Table 1. UvrD monomer ssDNA translocation kinetic parameters as a function of ATP concentration.

(T₂₀ buffer, 2.0 mM MgCl₂, and 4 mg/ml heparin at 25°C)

Translocation Kinetic Parameters	ATP (μM)
	10	25	50	75	100	250	500
kt (kinetic steps sec−1)	6.7±0.1	17.5±0.3	27.4±0.5	32.5±0.5	35.9±0.5	40±1	41±1
kd (sec−1)	0.67±0.01	0.75±0.01	0.77±0.02	0.85±0.01	0.85±0.01	0.90±0.02	0.85±0.03
Dissociation from 5′-endA
kc (sec−1) Fluorescein	36±4	20±1	17.8±0.5	17.2±0.4	16.0±0.3	13.7±0.3	13.9±0.3
Cy3	49±7	25±2	26±1	27±1	24±1	25±3	25±3
kend (sec−1) Fluorescein	22±1	6.3±0.3	4.5±0.1	3.7±0.1	3.4±0.1	2.8±0.1	3.0±0.1
Cy3	2±1	3±1	3±2	2.5±1	0.6±0.1	2±1	1.1±0.8
Tryptophan	44±8	34±4	---	---	19±1	---	18±1
ka (ATP UvrD−1 sec−1)	0	10±19	---	---	63±13	---	53±19
c (ATP kinetic-step−1)	5.8±0.1	4.5±0.1	---	---	3.8±0.1	---	4.3±0.1
r	8±1	2.5±0.2	1.9±0.1	1.9±0.1	1.4±0.1	1.4±0.3	1.4±0.3
m (nts kinetic-step−1)	7.2±0.2	5.2±0.1	4.7±0.1	4.5±0.1	4.5±0.1	4.6±0.2	4.8±0.2
d (contact size, nts)	7.3±0.8	9.6±0.4	10.2±0.3	10.1±0.4	9.6±0.3	9.5±0.7	9.3±0.7
c/m (ATP nt−1)	0.81±0.04	0.87±0.04	---	---	0.84±0.04	---	0.89±0.06
mkt (nts sec−1)B	48.8±0.6	90.9±0.7	129±1	148±1	160±1	186±1	199±1
1/(1−P) (nts)	74±1	122±1	168±1	174±1	189±1	207±1	241±1

^ADissociation from the 5′-end in the translocation assay is fluorophore dependent and is a two step process defined by k_c and k_end. In the absence of fluorophore dissociation from the 5′-end can be modeled as a single step (k_end, Tryptophan, see Figure S5).

^BMacroscopic translocation rate.

P Is the translocation processivity where $P=\frac{{mk}_t}{{mk}_t+k_d}$ (in nucleotide units). 1/(1−P) is the average number of nucleotides translocated before dissociation from the ssDNA under the experimental conditions.

The reported error represents ± 1 σ determined from a 100 cycle Monte Carlo simulation