UniProtKB - P0A7M6 (RL29_ECOLI)
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- BLAST>sp|P0A7M6|RL29_ECOLI 50S ribosomal protein L29 OS=Escherichia coli (strain K12) OX=83333 GN=rpmC PE=1 SV=1 MKAKELREKSVEELNTELLNLLREQFNLRMQAASGQLQQSHLLKQVRRDVARVKTLLNEK AGA
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Protein
50S ribosomal protein L29
Gene
rpmC
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Binds 23S rRNA. It is not essential for growth.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"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. - Ref.9"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract]Cited for: BINDING TO TRIGGER FACTOR, DISRUPTION PHENOTYPE.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666).1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract]Cited for: BINDING TO TRIGGER FACTOR, DISRUPTION PHENOTYPE.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- rRNA binding Source: UniProtKB-KW
- structural constituent of ribosome Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- ribosomal large subunit assembly Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- translation Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10887-MONOMER MetaCyc:EG10887-MONOMER |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 50S ribosomal protein L29Alternative name(s): Large ribosomal subunit protein uL291 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:rpmC Ordered Locus Names:b3312, JW3274 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG10887 rpmC |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- cytosolic large ribosomal subunit Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Cells missing both S17 and L29 grow very slowly and have a rather unstable temperature-sensitive phenotype.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surface."
Stoeffler-Meilicke M., Dabbs E.R., Albrecht-Ehrlich R., Stoeffler G.
Eur. J. Biochem. 150:485-490(1985) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF A STRAIN MISSING S17 AND L29. - Ref.9"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract]Cited for: BINDING TO TRIGGER FACTOR, DISRUPTION PHENOTYPE.
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000130384 | 1 – 63 | 50S ribosomal protein L29Add BLAST | 63 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0A7M6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A7M6 |
PRoteomics IDEntifications database More...PRIDEi | P0A7M6 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Part of the 50s ribosomal subunit (PubMed:1092361, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:21499241, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts protein L23 (PubMed:2665813), trigger factor (PubMed:12226666) and protein nascent chains (PubMed:12756233). Might also contact SecE and probably does contact SecG when the SecYEG translocation complex is docked with the ribosome (PubMed:16292303).1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.12"Structure of the E. coli protein-conducting channel bound to a translating ribosome."
Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"The primary structure of the ribosomal protein L29 from Escherichia coli."
Bitar K.G.
Biochim. Biophys. Acta 386:99-106(1975) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, SUBUNIT. - Ref.7"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]Cited for: CROSS-LINKING TO L23. - Ref.9"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract]Cited for: BINDING TO TRIGGER FACTOR, DISRUPTION PHENOTYPE. - Ref.10"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CROSS-LINKS TO NASCENT PROTEIN CHAINS. - Ref.11"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, SUBUNIT. - Ref.14"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), SUBUNIT. - Ref.15"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, SUBUNIT. - Ref.16"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment."
Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.
Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN, SUBUNIT. - Ref.17"Molecular basis for the ribosome functioning as an L-tryptophan sensor."
Bischoff L., Berninghausen O., Beckmann R.
Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S RIBOSOMAL SUBUNIT, SUBUNIT. - Ref.18"Structural and functional insights into the mode of action of a universally conserved Obg GTPase."
Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y., Zhang Y., Wang Z., Wu J., Sanyal S., Lei J., Gao N.
PLoS Biol. 12:E1001866-E1001866(2014) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL SUBUNIT IN COMPLEX WITH OBGE AND GMP-PNP, SUBUNIT. - Ref.19"Mechanistic insights into the alternative translation termination by ArfA and RF2."
Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.
Nature 541:550-553(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT. - Ref.20"Structural basis for ArfA-RF2-mediated translation termination on mRNAs lacking stop codons."
Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R., Wilson D.N.
Nature 541:546-549(2017) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT. - Ref.21"Translational termination without a stop codon."
James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.
Science 354:1437-1440(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2, SUBUNIT.
