SitesBLAST

276 C→A: Lower ATPase activity and transport efficiency.
297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.

8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
28% identity, 44% coverage: 7:236/525 of query aligns to 3:220/358 of 8y5iA

query
sites
8y5iA

I

V

Q

Q

L

L

S

A

G

G

V

I

S

R

K

K

S

C

F
|
F

D

D

G

G

F
x
K

M

E

A

V

L

I

S

P

Q

Q

A

L

D

D

F

L

T

T

A

I

R

N

W

N

G

G

E

E

V

F

H

L

A

T

L

L

G

G

E

P

N

S

G
|
G

A

C

G

G

K
|
K

S
x
T

L

V

M

L

N

R

I

L

A

I

A

A

G

G

L

L

Y

E

A

T

P

V

E

D

S

S

G

G

S

R

L

I

L

M

I

L

N

-

D

D

N

N

A

E

V

D

R

I

L

T

S

H

G

V

P

P

R

-

D

-

A

A

S

E

R

N

Y

R

H

Y

I

V

G

N

M

T

V

V

H

F

Q

Q

H

S

F

Y

K

A

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

F

E

E

N

N

I

V

Q

A

L

F

A

G

L

L

P

-

E

-

G

-

P

-

G

-

N

-

H

-

A

-

F

-

S

-

G

R

S

M

H

Q

R

K

Q

T

R

P

L

A

A

A

A

E

L

I

E

T

Q

P

R

R

I

V

S

M

D

E

K

A

A

L

A

R

E

M

L

V

G

Q

F

L

S

E

I

T

D

F

P

A

R

Q

K
x
R

I

K

T

P

E

H

S
x
Q

L

L

S
|
S

V

G

A

G

E

Q

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

V

A

N

G

K

A

P

R

R

I

L

L

L

I

L

L

L

D

D

E

Q

P

S

T

L

A

S

V

A

L

L

T

D

D

Y

G

K

E

L

A

R

E

K

R

Q

L

M

L

Q

E

N

T

E

V

L

R

K

A

A

F

L

A

Q

R

R

Q

K

-

L

G

G

A

I

A

T

V

F

I

V

L

F

V

V

T

T

H

H

K

D

M

Q

S

E

D

E

V

A

K

L

R

T

F

M

A

S

D

D

R

R

V

I

T

V

V

V

M

M

R

R

G

D

G

G

R

R

T

I

I

E

Q

Q

T

D

L

G

D

T

P

P

Q

R

T

E

V

I

binding adenosine-5'-triphosphate: F12 (= F16), K15 (≠ F19), G38 (= G42), K41 (= K45), T42 (≠ S46), T43 (≠ S47), R128 (≠ K145), Q132 (≠ S149), S134 (= S151)

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 42% coverage: 7:229/525 of query aligns to 2:221/343 of P30750

query
sites
P30750

I

I

Q

K

L

L

S

S

G

N

V

I

S

T

K

K

S

V

F

F

D

H

-

Q

-

G

-

T

-

R

G

T

F

I

M

Q

A

A

L

L

S

N

Q

N

A

V

D

S

F

L

T

H

A

V

R

P

W

A

G

G

E

Q

V

I

H

Y

A

G

L

V

L

I

G

G

E

A

N
x
S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

I

N

R

I

C

A

V

A

N

G

L

L

L

Y

E

A

R

P

P

E

T

S

E

G

G

S

S

L

V

L

L

I

V

N

D

D

G

N

Q

A

E

V

L

R

T

L

T

S

L

G

S

P

E

R

S

D

E

A

L

S

T

-

K

-

A

R

R

Y

R

H

Q

I

I

G

G

M

M

V

I

H

F

Q

Q

H

H

F

F

K

N

L

L

V

L

K

S

P

S

F

R

T

T

V

V

A

F

E

G

N

N

I

V

Q

-

L

-

A

A

L

L

P

P

E

L

G

E

P

L

G

D

N

N

H

T

A

P

F

K

S

D

G

E

S

V

H

K

R

R

Q

-

R

-

L

-

A

-

L

-

E

-

Q

-

R

R

I

V

S

T

D

E

K

L

A

L

A

S

E

L

L

V

G

G

F

L

S

G

I

D

D

K

P

H

R

D

K

S

I

Y

T

P

E

S

S

N

L

L

S

S

V

G

A

G

E

Q

Q

K

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

S

G

N

A

P

R

K

I

V

L

L

I

L

L

C

D

D

E
|
E

P

A

T

T

A

S

V

A

L

L

T

D

D

P

G

A

E

T

A

T

E

R

R

S

L

I

L

L

E

E

T

L

V

L

R

K

A

D

F

I

A

N

R

R

Q

R

-

L

G

G

A

L

A

T

V

I

I

L

L

L

V

I

T

T

H

H

K

E

M

M

S

D

D

V

V

V

K

K

R

R

F

I

A

C

D

D

R

C

V

V

T

A

V

V

M

I

R

S

G

N

G

G

R

E

T

L

I

I

Q

E

40:46 (vs. 41:47, 71% identical) binding ATP
E166 (= E175) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

