Archaeal protein PH0471, N-terminal (IPR033853)

Short name: PH1510-N

Overlapping homologous superfamilies

Domain relationships



The N-terminal region of the the PH1510 protein (1510-N or PH1510-N) from archaebacterium Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. It is structurally related to ClpP. In the genome of Pyrococcus horikoshii, PH1510 is homologous to the genes nfed (nodulation formation efficiency D) [PMID: 15611110].

PH1510 (MEROPS identifier S49.005) is thought to be a signal peptide peptidase, which degrades the membrane-bound signal peptide after it has been released from secreted proteins [PMID: 17259602]. The peptidase domain is followed by a C-terminal NfeD domain [PMID: 20012272].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.