1. LILL, R., CUNNINGHAM, K., BRUNDAGE, L.A., ITO, K., OLIVER, D. AND
SecA protein hydrolyzes ATP and is an essential component of the protein
translocation ATPase of Escherichia coli.
EMBO J. 8(3) 961-966 (1989).
2. SCHMIDT, M.G., ROLLO, E.E., GRODBERG, J. AND OLIVER, D.B.
Nucleotide sequence of the secA gene and secA(Ts) mutations preventing
protein export in Escherichia coli.
J.BACTERIOL. 170(8) 3404-3414 (1988).
3. VALENTIN, K.
SecA is plastid-encoded in red alga: implications for the evolution of
plastid genomes and thylakoid protein import apparatus.
MOL.GEN.GENET. 236 245-250 (1993).
4. NOHARA, T., NAKAI, M. GOTO, A. AND ENDO, T.
Isolation and characterization of the cDNA for pea chloroplast SecA.
Evolutionary conservation of the bacterial-type SecA-dependent protein
transport within chloroplasts.
FEBS LETT. 364 305-308 (1995).
The secA protein is one of seven secretory proteins (secA-F and secY) that
form the prokaryotic protein translocation apparatus. SecA has a central
role in coupling the hydrolysis of ATP to the transfer of pre-secretory
periplasmic and outer membrane proteins across the membrane [1,2].
Homologues of secA are also encoded in chloroplast genomes of some algae
, as well as in the nuclear genome of some plants ; they may contain
a similar secA protein-dependent system for intra-organellar transport
SECA is a 7-element fingerprint that provides a signature for the secA
protein family. The fingerprint was derived from an initial alignment of 9
sequences: the motifs were drawn from conserved regions of the hydrophobic
N-terminal and central regions of the alignment. Three iterations on
OWL30.1 were required to reach convergence, at which point a true set
comprising 32 sequences was identified. Two partial matches were also found,
MBU43178 and ZMU71123, both of which are secA protein fragments.
An update on SPTR37_9f identified a true set of 33 sequences, and 2