The fimA gene of Xanthomonas campestris pv. vesicatoria was identified and characterized. A 20-mer degenerate oligonucleotide complementary to the N-terminal amino acid sequence of the purified 15.5-kDa fimbrillin was used to locate fimA on a 2.6-kb SalI fragment of the X. campestris pv. vesicatoria 3240 genome. The nucleotide sequence of a 1.4-kb fragment containing the fimA region revealed two open reading frames predicting highly homologous proteins FimA and FimB. FimA, which was composed of 136 amino acids and had a calculated molecular weight of 14,302, showed high sequence identity to the type IV fimbrillin precursors. fimB predicted a protein product of 135 amino acids and a molecular weight of 13,854. The open reading frame for fimB contained near the 5 end a palindromic sequence with a terminator loop potential, and the expression level of fimB in vitro and in Xanthomonas was considerably lower than that of fimA. We detected an efficiently transcribed fimA-specific mRNA of 600 bases as well as two weakly expressed, longer mRNA species that reacted with both fimA and fimB. A homolog of fimA but not of fimB was detected by Southern hybridization in strains of X. campestris pv. vesicatoria, campestris, begoniae, translucens, and graminis. A fimA::⍀ mutant of strain 3240 was not significantly reduced in virulence or adhesiveness to tomato leaves. However, the fimA mutant was dramatically reduced in cell aggregation in laboratory cultures and on infected tomato leaves. The fimA mutant strain also exhibited decreased tolerance to UV light.Xanthomonas campestris is a plant pathogen divided into more than 140 pathovars on the basis of the host plants of X. campestris isolates (48). Commonly, the pathovars exhibit a high degree of host specificity in causing the disease, which makes X. campestris infections an interesting target for studies on bacterium-plant interactions and pathogenetic mechanisms of the infections. The ability of X. campestris isolates to cause disease is controlled by hrp (hypersensitive reaction and pathogenicity) genes, whose pathogenetic functions have not yet been characterized. Some of the identified hrp gene products of X. campestris exhibit sequence homology to proteins functioning in secretion of virulence factors of bacteria causing infections in animals (reviewed in reference 5), suggesting that secreted proteins play a role in pathogenesis of X. campestris infections. Isolates of X. campestris secrete plant cell walldegrading enzymes whose function in the pathogenetic processes of X. campestris infections, however, has remained unclear (reviewed in reference 13).In contrast to bacterial infections in mammals, the importance of fimbriae and bacterial adhesion to plant tissue in the pathogenetic processes of plant pathogens has remained controversial (reviewed in references 4 and 34). Fimbriae have been indicated to mediate adhesion of Pseudomonas syringae to bean leaves and to affect the virulence of P. syringae in bean (35). Recently, van Doorn et al. (47) isolated fimbriae from ...