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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 885 - 885 aligns to "C" in entry P10408 Subsequence at position 887 - 887 aligns to "C" in entry P10408 Subsequence at position 896 - 896 aligns to "C" in entry P10408 Subsequence at position 897 - 897 aligns to "[CH]" 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 885 - 885 aligns to "C" in entry P10408 (applies "Zinc") Subsequence at position 887 - 887 aligns to "C" in entry P10408 (applies "Zinc") 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 102 - 109 aligns to "M-[RKQNDAMFPHGSY]-T-G-E-G-K-[TS]" in entry P10408

... then these annotations are applied i

Protein namei

  • Recommended name:
    Protein translocase subunit SecA

Gene namei

  • Name:secA

Cofactori

  • Zn2+Note: May bind 1 zinc ion per subunit.

Sequence similaritiesi

Inductioni

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

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.

Subcellular locationi

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.

Metal bindingi

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

Nucleotide bindingi

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

Keywordsi

GO (Gene Ontology) termsi

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