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-47911N |
Protein interaction database and analysis system More...IntActi | P0A7M6, 35 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3487 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 5 – 8 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 11 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 23 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 41 – 61 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A7M6 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A7M6 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0A7M6 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the universal ribosomal protein uL29 family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG41083MP Bacteria COG0255 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000248754 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0A7M6 |
KEGG Orthology (KO) More...KOi | K02904 |
Identification of Orthologs from Complete Genome Data More...OMAi | RFQNATN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0A7M6 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00374 Ribosomal_L29, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001854 Ribosomal_L29/L35 IPR036049 Ribosomal_L29/L35_sf IPR018254 Ribosomal_L29_CS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00831 Ribosomal_L29, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46561 SSF46561, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00012 L29, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00579 RIBOSOMAL_L29, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
P0A7M6-1 [UniParc]FASTAAdd to basketAdded to basketShow »
10 20 30 40 50
MKAKELREKS VEELNTELLN LLREQFNLRM QAASGQLQQS HLLKQVRRDV
60
ARVKTLLNEK AGA
Length:63
Mass (Da):7,273
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iDAEF8F126B0AA077
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence described in PubMed:1092361 differs from that shown. Exchange of two tryptic peptides.Curated
<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 7273.4 Da from positions 1 - 63. Determined by MALDI. 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"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, SUBUNIT.
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X02613 Genomic DNA Translation: CAA26468.1 U18997 Genomic DNA Translation: AAA58109.1 U00096 Genomic DNA Translation: AAC76337.1 AP009048 Genomic DNA Translation: BAE77979.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B37519 R5EC29 |
NCBI Reference Sequences More...RefSeqi | NP_417771.1, NC_000913.3 WP_000644741.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76337; AAC76337; b3312 BAE77979; BAE77979; BAE77979 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947807 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3274 eco:b3312 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3419 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A7M6 | 50S ribosomal protein L29 | 63 | |||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| +189 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0A7M6 | 50S ribosomal protein L29 | 63 | |||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| 50S ribosomal protein L29 | 63 | ||||
| +640 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X02613 Genomic DNA Translation: CAA26468.1 U18997 Genomic DNA Translation: AAA58109.1 U00096 Genomic DNA Translation: AAC76337.1 AP009048 Genomic DNA Translation: BAE77979.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B37519 R5EC29 |
