85[»]
3J5Kelectron microscopy9.00W7-85[»]
3J5Oelectron microscopy6.80W1-85[»]
3J5Uelectron microscopy7.60Y2-85[»]
3J5Welectron microscopy7.60Z2-85[»]
3KCRelectron microscopy-W1-85[»]
3OASX-ray3.25W7-85[»]
3OATX-ray3.25W7-85[»]
3OFCX-ray3.19W7-85[»]
3OFDX-ray3.19W7-85[»]
3OFQX-ray3.10W7-85[»]
3OFRX-ray3.10W7-85[»]
3OFZX-ray3.29W7-85[»]
3OG0X-ray3.29W7-85[»]
3ORBX-ray3.30W1-85[»]
3R8SX-ray3.00W10-85[»]
3R8TX-ray3.00W11-85[»]
3SGFX-ray3.2001-85[»]
3UOSX-ray3.7001-85[»]
4GARX-ray3.30W1-85[»]
4GAUX-ray3.30W1-85[»]
4KIXX-ray2.90W1-85[»]
4KIZX-ray2.90W1-85[»]
4KJ1X-ray2.90W1-85[»]
4KJ3X-ray2.90W1-85[»]
4KJ5X-ray2.90W1-85[»]
4KJ7X-ray2.90W1-85[»]
4KJ9X-ray2.90W1-85[»]
4KJBX-ray2.90W1-85[»]
DisProtDP00140.
ProteinModelPortalP0A7L8.
SMRP0A7L8. Positions 2-85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid849576. 1 interaction.
DIPDIP-47933N.
IntActP0A7L8. 23 interactions.
MINTMINT-1317488.
STRING511145.b3185.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7L8.
PRIDEP0A7L8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76217; AAC76217; b3185.
BAE77229; BAE77229; BAE77229.
GeneID12932199.
945190.
KEGGecj:Y75_p3105.
eco:b3185.
PATRIC32121790. VBIEscCol129921_3279.

Organism-specific databases

EchoBASEEB4296.
EcoGeneEG50002. rpmA.

Phylogenomic databases

eggNOGCOG0211.
HOGENOMHOG000111610.
KOK02899.
OMAKDHTLHA.
OrthoDBEOG6N94H6.
ProtClustDBPRK05435.

Enzyme and pathway databases

BioCycEcoCyc:EG50002-MONOMER.
ECOL316407:JW3152-MONOMER.

Gene expression databases

GenevestigatorP0A7L8.

Family and domain databases

HAMAPMF_00539. Ribosomal_L27.
InterProIPR001684. Ribosomal_L27.
IPR018261. Ribosomal_L27_CS.
[Graphical view]
PANTHERPTHR15893. PTHR15893. 1 hit.
PfamPF01016. Ribosomal_L27. 1 hit.
[Graphical view]
PRINTSPR00063. RIBOSOMALL27.
ProDomPD003114. Ribosomal_L27. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00062. L27. 1 hit.
PROSITEPS00831. RIBOSOMAL_L27. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7L8.
PROP0A7L8.

Entry information

Entry nameRL27_ECOLI
AccessionPrimary (citable) accession number: P0A7L8
Secondary accession number(s): P02427, Q2M927
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 93 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