278:283 binding L-methionine
295 N→A: Reduces the binding of L-methionine to undetectable levels.
295:296 binding L-methionine

3d31A Modbc from methanosarcina acetivorans (see paper)
26% identity, 44% coverage: 7:236/525 of query aligns to 2:215/348 of 3d31A

query
sites
3d31A

I

I

Q

E

L

I

S

E

G

S

V

L

S

S

K

R

S

K

F

W

D

K

G

N

F

F

M

-

A

S

L

L

S

D

Q

N

A

L

D

S

F

L

T

K

A

V

R

E

W

S

G

G

E

E

V

Y

H

F

A

V

L

I

L

L

G

G

E

P

N

T

G

G

A

A

G

G

K

K

S

T

S

L

L

F

M

L

N

E

I

L

A

I

A

A

G

G

L

F

Y

H

A

V

P

P

E

D

S

S

G

G

S

R

L

I

L

L

I

L

N

D

D

G

N

K

A

D

V

V

R

T

L

D

S

L

G

S

P

P

R

-

D

-

A

-

S

E

R

K

Y

H

H

D

I

I

G

A

M

F

V

V

H

Y

Q

Q

H

N

F

Y

K

S

L

L

V

F

K

P

P

H

F

M

T

N

V

V

A

K

E

K

N

N

I

L

Q

E

L

F

A

G

L

M

P

-

E

-

G

-

P

-

G

-

N

-

H

-

A

-

F

-

S

-

G

-

S

-

H

-

R

R

Q

M

R

K

L

K

A

I

A

K

L

D

E

P

Q

K

R

R

I

V

S

L

D

D

K

T

A

A

A

R

E

D

L

L

G

K

F

I

S

E

-

H

-

L

I

L

D

D

P

R

R

N

K

P

I

L

T

T

E

-

S

-

L

L

S

S

V

G

A

G

E

E

Q

Q

R

R

V

V

E

A

I

L

L

A

K

R

V

A

L

L

L

V

A

T

G

N

A

P

R

K

I

I

L

L

I

L

L

L

D

D

E

E

P

P

T

L

A

S

V

A

L

L

T

D

D

P

G

R

E

T

A

Q

E

E

R

N

L

A

L

R

E

E

T

M

V

L

R

S

A

V

F

L

A

H

R

K

Q

K

G

N

A

K

A

L

V

T

I

V

L

L

-

H

V

I

T

T

H

H

K

D

M

Q

S

T

D

E

V

A

K

R

R

I

F

M

A

A

D

D

R

R

V

I

T

A

V

V

M

V

R

M

G

D

G

G

R

K

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L

I

I

Q

Q

T

V

L

G

D

K

P

P

Q

E

T

E

V

I

Sites not aligning to the query:

binding tungstate(vi)ion: 286, 320, 323, 340, 341, 342

4u00A Crystal structure of ttha1159 in complex with adp (see paper)
28% identity, 44% coverage: 7:236/525 of query aligns to 3:223/241 of 4u00A

query
sites
4u00A

I

I

Q

R

L

I

S

R

G

N

V

L

S

H

K

K

S

W

F
|
F

D

G

G

P

F

L

M

H

A
x
V

L

L

S

K

Q

G

A

I

D

H

F

L

T

E

A

V

R

A

W

P

G

G

E

E

V

K

H

L

A

V

L

I

G

G

E

P

N
x
S

G
|
G

A
x
S

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

I

N

R

I

T

A

I

A

N

G

R

L

L

Y

E

A

D

P

F

E

Q

S

E

G

G

S

E

L

V

I

V

N

D

D

G

N

L

A

S

V

V

R

K

L

D

S

D

G

R

P

A

R

L

D

R

A

E

S

I

R

R

Y

R

H

E

I

V

G

G

M

M

V

V

H

F

Q

Q

H

Q

F

F

K

N

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

L

E

E

N

N

I

V

Q

T

L

L

A

A

L

-

P

P

E

M

G

R

P

V

G

R

N

R

H

W

A

P

F

R

S

E

G

K

S

A

H

E

R

K

Q

K

R

A

L

L

A

E

A

L

L

L

E

E

Q

R

R

-

I

-

S

-

D

-

K

-

A

-

E

-

L

V

G

G

F

I

S

L

I

D

D

Q

P

A

R

R

K

K

I

Y

T

P

E

A

S

Q

L

L

S

S

V

G

A

G

E

Q

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

E

A

P

R

K

I

I

L

M

I

L

L

F

D

D

E

E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

G

R

E

L

V

L

L

E

D

T

V

V

M

R

R

A

D

F

L

A

A

R

Q

Q

G

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H

H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

A

D

D

R

R

V

V

T

V

V

F

M

M

R

D

G

G

R

Q

T

I

I

V

Q

E

T

E

L

G

D

R

P

P

Q

E

T

E

V

I

binding adenosine-5'-diphosphate: F12 (= F16), V17 (≠ A21), S37 (≠ N41), G38 (= G42), S39 (≠ A43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (≠ S47)

