8,A.229. The Chlamydial Inclusion Membrane Protein, MrcA (MrcA) Family
The obligate intracellular bacterium, Chlamydia trachomatis, replicates within a parasitophorous vacuole termed an inclusion. During development, host proteins critical for regulating intracellular calcium (Ca2+) homeostasis interact with the inclusion membrane. The inclusion membrane protein, MrcA, interacts with the inositol-trisphosphate receptor (IP3R), an ER cationic channel that conducts Ca2+. Stromal interaction molecule 1 (STIM1), an ER transmembrane protein important for regulating store-operated Ca2+ entry (SOCE), localizes to the inclusion membrane via an uncharacterized interaction. Chamberlain et al. 2022 examined Ca2+ mobilization in C. trachomatis infected cells. Utilizing a variety of Ca2+ indicators to assess changes in cytosolic Ca2+ concentration, they demonstrate that C. trachomatis impairs host cell SOCE. Ca2+ regulates many cellular signaling pathways. The SOCE-dependent NFAT/calcineurin signaling pathway is impaired in C. trachomatis infected HeLa cells and likely has major implications on host cell physiology as it relates to C. trachomatis pathogenesis.
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Penicillin binding protein, MrcA of 428 aas and 1 - 3 TMSs. This inclusion membrane protein interacts with the inositol trisphosphate receptor (IP3R) (TC# 1.A.3.2.6) influencing Ca2+ fluxes between the ER and the cytoplasm (Chamberlain et al. 2022).
MrcA of Chlamydia trachomatis
Membrane peptidoglycan carboxypeptidase of 847 aas and 1 N-terminal TMS.
PCP of Streptomyces avidinii
K03693 penicillin-binding protein (PBP) of 766 aas and 1 N-terminal TMS.
PBP of Streptococcus dysgalactiae subsp. equisimilis AC-2713