InterPro : IPR014018

Name  SecA motor DEAD Short Name  SecA_motor_DEAD
Type  Domain Description  SecA is a cytoplasmic protein of 800 to 960 amino acid residues. The eubacterial secA protein []plays an important role in protein export. It interacts with the secY and secE components of the protein translocation system. It has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the membrane.SecA is a superfamily 2 (SF2) helicase that adapted to translocate proteins. It contains the characteristic DEAD/DEXH ATPase core structure with the seven SF2 motifs []. Several structural analyses on secA have been reported [, ]. They show that secA contains two recA-like domains similar to SF1 and SF2 helicases. In helicases, the two recA-like domains move relative to one another during the ATPase cycle, generating domain movements that translocate the helicase along nucleic acids. In secA, it seems that a similar mechanism is used to generate domain movements that are coupled to polypeptide translocation. The N-terminal recA-like domain of secA contains an insert of about 150 residues that forms the preprotein crosslinking domain (PPXD) which has the ability to bind preproteins in solution and which is important for preprotein loading onto SecYEG-containing membranes [].Homologs of secA are also encoded in the chloroplast genome of some algae []as well as in the nuclear genome of plants []. It could be involved in the intraorganellar protein transport into thylakoids.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

3 Contains

Id Name Short Name Type
IPR001650 Helicase, C-terminal Helicase_C Domain
IPR011130 SecA preprotein, cross-linking domain SecA_preprotein_X-link_dom Domain
IPR020937 SecA conserved site SecA_CS Conserved_site

2 Found In

Id Name Short Name Type
IPR000185 Protein translocase subunit SecA SecA Family
IPR022490 Protein translocase subunit SecA2 SecA2 Family

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Nohara T Isolation and characterization of the cDNA for pea chloroplast SecA. Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts. 1995 FEBS Lett 364 305-8
Valentin K SecA is plastid-encoded in a red alga: implications for the evolution of plastid genomes and the thylakoid protein import apparatus. 1993 Mol Gen Genet 236 245-50
Lill R SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. 1989 EMBO J 8 961-6
Hunt JF Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. 2002 Science 297 2018-26
Koonin EV Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein. 1992 FEBS Lett 298 6-8
Sharma V Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. 2003 Proc Natl Acad Sci U S A 100 2243-8
Papanikou E Identification of the preprotein binding domain of SecA. 2005 J Biol Chem 280 43209-17

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)