6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
28% identity, 43% coverage: 5:229/525 of query aligns to 1:222/344 of 6cvlD

query
sites
6cvlD

N

H

A

M

I

I

Q

K

L

L

S

S

G

N

V

I

S

T

K

K

S

V

F
|
F

D

H

-
x
Q

-

G

-

T

-

R

G

T

F
x
I

M

Q

A

A

L

L

S

N

Q

N

A

V

D

S

F

L

T

H

A

V

R

P

W

A

G

G

E

Q

V

I

H

Y

A

G

L

V

L

I

G

G

E

A

N
x
S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

I

N

R

I

C

A

V

A

N

G

L

L

L

Y

E

A

R

P

P

E

T

S

E

G

G

S

S

L

V

L

L

I

V

N

D

D

G

N

Q

A

E

V

L

R

T

L

T

S

L

G

S

P

E

R

S

D

E

A

L

S

T

-

K

-

A

R

R

Y

R

H

Q

I

I

G

G

M

M

V

I

H

F

Q

Q

H

H

F

F

K

N

L

L

V

L

K

S

P

S

F

R

T

T

V

V

A

F

E

G

N

N

I

V

Q

-

L

-

A

A

L

L

P

P

E

L

G

E

P

L

G

D

N

N

H

T

A

P

F

K

S

D

G

E

S

V

H

K

R

R

Q

-

R

-

L

-

A

-

L

-

E

-

Q

-

R

R

I

V

S

T

D

E

K

L

A

L

A

S

E

L

L

V

G

G

F

L

S

G

I

D

D

K

P

H

R

D

K

S

I

Y

T

P

E

S

S
x
N

L

L

S
|
S

V

G

A

G

E
x
Q

Q

K

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

S

G

N

A

P

R

K

I

V

L

L

I

L

L

C

D

D

E

Q

P

A

T

T

A

S

V

A

L

L

T

D

D

P

G

A

E

T

A

T

E

R

R

S

L

I

L

L

E

E

T

L

V

L

R

K

A

D

F

I

A

N

R

R

Q

R

-

L

G

G

A

L

A

T

V

I

I

L

L

L

V

I

T

T

H
|
H

K

E

M

M

S

D

D

V

V

V

K

K

R

R

F

I

A

C

D

D

R

C

V

V

T

A

V

V

M

I

R

S

G

N

G

G

R

E

T

L

I

I

Q

E

binding phosphothiophosphoric acid-adenylate ester: F12 (= F16), Q14 (vs. gap), I19 (≠ F19), S41 (≠ N41), G42 (= G42), A43 (= A43), G44 (= G44), K45 (= K45), S46 (= S46), T47 (≠ S47), N141 (≠ S149), S143 (= S151), Q146 (≠ E154), H200 (= H207)

3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
27% identity, 43% coverage: 5:229/525 of query aligns to 1:222/344 of 3tuzC

query
sites
3tuzC

N

H

A

M

I

I

Q

K

L

L

S

S

G

N

V

I

S

T

K

K

S

V

F
|
F

D

H

-
x
Q

-

G

-

T

-

R

G

T

F

I

M

Q

A

A

L

L

S

N

Q

N

A

V

D

S

F

L

T

H

A

V

R

P

W

A

G

G

E

Q

V

I

H

Y

A

G

L

V

L

I

G

G

E

A

N

S

G
|
G

A

A

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

I

N

R

I

C

A

V

A

N

G

L

L

L

Y

E

A

R

P

P

E

T

S

E

G

G

S

S

L

V

L

L

I

V

N

D

D

G

N

Q

A

E

V

L

R

T

L

T

S

L

G

S

P

E

R

S

D

E

A

L

S

T

-

K

-

A

R

R

Y

R

H

Q

I

I

G

G

M

M

V

I

H

F

Q

Q

H

H

F

F

K

N

L

L

V

L

K

S

P

S

F

R

T

T

V

V

A

F

E

G

N

N

I

V

Q

A

L

L

A

P

L

L

P

E

-

L

-

D

E

N

G

T

P

P

G

K

N

D

H

E

A

-

F

-

S

-

G

-

S

-

H

-

R

-

Q

-

R

-

L

-

A

-

L

V

E

K

Q

R

R

R

I

V

S

T

D

E

K

L

A

L

A

S

E

L

L

V

G

G

F

L

S

G

I

D

D

K

P

H

R

D

K

S

I

Y

T

P

E

S

S

N

L

L

S

S

V

G

A

G

E

Q

Q

K

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

S

G

N

A

P

R

K

I

V

L

L

I

L

L

C

D

D

E

Q

P

A

T

T

A

S

V

A

L

L

T

D

D

P

G

A

E

T

A

T

E

R

R

S

L

I

L

L

E

E

T

L

V

L

R

K

A

D

F

I

A

N

R

R

Q

R

-

L

G

G

A

L

A

T

V

I

I

L

L

L

V

I

T

T

H

H

K

E

M

M

S

D

D

V

V

V

K

K

R

R

F

I

A

C

D

D

R

C

V

V

T

A

V

V

M

I

R

S

G

N

G

G

R

E

T

L

I

I

Q

E

binding adenosine-5'-diphosphate: F12 (= F16), Q14 (vs. gap), G42 (= G42), G44 (= G44), K45 (= K45), S46 (= S46), T47 (≠ S47)

