Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoyl is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA. Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-methylbenzoate also act as substrates. Inactive towards 4-aminobenzoate, 4-hydroxybenzoate, 2-aminobenzoate, 2,3-dihydroxybenzoate, 4-coumarate and the aliphatic carboxylic acids palmate, caproate, laurate and butyrate. Negligible activity is detected when ATP is replaced by UTP, CTP or GTP as cosubstrate. 4-chlorobenzoate + ATP + CoA = 4-chlorobenzoyl-CoA + AMP + diphosphate Unaffected by 5,5'-dithiobis-(2-nitrobenzoic acid), 4-chloromercuribenzoate and sodium azide. Inhibited by Cu(2+), Fe(2+) and Zn(2+). Unaffected by Na(+), K(+) and Li(+). Optimum pH is 8.4. 85% of activity remains at pH 9.0, 54% of activity remains at pH 7.0. Optimum temperature is 35 degrees Celsius. Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3. Homodimer. Belongs to the ATP-dependent AMP-binding enzyme family.