NCBI Reference Sequences More...RefSeqi | NP_417771.1, NC_000913.3 WP_000644741.1, NZ_LN832404.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1ML5 | electron microscopy | 14.00 | w | 2-63 | [»] | |
| 2J28 | electron microscopy | 8.00 | X | 1-63 | [»] | |
| 2RDO | electron microscopy | 9.10 | X | 1-63 | [»] | |
| 2VRH | electron microscopy | 19.00 | D | 1-63 | [»] | |
| 3BBX | electron microscopy | 10.00 | X | 1-63 | [»] | |
| 3J45 | electron microscopy | 9.50 | Y | 1-63 | [»] | |
| 3J46 | electron microscopy | 10.10 | Y | 1-63 | [»] | |
| 3J5L | electron microscopy | 6.60 | Y | 1-63 | [»] | |
| 3J7Z | electron microscopy | 3.90 | Y | 1-63 | [»] | |
| 3J8G | electron microscopy | 5.00 | 1 | 1-63 | [»] | |
| 3J9Y | electron microscopy | 3.90 | Y | 1-63 | [»] | |
| 3J9Z | electron microscopy | 3.60 | LW | 1-63 | [»] | |
| 3JA1 | electron microscopy | 3.60 | L0 | 1-63 | [»] | |
| 3JBU | electron microscopy | 3.64 | 1 | 1-63 | [»] | |
| 3JBV | electron microscopy | 3.32 | 1 | 1-63 | [»] | |
| 3JCD | electron microscopy | 3.70 | Y | 1-63 | [»] | |
| 3JCE | electron microscopy | 3.20 | Y | 1-63 | [»] | |
| 3JCJ | electron microscopy | 3.70 | X | 1-63 | [»] | |
| 3JCN | electron microscopy | 4.60 | Y | 1-63 | [»] | |
| 4CSU | electron microscopy | 5.50 | 1 | 1-63 | [»] | |
| 4U1U | X-ray | 2.95 | BY/DY | 1-63 | [»] | |
| 4U1V | X-ray | 3.00 | BY/DY | 1-63 | [»] | |
| 4U20 | X-ray | 2.90 | BY/DY | 1-63 | [»] | |
| 4U24 | X-ray | 2.90 | BY/DY | 1-63 | [»] | |
| 4U25 | X-ray | 2.90 | BY/DY | 1-63 | [»] | |
| 4U26 | X-ray | 2.80 | BY/DY | 1-63 | [»] | |
| 4U27 | X-ray | 2.80 | BY/DY | 1-63 | [»] | |
| 4UY8 | electron microscopy | 3.80 | Y | 1-63 | [»] | |
| 4V47 | electron microscopy | 12.30 | AW | 1-63 | [»] | |
| 4V48 | electron microscopy | 11.50 | AW | 1-63 | [»] | |
| 4V4H | X-ray | 3.46 | BX/DX | 1-63 | [»] | |
| 4V4Q | X-ray | 3.46 | BX/DX | 1-63 | [»] | |
| 4V4V | electron microscopy | 15.00 | BW | 1-60 | [»] | |
| 4V4W | electron microscopy | 15.00 | BW | 1-60 | [»] | |
| 4V50 | X-ray | 3.22 | BY/DY | 1-63 | [»] | |
| 4V52 | X-ray | 3.21 | BX/DX | 1-63 | [»] | |
| 4V53 | X-ray | 3.54 | BX/DX | 1-63 | [»] | |
| 4V54 | X-ray | 3.30 | BX/DX | 1-63 | [»] | |
| 4V55 | X-ray | 4.00 | BX/DX | 1-63 | [»] | |
| 4V56 | X-ray | 3.93 | BX/DX | 1-63 | [»] | |
| 4V57 | X-ray | 3.50 | BX/DX | 1-63 | [»] | |
| 4V5B | X-ray | 3.74 | AX/CX | 1-63 | [»] | |
| 4V5H | electron microscopy | 5.80 | B1 | 1-63 | [»] | |
| 4V5Y | X-ray | 4.45 | BX/DX | 1-63 | [»] | |
| 4V64 | X-ray | 3.50 | BX/DX | 1-63 | [»] | |
| 4V65 | electron microscopy | 9.00 | BQ | 1-63 | [»] | |
| 4V66 | electron microscopy | 9.00 | BQ | 1-63 | [»] | |
| 4V69 | electron microscopy | 6.70 | BY | 1-63 | [»] | |
| 4V6C | X-ray | 3.19 | BY/DY | 1-63 | [»] | |
| 4V6D | X-ray | 3.81 | BY/DY | 1-63 | [»] | |
| 4V6E | X-ray | 3.71 | BY/DY | 1-63 | [»] | |
| 4V6K | electron microscopy | 8.25 | AZ | 1-63 | [»] | |
| 4V6L | electron microscopy | 13.20 | BZ | 1-63 | [»] | |
| 4V6M | electron microscopy | 7.10 | BY | 1-63 | [»] | |
| 4V6N | electron microscopy | 12.10 | A0 | 1-63 | [»] | |
| 4V6O | electron microscopy | 14.70 | B0 | 1-63 | [»] | |
| 4V6P | electron microscopy | 13.50 | B0 | 1-63 | [»] | |
| 4V6Q | electron microscopy | 11.50 | B0 | 1-63 | [»] | |
| 4V6R | electron microscopy | 11.50 | B0 | 1-63 | [»] | |
| 4V6S | electron microscopy | 13.10 | A0 | 1-63 | [»] | |
| 4V6T | electron microscopy | 8.30 | BY | 1-63 | [»] | |
| 4V6V | electron microscopy | 9.80 | B2 | 1-63 | [»] | |
| 4V6Y | electron microscopy | 12.00 | BY | 1-63 | [»] | |
| 4V6Z | electron microscopy | 12.00 | BY | 1-63 | [»] | |