Sites not aligning to the query:

binding selenomethionine: 274, 279, 281, 282, 283, 284, 311, 313

3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
27% identity, 43% coverage: 5:229/525 of query aligns to 1:222/344 of 3tuiC

query
sites
3tuiC

N

H

A

M

I

I

Q

K

L

L

S

S

G

N

V

I

S

T

K

K

S

V

F
|
F

D

H

-

Q

-

G

-

T

-

R

G

T

F

I

M

Q

A

A

L

L

S

N

Q

N

A

V

D

S

F

L

T

H

A

V

R

P

W

A

G

G

E

Q

V

I

H

Y

A

G

L

V

L

I

G

G

E

A

N

S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

I

N

R

I

C

A

V

A

N

G

L

L

L

Y

E

A

R

P

P

E

T

S

E

G

G

S

S

L

V

L

L

I

V

N

D

D

G

N

Q

A

E

V

L

R

T

L

T

S

L

G

S

P

E

R

S

D

E

A

L

S

T

-

K

-

A

R

R

Y

R

H

Q

I

I

G

G

M

M

V

I

H

F

Q

Q

H

H

F

F

K

N

L

L

V

L

K

S

P

S

F

R

T

T

V

V

A

F

E

G

N

N

I

V

Q

A

L

L

A

P

L

L

P

E

-

L

-

D

E

N

G

T

P

P

G

K

N

D

H

E

A

-

F

-

S

-

G

-

S

-

H

-

R

-

Q

-

R

-

L

-

A

-

L

V

E

K

Q

R

R

R

I

V

S

T

D

E

K

L

A

L

A

S

E

L

L

V

G

G

F

L

S

G

I

D

D

K

P

H

R

D

K

S

I

Y

T

P

E

S

S

N

L

L

S

S

V

G

A

G

E

Q

Q

K

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

S

G

N

A

P

R

K

I

V

L

L

I

L

L

C

D

D

E

Q

P

A

T

T

A

S

V

A

L

L

T

D

D

P

G

A

E

T

A

T

E

R

R

S

L

I

L

L

E

E

T

L

V

L

R

K

A

D

F

I

A

N

R

R

Q

R

-

L

G

G

A

L

A

T

V

I

I

L

L

L

V

I

T

T

H

H

K

E

M

M

S

D

D

V

V

V

K

K

R

R

F

I

A

C

D

D

R

C

V

V

T

A

V

V

M

I

R

S

G

N

G

G

R

E

T

L

I

I

Q

E

binding adenosine-5'-diphosphate: F12 (= F16), G42 (= G42), A43 (= A43), G44 (= G44), K45 (= K45), S46 (= S46), T47 (≠ S47)

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
29% identity, 44% coverage: 4:233/525 of query aligns to 1:218/369 of P19566

query
sites
P19566

L

M

N

A

A

S

I

V

Q

Q

L

L

S

R

G

N

V

V

S

T

K

K

S

A

F

W

D

G

G

D

F

V

M

V

A

V

L

S

S

K

Q

D

A

I

D

N

F

L

T

D

A

I

R

H

W

D

G

G

E

E

V

F

H

V

A

V

L

F

L

V

G

G

E

P

N

S

G

G

A

C

G

G

K

K

S

S

S

T

L

L

M

L

N

R

I

M

A

I

A

A

G

G

L

L

Y

E

A

T

P

I

E

T

S

S

G

G

S

D

L

L

L

F

I

I

N

G

D

E

N

T

A

-

V

-

R

R

L

M

S

N

G

D

P

I

R

P

D

P

A

A

S

E

R

R

Y

-

H

G

I

V

G

G

M

M

V

V

H

F

Q

Q

H

S

F

Y

K

A

L
|
L

V

Y

K

P

P

H

F

L

T

S

V

V

A

A

E

E

N

N

I

M

Q

S

L

F

A

G

L

L

P

-

E

-

G

-

P

-

G

-

N

-

H

-

A

K

F

L

S

A

G

G

S

A

H

K

R

K

Q

E

R

-

L

-

A

-

A

V

L

M

E

N

Q

Q

R

R

I

V

S

N

D

Q

K

V

A

A

A

E

E

V

L

L

G

Q

F

L

S

A

I

H

D

L

P

L

R

E

K

R

I

K

T

P

E

K

S

A

L

L

S

S

V

G

A

G

E

Q

Q

R

Q

Q

R

R

V

V

E

A

I

I

L

G

K

R

V

T

L

L

L

V

A

A

G

E

A

P

R

R

I

V

L

F

I

L

L

L

D

D

E

E

P
|
P

T

L

A

S

V

N

L

L

T
x
D

D

A

G

A

-

L

E

R

A

V

E

Q

R

M

L

R

L

I

E

E

T

I

V

S

R

R

A

L

F

H

A

K

R

R

Q

L

G

G

A

R

A

T

V

M

I

I

L

Y

V

V

T

T

H

H

K

D

M

Q

S

V

D

E

V

A

K

M

R

T

F

L

A

A

D

D

R

K

V

I

T

V

V

V

M

L

R

D

G

A

G

G

R

R

T

V

I

A

Q

Q

T

V

L

G

D

K

P

P

L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
D165 (≠ T181) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.

