Journal of Microbiology

Journal Article

Taxonomic description and genome sequence of Halobacillus marinus sp. nov., a novel strain isolated from Chilika Lake, India: Ananta N. Panda , Samir Ranjan Mishra , Lopamudra Ray , Surajit Das , Gurdeep Rastogi , Tapan Kumar Adhya , Mrutyunjay Suar , Vishakha Raina; J. Microbiol. 2018;56(4):223-230. Published online April 2, 2018; DOI: https://doi.org/10.1007/s12275-018-7387-x

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A moderately halophilic spore forming, motile, Gram-positive, rod-shaped bacterial strain designated as KGW1T was isolated from water sample of Chilika Lake and characterized taxonomically using polyphasic approach. The strain grew in the presence of 0–25% (w/v) NaCl in marine salt agar media, hydrolyzes casein, and gelatin and shows presence of alkaline proteases. The major cell wall menaquinone was MK7 and major cellular fatty acids were anteiso-C15:0 (44.89%), anteiso-C17:0 (6.18%), isoC15:0 (19.38%), and iso-C16:0 (7.39%). Several chemotaxonomic features conform the isolate be a member of genus Halobacillus. The isolate KGW1T contained A1γ meso-Dpm-direct type of peptidoglycan which is different from its phylogenetically closest neighbours. The 16S rRNA gene sequence based phylogenetic analysis also revealed the strain KGW1T was affiliated to the genus Halobacillus and sequence similarity between the isolated strain and the type strains of Halobacillus species were found closest to, H. dabanensis D-8 DSM 18199T (99.08%) and H. faecis IGA7-4 DSM 21559T (99.01%), H. trueperi SL-5 DSM 10404T (98.94%). The in silico DDH showed that the values in a range of 14.2–17.5% with the most closest strain H. dabanensis D-8 DSM 18199T and other type strains of the genus Halobacillus for which whole genome sequence is reported. DNA-DNA relatedness between strain KGW1T and the closest type strain Halobacillus trueperi DSM 10404T was 11.75% (± 1.15). The draft genome sequence includes 3,683,819 bases and comprises of 3898 predicted coding sequences with a G + C content of 46.98%. Thus, the significant distinctiveness supported by phenotypic and genotypic data with its closest neighbors and other closely related species confirm the strain KGW1T to be classified as a novel species within the genus Halobacillus, for which the name Halobacillus marinus sp. nov. is proposed. The type strain is KGW1T (= DSM 29522 = JCM 30443).

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Draft genome sequence of Halobacillus campisalis strain ASL-17
Anushree Srivastava, Michael Christopher Macey, Terry J. McGenity, Karen Olsson-Francis, Frank J. Stewart
Microbiology Resource Announcements.2024;[Epub] CrossRef
Trachyspermum ammi seed extract-mediated Ag nanoparticles: an insight into its in vitro biopotency
Vikneshvar K. S., R Subashini, Anieya Israel, Karuvelan Murugan, Namitha Ramakrishnan
Biomass Conversion and Biorefinery.2023;[Epub] CrossRef
Identification of antibacterial metabolites produced by a marine bacterium Halobacillus marinus HMALI004
Sardar Ali, Runlin Cai, Hao Feng, Jianmin Xie, Yueling Zhang, Hui Wang
Journal of Applied Microbiology.2022; 133(5): 3030. CrossRef

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Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules: Young Jun An , Jung-Hyun Na , Myung-Il Kim , Sun-Shin Cha; J. Microbiol. 2015;53(10):711-717. Published online October 2, 2015; DOI: https://doi.org/10.1007/s12275-015-5417-5

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Abstract

Lon proteases degrade defective or denature proteins as well as some folded proteins for the control of cellular protein quality. There are two types of Lon proteases, LonA and LonB. Each consists of two functional components: a protease component and an ATPase associated with various cellular activities (AAA+ module). Here, we report the 2.03 Å-resolution crystal structure of the isolated AAA+ module (iAAA+ module) of LonB from Thermococcus onnurineus NA1 (TonLonB). The iAAA+ module, having no bound nucleotide, adopts a conformation virtually identical to the ADP-bound conformation of AAA+ modules in the hexameric structure of TonLonB; this provides insights into the ATP-independent proteolytic activity observed in a LonB protease. Structural comparison of AAA+ modules between LonA and LonB revealed that the AAA+ modules of Lon proteases are separated into two distinct clades depending on their structural features. The AAA+ module of LonB belongs to the ‘H2 & Ins1 insert clade (HINS clade)’ defined for the first time in this study, while the AAA+ module of LonA is a member of the HCLR clade.

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Citations to this article as recorded by

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
Alla Gustchina, Mi Li, Anna G. Andrianova, Arsen M. Kudzhaev, George T. Lountos, Bartosz Sekula, Scott Cherry, Joseph E. Tropea, Ivan V. Smirnov, Alexander Wlodawer, Tatyana V. Rotanova
International Journal of Molecular Sciences.2022; 23(19): 11425. CrossRef
Structure and the Mode of Activity of Lon Proteases from Diverse Organisms
Alexander Wlodawer, Bartosz Sekula, Alla Gustchina, Tatyana V. Rotanova
Journal of Molecular Biology.2022; 434(7): 167504. CrossRef
Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme
Nicholas P. Robinson, Julie A. Maupin-Furlow
Emerging Topics in Life Sciences.2018; 2(4): 561. CrossRef

Cloning of the gense coding for extracellular proteases from alkalophilic xanthomonas SP. JK311: Kim, Young Hun , Jang, Ji Yeon , Yeeh, Yeehn , Kim, Yong Ho , Kim, Sang Hae; J. Microbiol. 1995;33(4):344-349.

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Abstract: The alkalophilic bacterium, Xanthomonas sp. JK311, producing extracellular proteases, was isolated from soil. Xanthomonas sp. JK311 produced five extracellular proteases that are all metalloproteases. Four of them were resistant against 1% SDS. Chromosomal DNA of the Xanthomonas sp. JK311 was digested with BamHI and cloned into PUC19. Among E. coli strain HB101 transformants, a clone secreting the proteases was screened through halo formation on skim-milk agar plate and by Southern blot analysis. It had the recombinant plasmid pXEP-1 containing the 7.5 kb-BamHI DNA fragment and produced three extacellular proteases. Their protease properties corresponded to those of Xanthomonas sp. JK311.

Partial characterization of proteases from culture filtrate of mycobacterium tuberculosis: Na, Byoung Kuk , Song, Chul Yong , Park, Young Kil , Bai, Gill Han , Ki, Sang Jae; J. Microbiol. 1996;34(2):198-205.

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Abstract: Two proteases were partially characterized from culture filtrate of Mycobacterium, tuberculosis KIT110. Their molecular weights were approximately 200 and 180 kDa, respectively and they exhibited similar enzymatic characteristics. These enzymes were inhibited significantly by EDTA and to some extent by EGTA. Their activity was enhanced by Ca^2+ and Mg^2+ to some degree. However, Cu^2+ and Ag^2+ completely inhibited the enzyme activity at the concentration of 2.5 and 5 mM, respectively. The optimal pH was 7.0 and optimal temperature was around 40℃. These enzymes were rapidly inactivated at 80℃. Therefore, they were heat-labile, neutral metalloproteases. These enzymes exhibited antigenicity shown by their reacting with sera from the partients with pulmonary tuberculosis. These enzymes were able to degrade serum proteins including hemoglobin, bovine serum albumin, lysozyme and immunoglobulin G and structural matrix protein such as type I collagen. Therefore, these enzymes may be thought to contribute to tissue necrosis and pathogenesis during infection.

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