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Background  Cellulose is synthesized by an array of bacterial species.  Komagataeibacter xylinus  is the best characterized as it produces copious amounts of the polymer extracellularly. Despite many advances in the past decade, the mechanisms underlying cellulose biosynthesis are not completely understood. Elucidation of these mechanisms is essential for efficient cellulose production in industrial applications.    Results  In an effort to gain a better understanding of cellulose biosynthesis and its regulation, cellulose crystallization was investigated in  K. xylinus  mutants resistant to an inhibitor of cellulose I formation, pellicin. Through the use of forward genetics and site-directed mutagenesis, A449T and A449V mutations in the  K. xylinus  BcsA protein were found to be important for conferring high levels of pellicin resistance. Phenotypic analysis of the  bcsA   A449T   and  bcsA   A449V   cultures revealed that the mutations affect cellulose synthesis rates and that cellulose crystallinity is affected in wet pellicles but not dry ones.    Conclusions  A449 is located in a predicted transmembrane domain of the BcsA protein suggesting that the structure of the transmembrane domain influences cellulose crystallization either by affecting the translocation of the nascent glucan chain or by allosterically altering protein-protein interactions.    Electronic supplementary material  The online version of this article (10.1186/s12866-019-1577-5) contains supplementary material, which is available to authorized users.

Missense mutations in a transmembrane domain of the Komagataeibacter xylinus BcsA lead to changes in cellulose synthesis