UniProtKB - P10026 (TRAM1_ECOLI)
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- BLAST>sp|P10026|TRAM1_ECOLI Relaxosome protein TraM OS=Escherichia coli (strain K12) OX=83333 GN=traM PE=1 SV=1 MAKVNLYISNDAYEKINAIIEKRRQEGAREKDVSFSATASMLLELGLRVHEAQMERKESA FNQTEFNKLLLECVVKTQSSVAKILGIESLSPHVSGNSKFEYANMVEDIREKVSSEMERF FPKNDDE
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Relaxosome protein TraM
traM
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
<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.4"The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids."
Di Laurenzio L., Frost L.S., Paranchych W.
Mol. Microbiol. 6:2951-2959(1992) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DNA-BINDING, SUBCELLULAR LOCATION. - Ref.5"Regulation of the expression of the traM gene of the F sex factor of Escherichia coli."
Penfold S.S., Simon J., Frost L.S.
Mol. Microbiol. 20:549-558(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION IN AUTOREGULATION, DISRUPTION PHENOTYPE. - Ref.7"Characterizing the DNA contacts and cooperative binding of F plasmid TraM to its cognate sites at oriT."
Fekete R.A., Frost L.S.
J. Biol. Chem. 277:16705-16711(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN COOPERATIVITY OF DNA-BINDING, FUNCTION IN DNA-BENDING. - Ref.9"The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage at oriT through an interaction with TraI."
Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.
Mol. Microbiol. 63:1173-1184(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN STIMULATING TRAI NICKING, DNA-BINDING, INTERACTION WITH TRAY, SUBUNIT.
<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
- DNA binding Source: UniProtKB-KW
<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
- conjugation Source: UniProtKB-KW
- regulation of transcription, DNA-templated Source: UniProtKB-KW
- transcription, DNA-templated Source: UniProtKB-KW
<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 | DNA-binding, Repressor |
| Biological process | Conjugation, Transcription, Transcription regulation |
<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: Relaxosome protein TraM |
| <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:traM Ordered Locus Names:ECOK12F071 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oni | Plasmid F12 Publications
|
| <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 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
- Cytoplasm 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.4"The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids."
Di Laurenzio L., Frost L.S., Paranchych W.
Mol. Microbiol. 6:2951-2959(1992) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DNA-BINDING, SUBCELLULAR LOCATION.
<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
- cytoplasm Source: UniProtKB-SubCell
<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 - Cellular componenti
Cytoplasm<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
<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"Regulation of the expression of the traM gene of the F sex factor of Escherichia coli."
Penfold S.S., Simon J., Frost L.S.
Mol. Microbiol. 20:549-558(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION IN AUTOREGULATION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 5 | N → D: Loss of all functions. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 76 | K → E: 100,000-fold decrease in conjugation efficiency, but tetramerizes and binds DNA normally. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 88 | E → L or Q: Increased homotetramer stability. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 99 | K → E: 100,000-fold decrease in conjugation efficiency, but tetramerizes and binds DNA normally. Binds less well to TraD. May be dominant over wild-type. Partially rescued by a TraD E-712 mutation. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 106 | V → A: 2000-fold decrease in conjugation efficiency, but tetramerizes and binds DNA normally. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 110 | R → E: 33,000-fold decrease in conjugation efficiency, but tetramerize and bind DNA normally. 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
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 121 | F → S: Alters oligomerization, probably more dimers than tetramers. 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
| 1 |
<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_0000068467 | 1 – 127 | Relaxosome protein TraMAdd BLAST | 127 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | P10026 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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"Regulation of the expression of the traM gene of the F sex factor of Escherichia coli."
Penfold S.S., Simon J., Frost L.S.
Mol. Microbiol. 20:549-558(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION IN AUTOREGULATION, DISRUPTION PHENOTYPE.
<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
<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"The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro."
Disque-Kochem C., Dreiseikelmann B.
J. Bacteriol. 179:6133-6137(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TRAD. - Ref.8"Mutations in the C-terminal region of TraM provide evidence for in vivo TraM-TraD interactions during F-plasmid conjugation."
Lu J., Frost L.S.
J. Bacteriol. 187:4767-4773(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TRAD, MUTAGENESIS OF LYS-99 AND PHE-121. - Ref.9"The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage at oriT through an interaction with TraI."
Ragonese H., Haisch D., Villareal E., Choi J.H., Matson S.W.
Mol. Microbiol. 63:1173-1184(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN STIMULATING TRAI NICKING, DNA-BINDING, INTERACTION WITH TRAY, SUBUNIT. - Ref.10"Structural basis of cooperative DNA recognition by the plasmid conjugation factor, TraM."
Wong J.J., Lu J., Edwards R.A., Frost L.S., Glover J.N.
Nucleic Acids Res. 39:6775-6788(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT. - Ref.11"Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM."
Lu J., Edwards R.A., Wong J.J., Manchak J., Scott P.G., Frost L.S., Glover J.N.