Sites not aligning to the query:

306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.

4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
27% identity, 44% coverage: 7:236/525 of query aligns to 2:223/240 of 4ymuJ

query
sites
4ymuJ

I

I

Q

F

L

V

S

N

G

D

V

V

S

Y

K

K

S

N

F
|
F

D

G

G

S

F

L

M

E

A
x
V

L

L

S

K

Q

G

A

V

D

T

F

L

T

K

A

V

R

N

W

K

G

G

E

E

V

V

H

V

A

V

L

I

G

G

E

P

N
x
S

G
|
G

A
x
S

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

L

N

R

I

C

A

I

A

N

G

L

L

L

Y

E

A

E

P

P

E

T

S

K

G

G

S

E

L

V

L

F

I

I

N

D

D

-

N

-

A

G

V

V

R

K

L

I

S

N

G

N

P

G

R

K

-

V

-

N

-

I

D

N

A

K

S

V

R

R

Y

Q

H

K

I

V

G

G

M

M

V

V

H

F

Q

Q

H

H

F

F

K

N

L

L

V

F

K

P

P

H

F

L

T

T

V

A

A

I

E

E

N

N

I

I

Q

T

L

L

A

A

L

-

P

-

E

-

G

-

P

P

G

-

N

-

H

-

A

-

F

-

S

V

G

K

S

V

H

K

R

K

Q

M

R

N

L

K

A

K

A

E

L

A

E

E

Q

E

R

L

I

A

S

V

D

D

K

L

A

L

A

A

E

K

L

V

G

G

F

L

S

L

I

D

D

K

P

K

R

D

K

Q

I

Y

T

P

E

I

S

K

L

L

S

S

V

G

A

G

E

Q

Q

K

Q

Q

R

R

V

L

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

Q

A

P

R

E

I

V

L

M

I

L

L

F

D

D

E
|
E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

K

R

E

L

V

L

L

E

N

T

V

V

M

R

K

A

Q

F

L

A

A

R

N

Q

E

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H
|
H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

G

D

D

R

R

V

V

T

I

V

F

M

M

R

D

G

D

G

G

R

V

T

I

I

V

Q

E

T

E

L

G

D

T

P

P

Q

E

T

E

V

I

binding adenosine-5'-triphosphate: F11 (= F16), V16 (≠ A21), S36 (≠ N41), G37 (= G42), S38 (≠ A43), G39 (= G44), K40 (= K45), S41 (= S46), T42 (≠ S47), E162 (= E175), H194 (= H207)
binding magnesium ion: S41 (= S46), E162 (= E175)

3c4jA Abc protein artp in complex with atp-gamma-s
28% identity, 44% coverage: 4:236/525 of query aligns to 1:225/242 of 3c4jA

query
sites
3c4jA

L

L

N

Q

A

M

I

I

Q

D

L

V

S

H

G

Q

V

L

S

K

K

K

S

S

F
|
F

D

G

G

S

F

L

M

E

A
x
V

L

L

S

K

Q

G

A

I

D

N

F

V

T

H

A

I

R

R

W

E

G

G

E

E

V

V

H

V

A

V

L

V

L

I

G

G

E

P

N
x
S

G
|
G

A
x
S

G
|
G

K
|
K

S
|
S

S
x
T

L

F

M

L

N

R

I

C

A

L

A

N

G

L

L

L

Y

E

A

D

P

F

E

D

S

E

G

G

S

E

L

I

I

I

N

D

D

G

N

I

A

N

V

L

R

K

L

A

S

K

G

D

P

T

R

N

-

L

D

N

A

K

S

V

R

R

Y

E

H

E

I

V

G

G

M

M

V

V

H

F

Q

Q

H

R

F

F

K

N

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

L

E

N

N

N

I

I

Q

T

L

L

A

A

L

-

P

-

E

-

G

-

P

-

G

-

N

P

H

M

A

K

F

V

S

R

G

K

S

W

H

P

R

R

Q

E

R

K

L

A

A

E

A

A

L

K

E

A

Q

M

R

E

I

L

S

L

D

D

K

K

A

-

E

-

L

V

G

G

F

L

S

K

I

D

D

K

P

A

R

H

K

A

I

Y

T

P

E

D

S

S

L

L

S

S

V

G

A

G

E

Q

Q

A

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

E

A

P

R

K

I

I

L

M

I

L

L

F

D

D

E

E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

G

R

E

L

V

L

L

E

S

T

V

V

M

R

K

A

Q

F

L

A

A

R

N

Q

E

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H

H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

G

D

D

R

R

V

V

T

L

V

F

M

M

R

D

G

G

R

Y

T

I

I

I

Q

E

T

E

L

G

D

K

P

P

Q

E

T

D

V

L

binding phosphothiophosphoric acid-adenylate ester: F13 (= F16), V18 (≠ A21), S38 (≠ N41), G39 (= G42), S40 (≠ A43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (≠ S47)

