The World Health Organization (WHO) report stated that Acinetobacter baumannii had been classified as one of the most important pathogenic bacteria causing nosocomial infection in hospital patients due to multi-drug resistance (MDR). It is vital to find out new bacterial drug targets and annotated their structure and function for the exploration of new anti-bacterial agents. The present study utilized a systematic route to prioritize the potential drug targets that belong to Mur family of Acinetobacter baumannii and identify their homologous proteins using a computational approach such as sequence similarity search, multiple sequence alignment, phylogenetic analysis, protein sequence, and protein structure analysis. From the results of protein sequence analysis of eight Mur family proteins, they divided into three main enzymatic classes namely transferases (MurG, MurA and MraY), ligases (MurC, MurD, MurE, and MurF), and oxidoreductase (MurB). Based on the results of intra-comparative protein sequence analysis and enzymatic classification, we have chosen MurB, MurE, and MurG as the prioritized drug targets from A. baumannii and subjected them for further detailed studies of inter-species comparison. This inter-species comparison help us to explore the sequential and structural properties of homologous proteins in other species and hence, opens a gateway for new target identification and using common inhibitor for different bacterial species caused by various diseases. The pairwise sequence alignment results between A. baumannii’s MurB with A. calcoaceticus’s MurB, A. baumannii’s MurE with A. seifertii’s MurE, and A. baumannii’s MurG with A. pittii’s MurG showed that every group of the proteins are highly similar with each other and they showed sequence identity of 95.7% and sequence similarity of 97.2%. Together with the results of secondary and three-dimensional structure predictions explained that three selected proteins (MurB, MurE, and MurG) from A. baumannii and their related proteins (AcMurB, AsMurE, and ApMurG) belong to mixed αβ class and they are very similar.

中文翻译：

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Mur家族药物针对鲍曼不动杆菌的优先次序，并通过分子系统发育，一级序列和结构分析鉴定其同源蛋白。

世界卫生组织（WHO）的报告指出，鲍曼不动杆菌由于多药耐药性（MDR）被列为引起医院患者医院感染的最重要的致病菌之一。寻找新的细菌药物靶标并注释其结构和功能对于探索新的抗菌剂至关重要。本研究利用系统的途径对鲍曼不动杆菌Mur家族的潜在药物靶标进行优先排序，并使用诸如序列相似性搜索，多序列比对，系统发育分析，蛋白序列和蛋白结构分析等计算方法来鉴定其同源蛋白。 。从八个Mur家族蛋白的蛋白序列分析结果来看，它们分为三个主要的酶类，即转移酶（MurG，MurA和MraY），连接酶（MurC，MurD，MurE和MurF）和氧化还原酶（MurB）。根据内部比较蛋白序列分析和酶促分类的结果，我们选择了MurB，MurE和MurG作为鲍曼不动杆菌的优先药物靶标，并对其进行种间比较的进一步详细研究。这种种间比较有助于我们探索其他物种中同源蛋白的顺序和结构特性，因此，为新的靶标鉴定和使用由多种疾病引起的不同细菌物种使用通用抑制剂打开了大门。鲍曼不动杆菌的MurB与钙乙酸拟南芥的MurB，鲍曼不动杆菌的MurE与塞弗尔梯氏菌的MurE和鲍氏不动杆菌之间的成对序列比对结果。鲍曼氏菌的MurG与皮氏曲霉的MurG表明，每组蛋白质彼此高度相似，并且它们显示出95.7％的序列同一性和97.2％的序列相似性。连同二级和三维结构预测的结果一起说明，鲍曼不动杆菌中的三个选定蛋白质（MurB，MurE和MurG）及其相关蛋白质（AcMurB，AsMurE和ApMurG）属于混合αβ类，它们非常类似。