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Int J Syst Evol Microbiol 57 (2007), 1549-1553; DOI  10.1099/ijs.0.65084-0
© 2007 International Union of Microbiological Societies

Alkalimonas collagenimarina sp. nov., a psychrotolerant, obligate alkaliphile isolated from deep-sea sediment

Atsushi Kurata, Masayuki Miyazaki, Tohru Kobayashi, Yuichi Nogi and Koki Horikoshi

Extremobiosphere Research Center of Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima, Yokosuka 237-0061, Japan

Correspondence
Atsushi Kurata
akurata{at}jamstec.go.jp

A psychrotolerant, obligately alkaliphilic, collagenolytic enzyme-producing bacterium, strain AC40T, was isolated from a deep-sea sediment off Torishima Island, Japan, at a depth of 4026 m. Phylogenetic analysis of 16S rRNA gene sequences indicated that this bacterium was closely related to members of the genus Alkalimonas, with highest sequence similarity (97.9 %) to Alkalimonas delamerensis 1E1T. DNA–DNA hybridization experiments of strain AC40T with A. delamerensis 1E1T revealed a level of relatedness of less than 30 %. Cells of strain AC40T were strictly aerobic, rod-shaped, Gram-negative and motile by means of a single polar flagellum. The organism grew over a range of temperatures from 5 to 37 °C and at initial pH values between 7.0 and 10.5. Optimal growth was observed at 33 °C and at pH 8.5–10.0. Cellular fatty acids of strain AC40T were predominantly saturated and mono-unsaturated straight-chain components (C16 : 0 and C18 : 1). The major isoprenoid quinone was Q-8. The G+C content of the DNA was 49.3 mol%. Phylogenetic characteristics, physiological properties and DNA–DNA hybridization data indicate that strain AC40T represents a novel species of the genus Alkalimonas, for which the name Alkalimonas collagenimarina sp. nov. is proposed. The type strain is AC40T (=JCM 14267T=NCIMB 14266T).


The GenBank/EMBL/DDBJ accession number for the 16S rRNA gene sequence of strain AC40T is AB270706.




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Hydrolysis of Insoluble Collagen by Deseasin MCP-01 from Deep-sea Pseudoalteromonas sp. SM9913: COLLAGENOLYTIC CHARACTERS, COLLAGEN-BINDING ABILITY OF C-TERMINAL POLYCYSTIC KIDNEY DISEASE DOMAIN, AND IMPLICATION FOR ITS NOVEL ROLE IN DEEP-SEA SEDIMENTARY PARTICULATE ORGANIC NITROGEN DEGRADATION
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