3c41J Abc protein artp in complex with amp-pnp/mg2+
28% identity, 44% coverage: 4:236/525 of query aligns to 1:225/242 of 3c41J

query
sites
3c41J

L

L

N

Q

A

M

I

I

Q

D

L

V

S

H

G

Q

V

L

S

K

K

K

S

S

F
|
F

D

G

G

S

F

L

M

E

A
x
V

L

L

S

K

Q

G

A

I

D

N

F

V

T

H

A

I

R

R

W

E

G

G

E

E

V

V

H

V

A

V

L

V

L

I

G

G

E

P

N
x
S

G
|
G

A

S

G
|
G

K
|
K

S
|
S

S
x
T

L

F

M

L

N

R

I

C

A

L

A

N

G

L

L

L

Y

E

A

D

P

F

E

D

S

E

G

G

S

E

L

I

I

I

N

D

D

G

N

I

A

N

V

L

R

K

L

A

S

K

G

D

P

T

R

N

-

L

D

N

A

K

S

V

R

R

Y

E

H

E

I

V

G

G

M

M

V

V

H

F

Q

Q

H

R

F

F

K

N

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

L

E

N

N

N

I

I

Q

T

L

L

A

A

L

-

P

-

E

-

G

-

P

-

G

-

N

P

H

M

A

K

F

V

S

R

G

K

S

W

H

P

R

R

Q

E

R

K

L

A

A

E

A

A

L

K

E

A

Q

M

R

E

I

L

S

L

D

D

K

K

A

-

E

-

L

V

G

G

F

L

S

K

I

D

D

K

P

A

R

H

K

A

I

Y

T

P

E

D

S

S

L

L

S

S

V

G

A

G

E

Q

Q

A

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

E

A

P

R

K

I

I

L

M

I

L

L

F

D
|
D

E

E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

G

R

E

L

V

L

L

E

S

T

V

V

M

R

K

A

Q

F

L

A

A

R

N

Q

E

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H

H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

G

D

D

R

R

V

V

T

L

V

F

M

M

R

D

G

G

R

Y

T

I

I

I

Q

E

T

E

L

G

D

K

P

P

Q

E

T

D

V

L

binding phosphoaminophosphonic acid-adenylate ester: F13 (= F16), V18 (≠ A21), S38 (≠ N41), G39 (= G42), G41 (= G44), K42 (= K45), S43 (= S46), T44 (≠ S47)
binding magnesium ion: S43 (= S46), D163 (= D174)

2olkA Abc protein artp in complex with adp-beta-s
28% identity, 44% coverage: 4:236/525 of query aligns to 1:225/242 of 2olkA

query
sites
2olkA

L

L

N

Q

A

M

I

I

Q

D

L

V

S

H

G

Q

V

L

S

K

K

K

S

S

F
|
F

D

G

G

S

F

L

M

E

A
x
V

L

L

S

K

Q

G

A

I

D

N

F

V

T

H

A

I

R

R

W

E

G

G

E

E

V

V

H

V

A

V

L

V

L

I

G

G

E

P

N
x
S

G
|
G

A
x
S

G
|
G

K
|
K

S
|
S

S
x
T

L

F

M

L

N

R

I

C

A

L

A

N

G

L

L

L

Y

E

A

D

P

F

E

D

S

E

G

G

S

E

L

I

I

I

N

D

D

G

N

I

A

N

V

L

R

K

L

A

S

K

G

D

P

T

R

N

-

L

D

N

A

K

S

V

R

R

Y

E

H

E

I

V

G

G

M

M

V

V

H

F

Q

Q

H

R

F

F

K

N

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

L

E

N

N

N

I

I

Q

T

L

L

A

A

L

-

P

-

E

-

G

-

P

-

G

-

N

P

H

M

A

K

F

V

S

R

G

K

S

W

H

P

R

R

Q

E

R

K

L

A

A

E

A

A

L

K

E

A

Q

M

R

E

I

L

S

L

D

D

K

K

A

-

E

-

L

V

G

G

F

L

S

K

I

D

D

K

P

A

R

H

K

A

I

Y

T

P

E

D

S

S

L

L

S

S

V

G

A

G

E

Q

Q

A

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

E

A

P

R

K

I

I

L

M

I

L

L

F

D

D

E

E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

G

R

E

L

V

L

L

E

S

T

V

V

M

R

K

A

Q

F

L

A

A

R

N

Q

E

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H

H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

G

D

D

R

R

V

V

T

L

V

F

M

M

R

D

G

G

R

Y

T

I

I

I

Q

E

T

E

L

G

D

K

P

P

Q

E

T

D

V

L

binding 5'-o-[(r)-hydroxy(thiophosphonooxy)phosphoryl]adenosine: F13 (= F16), V18 (≠ A21), S38 (≠ N41), G39 (= G42), S40 (≠ A43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (≠ S47)