| 4V70 | electron microscopy | 17.00 | BY | 1-63 | [»] | |
| 4V71 | electron microscopy | 20.00 | BY | 1-63 | [»] | |
| 4V72 | electron microscopy | 13.00 | BY | 1-63 | [»] | |
| 4V73 | electron microscopy | 15.00 | BY | 1-63 | [»] | |
| 4V74 | electron microscopy | 17.00 | BY | 1-63 | [»] | |
| 4V75 | electron microscopy | 12.00 | BY | 1-63 | [»] | |
| 4V76 | electron microscopy | 17.00 | BY | 1-63 | [»] | |
| 4V77 | electron microscopy | 17.00 | BY | 1-63 | [»] | |
| 4V78 | electron microscopy | 20.00 | BY | 1-63 | [»] | |
| 4V79 | electron microscopy | 15.00 | BY | 1-63 | [»] | |
| 4V7A | electron microscopy | 9.00 | BY | 1-63 | [»] | |
| 4V7B | electron microscopy | 6.80 | BY | 1-63 | [»] | |
| 4V7C | electron microscopy | 7.60 | B1 | 1-63 | [»] | |
| 4V7D | electron microscopy | 7.60 | A2 | 1-63 | [»] | |
| 4V7I | electron microscopy | 9.60 | AY | 1-63 | [»] | |
| 4V7S | X-ray | 3.25 | BY/DY | 1-63 | [»] | |
| 4V7T | X-ray | 3.19 | BY/DY | 1-63 | [»] | |
| 4V7U | X-ray | 3.10 | BY/DY | 1-63 | [»] | |
| 4V7V | X-ray | 3.29 | BY/DY | 1-63 | [»] | |
| 4V85 | X-ray | 3.20 | 2 | 1-63 | [»] | |
| 4V89 | X-ray | 3.70 | B2 | 1-63 | [»] | |
| 4V9C | X-ray | 3.30 | BY/DY | 1-63 | [»] | |
| 4V9D | X-ray | 3.00 | CY/DY | 1-63 | [»] | |
| 4V9O | X-ray | 2.90 | AY/CY/EY/GY | 1-63 | [»] | |
| 4V9P | X-ray | 2.90 | AY/CY/EY/GY | 1-63 | [»] | |
| 4WF1 | X-ray | 3.09 | BY/DY | 1-63 | [»] | |
| 4WOI | X-ray | 3.00 | BY/CY | 1-63 | [»] | |
| 4WWW | X-ray | 3.10 | RY/YY | 1-63 | [»] | |
| 4YBB | X-ray | 2.10 | CZ/DZ | 2-63 | [»] | |
| 5ADY | electron microscopy | 4.50 | Y | 1-63 | [»] | |
| 5AFI | electron microscopy | 2.90 | Y | 1-63 | [»] | |
| 5AKA | electron microscopy | 5.70 | X | 1-63 | [»] | |
| 5GAD | electron microscopy | 3.70 | Z | 1-63 | [»] | |
| 5GAE | electron microscopy | 3.33 | Z | 1-63 | [»] | |
| 5GAF | electron microscopy | 4.30 | Z | 2-63 | [»] | |
| 5GAG | electron microscopy | 3.80 | Z | 1-63 | [»] | |
| 5GAH | electron microscopy | 3.80 | Z | 1-63 | [»] | |
| 5H5U | electron microscopy | 3.00 | Z | 1-63 | [»] | |
| 5IQR | electron microscopy | 3.00 | Y | 1-63 | [»] | |
| 5IT8 | X-ray | 3.12 | CZ/DZ | 2-63 | [»] | |
| 5J5B | X-ray | 2.80 | CZ/DZ | 2-63 | [»] | |
| 5J7L | X-ray | 3.00 | CZ/DZ | 2-63 | [»] | |
| 5J88 | X-ray | 3.32 | CZ/DZ | 2-63 | [»] | |
| 5J8A | X-ray | 3.10 | CZ/DZ | 2-63 | [»] | |
| 5J91 | X-ray | 2.96 | CZ/DZ | 2-63 | [»] | |
| 5JC9 | X-ray | 3.03 | CZ/DZ | 2-63 | [»] | |
| 5JTE | electron microscopy | 3.60 | BY | 1-63 | [»] | |
| 5JU8 | electron microscopy | 3.60 | BY | 1-63 | [»] | |
| 5KCR | electron microscopy | 3.60 | 12 | 1-63 | [»] | |
| 5KCS | electron microscopy | 3.90 | 12 | 1-63 | [»] | |
| 5KPS | electron microscopy | 3.90 | Y | 1-63 | [»] | |
| 5KPV | electron microscopy | 4.10 | X | 1-63 | [»] | |
| 5KPW | electron microscopy | 3.90 | X | 1-63 | [»] | |
| 5KPX | electron microscopy | 3.90 | X | 1-63 | [»] | |
| 5L3P | electron microscopy | 3.70 | 2 | 1-63 | [»] | |
| 5LZA | electron microscopy | 3.60 | Y | 1-63 | [»] | |
| 5LZB | electron microscopy | 5.30 | Y | 1-63 | [»] | |
| 5LZC | electron microscopy | 4.80 | Y | 1-63 | [»] | |
| 5LZD | electron microscopy | 3.40 | Y | 1-63 | [»] | |
| 5LZE | electron microscopy | 3.50 | Y | 1-63 | [»] | |
| 5LZF | electron microscopy | 4.60 | Y | 1-63 | [»] | |
| 5MDV | electron microscopy | 2.97 | Y | 1-63 | [»] | |
| 5MDW | electron microscopy | 3.06 | Y | 1-63 | [»] | |
| 5MDY | electron microscopy | 3.35 | Y | 1-63 | [»] | |
| 5MDZ | electron microscopy | 3.10 | Y | 1-63 | [»] | |
| 5MGP | electron microscopy | 3.10 | Y | 1-63 | [»] | |
