Protein Family Models

SecA is the preprotein translocase ATPase subunit and a superfamily 2 (SF2) RNA helicase [4]. This entry corresponds to the second P-loop domain. Paper describing PDB structure 1m6n. [1]. 12242434. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J;. Science 2002;297:2018-2026. Paper describing PDB structure 1nkt. [2]. 12606717. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. Sharma V, Arockiasamy A, Ronning DR, Savva CG, Holzenburg A, Braunstein M, Jacobs WR Jr, Sacchettini JC;. Proc Natl Acad Sci U S A. 2003;100:2243-2248. Paper describing PDB structure 1tf2. [3]. 15256599. A large conformational change of the translocation ATPase SecA. Osborne AR, Clemons WM Jr, Rapoport TA;. Proc Natl Acad Sci U S A. 2004;101:10937-10942. Paper describing PDB structure 2fsf. [4]. 17229438. Structure of dimeric SecA, the Escherichia coli preprotein translocase motor. Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K;. J Mol Biol. 2007;366:1545-1557. Paper describing PDB structure 2ibm. [5]. 16989859. A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA. Zimmer J, Li W, Rapoport TA;. J Mol Biol. 2006;364:259-265. (from Pfam)

Date:

2024-10-16

SecA protein binds to the plasma membrane where it interacts with proOmpA to support translocation of proOmpA through the membrane. SecA protein achieves this translocation, in association with SecY protein, in an ATP dependent manner [1,2]. This domain represents the N-terminal ATP-dependent helicase domain, which is related to the Pfam:PF00270 [3]. [1]. 9644254. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Mori H, Sugiyama H, Yamanaka M, Sato K, Tagaya M, Mizushima S;. J Biochem (Tokyo) 1998;124:122-129. [2]. 2542029. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. Lill R, Cunningham K, Brundage LA, Ito K, Oliver D, Wickner W;. EMBO J 1989;8:961-966. [3]. 12242434. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J;. Science 2002;297:2018-2026. (from Pfam)

Date:

2024-10-16

SecA protein binds to the plasma membrane where it interacts with proOmpA to support translocation of proOmpA through the membrane. SecA protein achieves this translocation, in association with SecY protein, in an ATP dependent manner. This family is composed of two C-terminal alpha helical subdomains: the wing and scaffold subdomains [1]. [1]. 12242434. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J;. Science 2002;297:2018-2026. (from Pfam)

Date:

2024-10-16

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 [1]. [1]. 12242434. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J;. Science 2002;297:2018-2026. (from Pfam)

Date:

2024-10-16

preprotein translocase subunit SecA is part of the Sec protein translocase complex, playing 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

Date:

2017-03-02

Functions in protein export; can interact with acidic membrane phospholipids and the SecYEG protein complex; binds to preproteins; binds to ATP and undergoes a conformational change to promote membrane insertion of SecA/bound preprotein; ATP hydrolysis appears to drive release of the preprotein from SecA and deinsertion of SecA from the membrane; additional proteins SecD/F/YajC aid SecA recycling; exists in an equilibrium between monomers and dimer

Gene:

secA

Date:

2020-10-26

Members of this family always occur in genomes with the preprotein translocase SecA (TIGR00963) and closely resemble it, hence the designation SecA2. However, this appears to mark a different type of accessory Sec system SecA2 (TIGR03714) from the serine-rich glycoprotein type found in Staphylococcus and Streptococcus, and the actinobacterial SecA2 (TIGR04221). This type occurs in species including Bacillus anthracis, Geobacillus thermoglucosidasius, Solibacillus silvestris, etc.

Gene:

secA2

Date:

2021-04-27

The proteins SecA-F and SecY, not all of which are necessary, comprise the standard prokaryotic protein translocation apparatus. Other, specialized translocation systems also exist but are not as broadly distributed. This HMM describes SecA, an essential member of the apparatus. This model excludes SecA2 of the accessory secretory system.

Gene:

secA

Date:

2024-05-30