2oljA Abc protein artp in complex with adp/mg2+
28% identity, 44% coverage: 4:236/525 of query aligns to 1:225/242 of 2oljA

query
sites
2oljA

L

L

N

Q

A

M

I

I

Q

D

L

V

S

H

G

Q

V

L

S

K

K

K

S

S

F
|
F

D

G

G

S

F

L

M

E

A
x
V

L

L

S

K

Q

G

A

I

D

N

F

V

T

H

A

I

R

R

W

E

G

G

E

E

V

V

H

V

A

V

L

V

L

I

G

G

E

P

N
x
S

G
|
G

A
x
S

G
|
G

K
|
K

S
|
S

S
x
T

L

F

M

L

N

R

I

C

A

L

A

N

G

L

L

L

Y

E

A

D

P

F

E

D

S

E

G

G

S

E

L

I

I

I

N

D

D

G

N

I

A

N

V

L

R

K

L

A

S

K

G

D

P

T

R

N

-

L

D

N

A

K

S

V

R

R

Y

E

H

E

I

V

G

G

M

M

V

V

H

F

Q

Q

H

R

F

F

K

N

L

L

V

F

K

P

P

H

F

M

T

T

V

V

A

L

E

N

N

N

I

I

Q

T

L

L

A

A

L

-

P

-

E

-

G

-

P

-

G

-

N

P

H

M

A

K

F

V

S

R

G

K

S

W

H

P

R

R

Q

E

R

K

L

A

A

E

A

A

L

K

E

A

Q

M

R

E

I

L

S

L

D

D

K

K

A

-

E

-

L

V

G

G

F

L

S

K

I

D

D

K

P

A

R

H

K

A

I

Y

T

P

E

D

S

S

L

L

S

S

V

G

A

G

E

Q

Q

A

Q

Q

R

R

V

V

E

A

I

I

L

A

K

R

V

A

L

L

L

A

A

M

G

E

A

P

R

K

I

I

L

M

I

L

L

F

D

D

E

E

P

P

T

T

A

S

V

A

L

L

T

D

D

P

G

E

E

M

A

V

E

G

R

E

L

V

L

L

E

S

T

V

V

M

R

K

A

Q

F

L

A

A

R

N

Q

E

G

G

A

M

A

T

V

M

I

V

L

V

V

V

T

T

H

H

K

E

M

M

S

G

D

F

V

A

K

R

R

E

F

V

A

G

D

D

R

R

V

V

T

L

V

F

M

M

R

D

G

G

R

Y

T

I

I

I

Q

E

T

E

L

G

D

K

P

P

Q

E

T

D

V

L

binding adenosine-5'-diphosphate: F13 (= F16), V18 (≠ A21), S38 (≠ N41), G39 (= G42), S40 (≠ A43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (≠ S47)

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
27% identity, 44% coverage: 4:233/525 of query aligns to 1:218/371 of P68187

