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The annotation and conditions in this rule are derived from the following entries: P10408 (SECA_ECOLI), P28366 (SECA_BACSU), P43803 (SECA_HAEIN)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01382
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented
    • Matches HAMAP signature MF_01382
    • gene location = Plastid
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 896 - 896 aligns to "C" in entry P10408 Subsequence at position 897 - 897 aligns to "[CH]" in entry P10408 Subsequence at position 887 - 887 aligns to "C" in entry P10408 Subsequence at position 885 - 885 aligns to "C" in entry P10408
    • gene location = Plastid; Chloroplast
    • gene location ≠ Plastid; Chloroplast
    • taxon = Gloeobacter
    • gene location ≠ Plastid; Chloroplast
    • gene location = Plastid; Chloroplast
    • proteome property = Membrane=2
    • taxon ≠ Cyanobacteria
    • gene location ≠ Plastid; Chloroplast
    • proteome property ≠ Membrane=*
    • taxon ≠ Cyanobacteria
    • gene location ≠ Plastid; Chloroplast
    • proteome property = Membrane=1
    • taxon ≠ Cyanobacteria
    • gene location ≠ Plastid; Chloroplast
  • Subsequence at position 896 - 896 aligns to "C" in entry P10408 (applies "Zinc") Subsequence at position 897 - 897 aligns to "[CH]" in entry P10408 (applies "Zinc") Subsequence at position 887 - 887 aligns to "C" in entry P10408 (applies "Zinc") Subsequence at position 885 - 885 aligns to "C" in entry P10408 (applies "Zinc")
    • Subsequence at position 102 - 109 aligns to "M-[RKQNDAMFPHGSY]-T-G-E-G-K-[TS]" in entry P10408

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 namei

  • Recommended name:
    Protein translocase subunit SecA

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 namei

  • Name:secA

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
  • Probably participates in protein translocation into and across both the cytoplasmic and thylakoid membranes in cyanobacterial cells.
  • Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
  • Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.

<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

  • Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
  • Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.

<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

  • Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM.

<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • ATP (to residues corresponding to positions 102 - 109)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Zinc (to residues corresponding to position 896)
  • Zinc (to residues corresponding to position 897)
  • Zinc (to residues corresponding to position 887)
  • Zinc (to residues corresponding to position 885)

<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

<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 (Gene Ontology) termsi

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