Protein Family Models

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

Domains containing the SEC-C motif (SecA C-terminal motif) is found broadly in bacteria. In Escherichia coli K-12, for example, it occurs in YchJ (once at each end of the protein), YecA, and SecA. The motif typically is CXCX(8)CH or CXCX(8)CC, although the spacing may vary.

Date:

2024-08-14

The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

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:

2020-12-14

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

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:

2021-07-21

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