摘要
In this study, histidine kinase gene kdpD in the two-component regulatory system of Vibrio alginolyticus strain HY9901 was cloned for bioinformatics analysis. Sequence analysis revealed that kdpD gene （GenBank accession number： KJ544668） was 1 374 bp in length, encoding a putative protein of 457 amino acids. The predicted molecular weight （MW） of KdpE was 51.60 kD with a theoretical isoelectric point （pl） of 6.02. Using SignalP 4.0, TMHMM Server 2.0 and SoftBerry-Psite software, it was predicted that KdpE protein was equally located in Golgi apparatus, plasma membrane and endoplasmie reticulum （33.3%） , which did not contain a signal peptide but contained three transmembrane domains. KdpE protein had five casein kinase 1I phosphorylation sites, five protein kinase C phosphorylation sites and one cAMP- and cGMP-dependent protein kinase phosphorylation site. A phylogenetic tree was constructed by MEGA 5.0 software, which revealed that KdpD from V. alginolyticus had close genetic relationship with corresponding proteins from V. campbellii and V. parahaemolyticus. Using SWISS- MODEL Workspace, the three-dimensional structure of HATPase_c conserved domain in KdpD protein was constructed. These results may provide the basis for fur- ther studies on two-comoonent regulatory system KdpD/KdpE of V. alginolyticus.
In this study, histidine kinase gene kdpD in the two-component regulatory system of Vibrio alginolyticus strain HY9901 was cloned for bioinformatics analysis. Sequence analysis revealed that kdpD gene （GenBank accession number： KJ544668） was 1 374 bp in length, encoding a putative protein of 457 amino acids. The predicted molecular weight （MW） of KdpE was 51.60 kD with a theoretical isoelectric point （pl） of 6.02. Using SignalP 4.0, TMHMM Server 2.0 and SoftBerry-Psite software, it was predicted that KdpE protein was equally located in Golgi apparatus, plasma membrane and endoplasmie reticulum （33.3%） , which did not contain a signal peptide but contained three transmembrane domains. KdpE protein had five casein kinase 1I phosphorylation sites, five protein kinase C phosphorylation sites and one cAMP- and cGMP-dependent protein kinase phosphorylation site. A phylogenetic tree was constructed by MEGA 5.0 software, which revealed that KdpD from V. alginolyticus had close genetic relationship with corresponding proteins from V. campbellii and V. parahaemolyticus. Using SWISS- MODEL Workspace, the three-dimensional structure of HATPase_c conserved domain in KdpD protein was constructed. These results may provide the basis for fur- ther studies on two-comoonent regulatory system KdpD/KdpE of V. alginolyticus.
基金
Supported by National Natural Science Foundation of China(31402344,31572656)
"Sail in the Sea-Launch Plan"Science and Technology Innovation Project for College Students
