TABLE 3.

Amino acids substitutions in AdeRS two component system in fluoroquinolone-resistant Acinetobacter baumannii isolates overexpressing AdeABC efflux pump.

		Amino acid at the indicated position*
		AdeS (360 aa)						AdeR (247 aa)
Different mutational patterns in AdeRS (No. of isolates in each pattern)	Isolate numbers (MLST/CC)	HAMP (82−138)	DHp (138−246)		CA (246−360)			REC (1−140)	Output domain (141−247)
		121	186	188	255	257	322	132	175	227	228
		E	G	S	V	I	L	F	I	L	I
Type 1 (n = 1)	A_112 (ST-32/CC32)				I				L	I
Type 2 (n = 1)	A_113 (ST-32/CC32)			F						I
Type 3 (n = 1)	A_124 (ST-1440/CC218)		V								V
Type 4 (n = 1)	A_138 (ST-905/CC32)		V		I				L
Type 5 (n = 1)	A_166 (ST-625/CC513)					V		S
Type 6 (n = 1)	A_146 (ST-1406/CC10)	K						No amino acid substitutions
Type 7 (n = 2)	A_136 (ST-149/CC149), A_149 (ST_149/CC149)			F	I			No amino acid substitutions
Type 8 (n = 7)	A_125 (ST-2/CC2), A_162 (ST-1406/CC10), A_163 (ST-575/CC10), A_167 (ST-2/CC2), A_172 (ST-526/CC2), A_173 (ST-526/CC2), A_179 (ST-7/CC1)		V					No amino acid substitutions
Type 9 (n = 1)	A_161 (ST-149/CC149)				I			No amino acid substitutions
Type 10 (n = 2)	A_131 (ST-902/CC1), A_158 (ST-1483/CC10)			F	I			No amino acid substitutions
Type 11 (n = 1)	A_145 (ST-149/CC149)			F	I		F	No amino acid substitutions
Type 12 (n = 1)	A_155 (ST-10/CC10)	K					F	No amino acid substitutions

aa, amino acids; CA, catalytic and ATP-binding domain; DHp, dimerization and histidine-containing phosphotransfer domain; HAMP, histidine kinase, adenylylcyclase, methyl-accepting protein, and phosphatase linker domain; REC, receiver domain; CC, Clonal Complex. * The AdeR and AdeS amino acid sequences of A. baumannii ACICU, A. baumannii AYE, ATCC 17978, and ATCC 19606 were used as reference strains for comparison. Amino acid substitutions are indicated using the one-letter code.