| 5NCO | electron microscopy | 4.80 | Z | 2-63 | [»] | |
| 5NP6 | electron microscopy | 3.60 | w | 1-63 | [»] | |
| 5NWY | electron microscopy | 2.93 | l | 1-63 | [»] | |
| 5O2R | electron microscopy | 3.40 | Y | 1-63 | [»] | |
| 5U4I | electron microscopy | 3.50 | Z | 1-63 | [»] | |
| 5U9F | electron microscopy | 3.20 | 27 | 1-63 | [»] | |
| 5U9G | electron microscopy | 3.20 | 27 | 1-63 | [»] | |
| 5UYK | electron microscopy | 3.90 | 27 | 1-63 | [»] | |
| 5UYL | electron microscopy | 3.60 | 27 | 1-63 | [»] | |
| 5UYM | electron microscopy | 3.20 | 27 | 1-63 | [»] | |
| 5UYN | electron microscopy | 4.00 | 27 | 1-63 | [»] | |
| 5UYP | electron microscopy | 3.90 | 27 | 1-63 | [»] | |
| 5UYQ | electron microscopy | 3.80 | 27 | 1-63 | [»] | |
| 5WDT | electron microscopy | 3.00 | Y | 1-60 | [»] | |
| 5WE4 | electron microscopy | 3.10 | Y | 1-60 | [»] | |
| 5WE6 | electron microscopy | 3.40 | Y | 1-60 | [»] | |
| 5WFK | electron microscopy | 3.40 | Y | 1-60 | [»] | |
| 6BU8 | electron microscopy | 3.50 | 27 | 1-63 | [»] | |
| 6ENF | electron microscopy | 3.20 | Y | 1-63 | [»] | |
| 6ENJ | electron microscopy | 3.70 | Y | 1-63 | [»] | |
| 6ENU | electron microscopy | 3.10 | Y | 1-63 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0A7M6 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0A7M6 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-47911N |
Protein interaction database and analysis system More...IntActi | P0A7M6, 35 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3487 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0A7M6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0A7M6 |
PRoteomics IDEntifications database More...PRIDEi | P0A7M6 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76337; AAC76337; b3312 BAE77979; BAE77979; BAE77979 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947807 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3274 eco:b3312 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3419 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0880 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10887 rpmC |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG41083MP Bacteria COG0255 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000248754 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0A7M6 |
KEGG Orthology (KO) More...KOi | K02904 |
Identification of Orthologs from Complete Genome Data More...OMAi | RFQNATN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0A7M6 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG10887-MONOMER MetaCyc:EG10887-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0A7M6 |
Protein Ontology More...PROi | PR:P0A7M6 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_00374 Ribosomal_L29, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001854 Ribosomal_L29/L35 IPR036049 Ribosomal_L29/L35_sf IPR018254 Ribosomal_L29_CS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00831 Ribosomal_L29, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46561 SSF46561, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00012 L29, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00579 RIBOSOMAL_L29, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RL29_ECOLI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0A7M6Primary (citable) accession number: P0A7M6 Secondary accession number(s): P02429, Q2M6X7 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | April 1, 1988 | |
| Last modified: | June 20, 2018 | |
| This is version 130 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- 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
