Two bacterial strains designated NKC220-2T and NKC851-2
were isolated from commercial kimchi from different areas
in Korea. The strains were Gram-positive, aerobic, oxidaseand
catalase-positive, rod-shaped, spore-forming, non-motile,
and halophilic bacteria. Both strains grew without NaCl,
unlike type species in the genus Lentibacillus. The optimal
pH for growth was 8.0, higher than that of the type species
in the genus Lentibacillus, although growth was observed at
pH 5.5–9.0. 16S rRNA gene sequence-based phylogenetic analysis
indicated that the two strains (99.3–99.9% similarity)
are grouped within the genus Lentibacillus and most closely
related to Lentibacillus juripiscarius IS40-3T (97.4–97.6% similarity)
isolated from fish sauce in Thailand. OrthoANI value
between two novel strains and Lentibacillus lipolyticus SSKP1-
9T (79.5–79.6% similarity) was far lower than the species demarcation
threshold. Comparative genomic analysis displayed
differences between the two strains as well as among other
strains belonging to Lentibacillus. Furthermore, each isolate
had strain-specific groups of orthologous genes based on pangenome
analysis. Genomic G + C contents of strains NKC-
220-2T and NKC851-2 were 41.9 and 42.2 mol%, respectively.
The strains contained meso-diaminopimelic acid in their
cell walls, and the major menaquinone was menaquinone-7.
Phosphatidylglycerol, diphosphatidylglycerol, and an unidentified
glycolipid, aminophospholipid, and phospholipid were
the major polar lipid components of both strains. The major
cellular fatty acids of the strains were anteiso-C15:0 and anteiso-
C17:0. Based on phenotypic, genomic, phylogenetic, and
chemotaxonomic features, strains NKC220-2T and NKC851-2
represent novel species of the genus Lentibacillus, for which
the name Lentibacillus cibarius sp. nov. is proposed. The type
strain is NKC220-2T (= KACC 21232T = JCM 33390T).
Since NAD(H)-dependent L-alanine dehydrogenase (EC
1.1.4.1; Ald) was identified as one of the major antigens present
in culture filtrates of Mycobacterium tuberculosis, many
studies on the enzyme have been conducted. Ald catalyzes
the reversible conversion of pyruvate to alanine with concomitant
oxidation of NADH to NAD+ and has a homohexameric
quaternary structure. Expression of the ald genes was
observed to be strongly upregulated in M. tuberculosis and
Mycobacterium smegmatis grown in the presence of alanine.
Furthermore, expression of the ald genes in some mycobacteria
was observed to increase under respiration-inhibitory
conditions such as oxygen-limiting and nutrient-starvation
conditions. Upregulation of ald expression by alanine or under
respiration-inhibitory conditions is mediated by AldR, a
member of the Lrp/AsnC family of transcriptional regulators.
Mycobacterial Alds were demonstrated to be the enzymes required
for utilization of alanine as a nitrogen source and to
help mycobacteria survive under respiration-inhibitory conditions
by maintaining cellular NADH/NAD+ homeostasis.
Several inhibitors of Ald have been developed, and their application
in combination with respiration-inhibitory antitubercular
drugs such as Q203 and bedaquiline was recently suggested.