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Reviewed, UniProtKB/Swiss-Prot P0A7K2 (RL7_ECOLI)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L7/L12
Alternative name(s):
    L8
Gene names
Name: rplL
Ordered Locus Names: b3986, JW3949
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation. HAMAP MF_00368

Subunit structure

Part of the 50S ribosomal subunit. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form a very strong complex (called L8). HAMAP MF_00368

Post-translational modification

Acetylation of Ser-2 converts L12 to L7. HAMAP MF_00368

Lys-82 was found to be 50% monomethylated. HAMAP MF_00368

Sequence similarities

Belongs to the ribosomal protein L12P family.

Mass spectrometry

Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated. Ref.12

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Chain2 – 12112050S ribosomal protein L7/L12 HAMAP MF_00368
PRO_0000157528

Amino acid modifications

Modified residue21N-acetylserine; in L7 HAMAP MF_00368
Modified residue821N6-methyllysine; partial HAMAP MF_00368

Experimental info

Sequence conflict61D → F AA sequence Ref.9

Secondary structure

................. 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7K2-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 08B051A0CDAA527E

FASTA12112,295
        10         20         30         40         50         60 
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE EKTEFDVILK 

        70         80         90        100        110        120 
AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS KDDAEALKKA LEEAGAEVEV 


K 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed: 377281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence determination in 3'-end proximalely labelled DNA."
Gurevich A.I., Avakov A.E.
Bioorg. Khim. 5:301-304(1979)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"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.
[6]"The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T."
Terhorst C., Moeller W., Laursen R., Wittmann-Liebold B.
Eur. J. Biochem. 34:138-152(1973) [PubMed: 4573678] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-121.
Strain: MRE-600.
[7]"The ribosomal protein L8 is a complex L7/L12 and L10."
Pettersson I., Hardy S.J.S., Liljas A.
FEBS Lett. 64:135-138(1976) [PubMed: 773698] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-121.
Strain: MRE-600.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[9]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed: 9868784] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[10]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]"The nucleotide sequence at the proximal end of rpoB gene of Escherichia coli."
Gurevich A.I., Avakov A.E., Kolosov M.N.
Bioorg. Khim. 5:1735-1739(1979)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-121.
[12]"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.
[13]"Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A."
Leijonmarck M., Liljas A.
J. Mol. Biol. 195:555-580(1987) [PubMed: 3309338] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[14]"Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution."
Bocharov E.V., Gudkov A.T., Arseniev A.S.
FEBS Lett. 379:291-294(1996) [PubMed: 8603708] [Abstract]
Cited for: STRUCTURE BY NMR.
[15]"Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10."
Bocharov E.V., Gudkov A.T., Budovskaya E.V., Arseniev A.S.
FEBS Lett. 423:347-350(1998) [PubMed: 9515737] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

V00339 Genomic DNA. Translation: CAA23624.1.
M38301 Genomic DNA. Translation: AAA24573.1.
U00006 Genomic DNA. Translation: AAC43084.1.
U00096 Genomic DNA. Translation: AAC76960.1.
AP009048 Genomic DNA. Translation: BAE77334.1.
PIRR5EC7. S12575.
RefSeqAP_003833.1.
NP_418413.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CTFX-ray1.70A48-121[»]
1RQSNMR-A48-120[»]
1RQTNMR-A/B2-37[»]
1RQUNMR-A/B2-120[»]
1RQVNMR-A/B2-120[»]
2BCWelectron microscopy-B54-120[»]
2GYAelectron microscopy-3/53-120[»]
2GYCelectron microscopy-3/53-121[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0A7K2. 124 interactions.

PTM databases

PhosSiteP0A7K2.

2-D gel databases

SWISS-2DPAGEP0A7K2.
ECO2DBASEA013.0. 6TH EDITION.
B013.0. 6TH EDITION.

Genome annotation databases

GeneID948489.
GenomeReviewsGene locus JW3949 in contig AP009048_GR.
Gene locus b3986 in contig U00096_GR.
KEGGecj:JW3949.
eco:b3986.

Organism-specific databases

EchoBASEEB0866.
EcoGeneEG10873. rplL.
CMRSearch...

Phylogenomic databases

HOGENOMP0A7K2.
OMAP0A7K2. KINVIKA.

Enzyme and pathway databases

BioCycEcoCyc:EG10873-MON.

Family and domain databases

HAMAPMF_00368.
[Tree]
InterProIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
[Graphical view]
Gene3DG3DSA:3.30.1390.10. Ribosomal_L7/12_C/ClpS-like. 1 hit.
PfamPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomPD001326. Ribosomal_L12. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00855. L12. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRL7_ECOLI
AccessionPrimary (citable) accession number: P0A7K2
Secondary accession number(s): P02392, Q2M8S2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents