PhoP Protein, E.coli (P.pastoris, Myc, His)

PhoP protein is an important component of the PhoP/PhoQ two-component regulatory system, adapting to low Mg(2+) environments and controlling acid-tolerant gene expression. Under low periplasmic Mg(2+), PhoQ phosphorylates PhoP, activating PhoP-activated genes (PAG) and repressing PhoP-repressed genes (PRG). PhoP Protein, E.coli (P.pastoris, Myc, His) is the recombinant E. coli-derived PhoP protein, expressed by P. pastoris , with N-His, C-Myc labeled tag. The total length of PhoP Protein, E.coli (P.pastoris, Myc, His) is 223 a.a., with molecular weight of ~29.0 kDa.

PhoP Protein, a crucial component of the two-component regulatory system PhoP/PhoQ, plays a pivotal role in adapting to low Mg(2+) environments and governing the expression of acid resistance genes. In conditions of low periplasmic Mg(2+), PhoQ phosphorylates PhoP, leading to the activation of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). Conversely, high periplasmic Mg(2+) triggers the dephosphorylation of phospho-PhoP by PhoQ, resulting in the repression of PAG and potential expression of certain PRG. PhoP facilitates magnesium influx to the cytosol through the activation of MgtA and promotes the expression of various genes, including rstA/rstB, hemL, mgrB, nagA, slyB, vboR, and yrbL. Additionally, the regulatory loop involves feedback inhibition by MgrB, which binds to PhoQ, influencing its activity and downstream effector PhoP. The redox sensitivity of PhoP-regulated transcription is evident in a more reducing periplasmic environment, influenced by factors such as the deletion of dsbA/dsbB or treatment with dithiothreitol, and MgrB operates in the pathway between DsbA/DsbB and PhoP/PhoQ.

E.coli

P. pastoris

N-His;C-Myc

P23836 (1M-223R)

945697  [NCBI]

MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR

Approximately 29.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.