EMBO J. 25:2930-2939(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 58-127, COILED-COIL DOMAIN, SUBUNIT, DNA-BINDING, MUTAGENESIS OF GLU-88. - Ref.12"Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation."
Lu J., Wong J.J., Edwards R.A., Manchak J., Frost L.S., Glover J.N.
Mol. Microbiol. 70:89-99(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 58-127 IN COMPLEX WITH C-TERMINUS OF TRAD, MUTAGENESIS OF ASN-5; LYS-76; LYS-99; VAL-106 AND ARG-110.
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-27653N |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 3 – 7 | 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 | 5 | |
| <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 | 10 – 24 | 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 | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 30 – 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 | 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 | 35 – 53 | 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 | 19 | |
| <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 | 63 – 89 | 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 | 27 | |
| <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 | 92 – 94 | 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 | 3 | |
| <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 | 98 – 100 | 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 | 3 | |
| <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 | 102 – 120 | 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 | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 123 – 125 | 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 | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P10026 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P10026 |
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 | P10026 |
<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
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 63 – 89 | 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
| 27 |
<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
<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 - Domaini
Coiled coilPhylogenomic databases
Identification of Orthologs from Complete Genome Data More...OMAi | SVEMERF |
Family and domain databases
Conserved Domains Database More...CDDi | cd14804 Tra_M, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010992 IHF-like_DNA-bd_dom_sf IPR007925 TRelaxosome_TraM |
Pfam protein domain database More...Pfami | View protein in Pfam PF05261 Tra_M, 1 hit |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD008204 T4SS_TraM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47729 SSF47729, 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.
10 20 30 40 50
MAKVNLYISN DAYEKINAII EKRRQEGARE KDVSFSATAS MLLELGLRVH
60 70 80 90 100
EAQMERKESA FNQTEFNKLL LECVVKTQSS VAKILGIESL SPHVSGNSKF
110 120
EYANMVEDIR EKVSSEMERF FPKNDDE
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 | K01147 Genomic DNA Translation: AAA24907.1 X00545 Genomic DNA Translation: CAA25216.1 U01159 Genomic DNA Translation: AAC44191.1 AP001918 Genomic DNA Translation: BAA97941.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A29331 JCECMF |
NCBI Reference Sequences More...RefSeqi | NP_061450.1, NC_002483.1 WP_001151527.1, NZ_CP014273.1 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1263565 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|83333.107.peg.642 |
<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 | |
|---|---|---|---|---|---|
| P10026 | Conjugal transfer protein TraM | 127 | |||
| UPI0000D894D1 | 70 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P10026 | Conjugal transfer protein TraM | 127 | |||
| IncF conjugal transfer protein TraM | 127 | ||||
| Relaxosome protein TraM | 127 | ||||
| TraM | 127 | ||||
| TraM | 127 | ||||
| +157 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P10026 | Conjugal transfer protein TraM | 127 | |||
| UPI0004D41BB7 | 127 | ||||
| UPI0004E285C4 | 127 | ||||
| TraM protein | 127 | ||||
| IncF conjugal transfer protein TraM | 127 | ||||
| +414 | |||||
<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 | K01147 Genomic DNA Translation: AAA24907.1 X00545 Genomic DNA Translation: CAA25216.1 U01159 Genomic DNA Translation: AAC44191.1 AP001918 Genomic DNA Translation: BAA97941.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A29331 JCECMF |
NCBI Reference Sequences More...RefSeqi | NP_061450.1, NC_002483.1 WP_001151527.1, NZ_CP014273.1 |
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 |
| 2G7O | X-ray | 1.40 | A | 58-127 | [»] | |
| 2G9E | X-ray | 1.80 | A | 58-127 | [»] | |
| 3D8A | X-ray | 2.55 | A/B/C/D/E/F/G/H | 58-127 | [»] | |
| 4QPO | X-ray | 2.00 | A/B/C/D | 2-54 | [»] | |
| 4QPQ | X-ray | 3.11 | A/B/C/D/E/F/G/H | 2-54 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P10026 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P10026 | |||||
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-27653N |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | P10026 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1263565 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|83333.107.peg.642 |
Phylogenomic databases
Identification of Orthologs from Complete Genome Data More...OMAi | SVEMERF |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P10026 |
Protein Ontology More...PROi | PR:P10026 |
Family and domain databases
Conserved Domains Database More...CDDi | cd14804 Tra_M, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR010992 IHF-like_DNA-bd_dom_sf IPR007925 TRelaxosome_TraM |
Pfam protein domain database More...Pfami | View protein in Pfam PF05261 Tra_M, 1 hit |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD008204 T4SS_TraM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47729 SSF47729, 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 | TRAM1_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 | P10026Primary (citable) accession number: P10026 | |
| <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 1, 1989 |
| Last sequence update: | July 1, 1989 | |
| Last modified: | May 23, 2018 | |
| This is version 117 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, PlasmidDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
