InterPro : IPR000185

Name  Protein translocase subunit SecA Short Name  SecA
Type  Family Description  Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocasepathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them tothe translocase component []. From there, the mature proteins are either targeted to the outermembrane, or remain as periplasmic proteins. The translocase protein subunits are encoded on the bacterialchromosome.The translocase itself comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integralmembrane complex (SecCY, SecE and SecG), and two additional membrane proteins that promote the release ofthe mature peptide into the periplasm (SecD and SecF) []. The chaperone protein SecB []is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial cytoplasm.SecB maintains preproteins in an unfolded state after translation, and targets these to the peripheral membraneprotein ATPase SecA for secretion [].SecA is a cytoplasmic protein of 800 to 960 amino acid residues.Homologues 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 theintraorganellar protein transport into thylakoids.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR022490 Protein translocase subunit SecA2 SecA2 Family
IPR026389 Protein translocase subunit SecA, Actinobacteria-type SecA_Actinobact_type Family

7 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
IPR014018 SecA motor DEAD SecA_motor_DEAD Domain
IPR011115 SecA DEAD-like, N-terminal SecA_DEAD Domain
IPR004027 SEC-C motif SEC_C_motif Conserved_site
IPR011116 SecA Wing/Scaffold SecA_Wing/Scaffold Domain
IPR020937 SecA conserved site SecA_CS Conserved_site

0 Found In

0 Parent Features

5 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
Bieker KL The sec and prl genes of Escherichia coli. 1990 J Bioenerg Biomembr 22 291-310
Driessen AJ SecB, a molecular chaperone with two faces. 2001 Trends Microbiol 9 193-6
Müller JP Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. 1999 FEMS Microbiol Lett 176 219-27



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)