Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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SecA_PP_bind SecA preprotein cross-linking domain

SMART accession number:	SM00958
Description:	The SecA ATPase is involved in the insertion and retraction of preproteins through the plasma membrane. This domain has been found to cross-link to preproteins, thought to indicate a role in preprotein binding. The pre-protein cross-linking domain is comprised of two sub domains that are inserted within the ATPase domain (PUBMED:12242434).
Interpro abstract (IPR011130):	The SecA ATPase is involved in the insertion and retraction of preproteins through the plasma membrane. This domain has been found to cross-link to preproteins, thought to indicate a role in preprotein binding. The pre-protein cross-linking domain is comprised of two sub domains that are inserted within the ATPase domain [ (PUBMED:12242434) ].
GO process:	protein import (GO:0017038)
GO component:	membrane (GO:0016020)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 24367 SecA_PP_bind domains in 24364 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing SecA_PP_bind domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with SecA_PP_bind domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing SecA_PP_bind domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: transport
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Hunt JF et al.
  • Nucleotide control of interdomain interactions in the conformationalreaction cycle of SecA.
  • Science. 2002; 297: 2018-26
  • Display abstract

  • The SecA adenosine triphosphatase (ATPase) mediates extrusion of the aminotermini of secreted proteins from the eubacterial cytosol based on cyclesof reversible binding to the SecYEG translocon. We have determined thecrystal structure of SecA with and without magnesium-adenosine diphosphatebound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution,respectively. Candidate sites for preprotein binding are located on asurface containing the SecA epitopes exposed to the periplasm upon bindingto SecYEG and are thus positioned to deliver preprotein to SecYEG.Comparisons with structurally related ATPases, including superfamily I andII ATP-dependent helicases, suggest that the interaction geometry of thetandem motor domains in SecA is modulated by nucleotide binding, which isshown by fluorescence anisotropy experiments to reverse an endothermicdomain-dissociation reaction hypothesized to gate binding to SecYEG.

• Structure (3D structures containing this domain)

• 3D Structures of SecA_PP_bind domains in PDB

  PDB code	Main view	Title
  1m6n		Crystal structure of the SecA translocation ATPase from Bacillus subtilis
  1m74		Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis
  1nkt		CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS
  1nl3		CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM
  1tf2		Crystal structure of SecA:ADP in an open conformation from Bacillus Subtilis
  1tf5		Crystal structure of SecA in an open conformation from Bacillus Subtilis
  2fsf		Escherichia coli SecA, the preprotein translocase dimeric ATPase
  2fsg		Complex SecA:ATP from Escherichia coli
  2fsh		Complex SecA:AMP-PNP from Escherichia coli
  2fsi		Complex SecA:ADP from Escherichia coli
  2ibm		A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
  2ipc		Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer
  2vda		Solution structure of the SecA-signal peptide complex
  3din		Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase
  3dl8		Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA
  3iqm		Active site mutants of B. subtilis SecA
  3iqy		Active site mutants of B. subtilis SecA
  3jux		Structure of the translocation ATPase SecA from Thermotoga maritima
  3jv2		Crystal Structure of B. subtilis SecA with bound peptide
  4uaq		4UAQ
  4ys0		4YS0
  5eul		5EUL

• Links (links to other resources describing this domain)

• PFAM	SecA_PP_bind
  INTERPRO	IPR011130

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