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)

There are 2127 SecA_PP_bind domains in 2127 proteins in SMART's nrdb database.

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

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	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
3jux	Structure of the translocation atpase seca from thermotoga maritima
3jv2	Crystal structure of b. subtilis seca with bound peptide

Links (links to other resources describing this domain)

• PFAM: SecA_PP_bind
• INTERPRO: IPR011130