Negative modulator of initiation of replication

<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>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 replication origin binding Source: EcoCyc <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
  • "A protein that binds to the P1 origin core and the oriC 13mer region in a methylation-specific fashion is the product of the host seqA gene."
    Brendler T., Abeles A., Austin S.
    EMBO J 14:4083-4089(1995) [PubMed] [Europe PMC] [Abstract]
• double-stranded methylated DNA binding Source: EcoCycInferred from direct assayⁱ
  • Ref.7

    "E. coli seqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration."
    Slater S., Wold S., Lu M., Boye E., Skarstad K., Kleckner N.
    Cell 82:927-936(1995) [PubMed] [Europe PMC] [Abstract]

    Cited for: CHARACTERIZATION, FUNCTION.
• hemi-methylated DNA-binding Source: EcoCycInferred from direct assayⁱ
  • "A protein that binds to the P1 origin core and the oriC 13mer region in a methylation-specific fashion is the product of the host seqA gene."
    Brendler T., Abeles A., Austin S.
    EMBO J 14:4083-4089(1995) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.15

    "Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex."
    Guarne A., Zhao Q., Ghirlando R., Yang W.
    Nat. Struct. Biol. 9:839-843(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 51-181 IN COMPLEX WITH HEMIMETHYLATED DNA, DNA-BINDING, SUBUNIT, DOMAIN.
  • Ref.17

    "Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization."
    Guarne A., Brendler T., Zhao Q., Ghirlando R., Austin S., Yang W.
    EMBO J. 24:1502-1511(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-50, SUBUNIT.
  • "The binary protein-protein interaction landscape of Escherichia coli."
    Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S., Ceol A., Hauser R., Siszler G., Wuchty S., Emili A., Babu M., Aloy P., Pieper R., Uetz P.
    Nat Biotechnol 32:285-290(2014) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• negative regulation of DNA-dependent DNA replication initiation Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.5

    "SeqA limits DnaA activity in replication from oriC in Escherichia coli."
    von Freiesleben U., Rasmussen K.V., Schaechter M.
    Mol. Microbiol. 14:763-772(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• regulation of transcription, DNA-templated Source: InterPro
• response to radiation Source: EcoCycInferred from mutant phenotypeⁱ
  • "Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database."
    Sargentini N.J., Gularte N.P., Hudman D.A.
    Mutat. Res. 793:1-14(2016) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

<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 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

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<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

Mutagenesis

<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

Proteomic databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.15

    "Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex."
    Guarne A., Zhao Q., Ghirlando R., Yang W.
    Nat. Struct. Biol. 9:839-843(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 51-181 IN COMPLEX WITH HEMIMETHYLATED DNA, DNA-BINDING, SUBUNIT, DOMAIN.
  • Ref.17

    "Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization."
    Guarne A., Brendler T., Zhao Q., Ghirlando R., Austin S., Yang W.
    EMBO J. 24:1502-1511(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-50, SUBUNIT.
  • "The binary protein-protein interaction landscape of Escherichia coli."
    Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S., Ceol A., Hauser R., Siszler G., Wuchty S., Emili A., Babu M., Aloy P., Pieper R., Uetz P.
    Nat Biotechnol 32:285-290(2014) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

Region

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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

Phylogenomic databases

Family and domain databases

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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
MKTIEVDDEL YSYIASHTKH IGESASDILR RMLKFSAASQ PAAPVTKEVR 
        60         70         80         90        100
VASPAIVEAK PVKTIKDKVR AMRELLLSDE YAEQKRAVNR FMLLLSTLYS 
       110        120        130        140        150
LDAQAFAEAT ESLHGRTRVY FAADEQTLLK NGNQTKPKHV PGTPYWVITN 
       160        170        180 
TNTGRKCSMI EHIMQSMQFP AELIEKVCGT I                     

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families