query
sites
P68187

L

M

N

A

A

S

I

V

Q

Q

L

L

S

Q

G

N

V

V

S

T

K

K

S

A

F

W

D

G

G

E

F

V

M

V

A

V

L

S

S

K

Q

D

A

I

D

N

F

L

T

D

A

I

R

H

W

E

G

G

E

E

V

F

H

V

A

V

L

F

L

V

G

G

E

P

N

S

G

G

A

C

G

G

K

K

S

S

S

T

L

L

M

L

N

R

I

M

A

I

A

A

G

G

L

L

Y

E

A

T

P

I

E

T

S

S

G

G

S

D

L

L

L

F

I

I

N

G

D

E

N

K

A

R

V

M

R

N

L

D

S

T

G

P

P

P

R

A

D

E

A

R

S

G

R

-

Y

-

H

-

I

V

G

G

M

M

V

V

H

F

Q

Q

H

S

F

Y

K
x
A

L

L

V

Y

K

P

P

H

F

L

T

S

V

V

A

A

E

E

N

N

I

M

Q

S

L

F

A

G

L

L

P

-

E

-

G

-

P

-

G

-

N

-

H

-

A

K

F

L

S

A

G

G

S

A

H
x
K

R

K

Q

E

R

-

L

-

A

-

A

V

L

I

E

N

Q

Q

R

R

I
x
V

S

N

D

Q

K
x
V

A

A

A
x
E

E

V

L

L

G

Q

F

L

S
x
A

I

H

D

L

P

L

R

D

K

R

I

K

T

P

E

K

S

A

L

L

S

S

V

G

A
x
G

E

Q

Q

R

Q

Q

R

R

V

V

E

A

I

I

L

G

K

R

V

T

L

L

L

V

A

A

G

E

A

P

R

S

I

V

L

F

I

L

L

L

D
|
D

E

E

P

P

T

L

A

S

V

N

L

L

T

D

D

A

G

A

-

L

E

R

A

V

E

Q

R

M

L

R

L

I

E

E

T

I

V

S

R

R

A

L

F

H

A

K

R

R

Q

L

G

G

A

R

A

T

V

M

I

I

L

Y

V

V

T

T

H

H

K

D

M

Q

S

V

D

E

V

A

K

M

R

T

F

L

A

A

D

D

R

K

V

I

T

V

V

V

M

L

R

D

G

A

G

G

R

R

T

V

I

A

Q

Q

T

V

L

G

D

K

P

P

A85 (≠ K91) mutation to M: Suppressor of EAA loop mutations in MalFG.
K106 (≠ H119) mutation to C: Suppressor of EAA loop mutations in MalFG.
V114 (≠ I130) mutation to C: Suppressor of EAA loop mutations in MalFG.
V117 (≠ K133) mutation to M: Suppressor of EAA loop mutations in MalFG.
E119 (≠ A135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
A124 (≠ S140) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
G137 (≠ A153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
D158 (= D174) mutation to N: Loss of maltose transport but retains ability to repress mal genes.

Sites not aligning to the query:

228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
267 W→G: Normal maltose transport but constitutive mal gene expression.
278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
340 G→A: Maltose transport is affected but retains ability to interact with MalT.
346 G→S: Normal maltose transport but constitutive mal gene expression.
355 F→Y: Maltose transport is affected but retains ability to interact with MalT.

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
28% identity, 43% coverage: 6:233/525 of query aligns to 2:217/371 of 3puyA

query
sites
3puyA

A

S

I

V

Q

Q

L

L

S

Q

G

N

V

V

S

T

K

K

S

A

F
x
W

D

G

G

E

F

V

M

V

A

V

L

S

S

K

Q

D

A

I

D

N

F

L

T

D

A

I

R

H

W

E

G

G

E

E

V

F

H

V

A

V

L

F

L

V

G

G

E

P

N
x
S

G
|
G

A
x
C

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

L

N

R

I

M

A

I

A

A

G

G

L

L

Y

E

A

T

P

I

E

T

S

S

G

G

S

D

L

L

L

F

I

I

N

G

D

E

N

K

A

R

V

M

R

N

L

D

S

T

G

P

P

P

R

A

D

E

A

R

S

G

R

-

Y

-

H

-

I

V

G

G

M

M

V

V

H

F

Q
|
Q

H

S

F

Y

K

A

L

L

V

Y

K

P

P

H

F

L

T

S

V

V

A

A

E

E

N

N

I

M

Q

S

L

F

A

G

L

L

P

-

E

-

G

-

P

-

G

-

N

-

H

-

A

K

F

L

S

A

G

G

S

A

H

K

R

K

Q

E

R

-

L

-

A

-

A

V

L

I

E

N

Q

Q

R

R

I

V

S

N

D

Q

K

V

A

A

A

E

E

V

L

L

G

Q

F

L

S

A

I

H

D

L

P

L

R

D

K
x
R

I

K

T

P

E

K

S
x
A

L

L

S
|
S

V

G

A
x
G

E
x
Q

Q

R

Q

Q

R

R

V

V

E

A

I

I

L

G

K

R

V

T

L

L

L

V

A

A

G

E

A

P

R

S

I

V

L

F

I

L

L

L

D

D

E
|
E

P

P

T

L

A

S

V

N

L

L

T

D

D

A

G

A

-

L

E

R

A

V

E

Q

R

M

L

R

L

I

E

E

T

I

V

S

R

R

A

L

F

H

A

K

R

R

Q

L

G

G

A

R

A

T

V

M

I

I

L

Y

V

V

T

T

H
|
H

K

D

M

Q

S

V

D

E

V

A

K

M

R

T

F

L

A

A

D

D

R

K

V

I

T

V

V

V

M

L

R

D

G

A

G

G

R

R

T

V

I

A

Q

Q

T

V

L

G

D

K

P

P

binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F16), S37 (≠ N41), G38 (= G42), C39 (≠ A43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (≠ S47), Q81 (= Q88), R128 (≠ K145), A132 (≠ S149), S134 (= S151), G136 (≠ A153), Q137 (≠ E154), E158 (= E175), H191 (= H207)
binding magnesium ion: S42 (= S46), Q81 (= Q88)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
28% identity, 43% coverage: 6:233/525 of query aligns to 2:217/371 of 3puxA

query
sites
3puxA

A

S

I

V

Q

Q

L

L

S

Q

G

N

V

V

S

T

K

K

S

A

F
x
W

D

G

G

E

F

V

M

V

A

V

L

S

S

K

Q

D

A

I

D

N

F

L

T

D

A

I

R

H

W

E

G

G

E

E

V

F

H

V

A

V

L

F

L

V

G

G

E

P

N
x
S

G
|
G

A
x
C

G
|
G

K
|
K

S
|
S

S
x
T

L

L

M

L

N

R

I

M

A

I

A

A

G

G

L

L

Y

E

A

T

P

I

E

T

S

S

G

G

S

D

L

L

L

F

I

I

N

G

D

E

N

K

A

R

V

M

R

N

L

D

S

T

G

P

P

P

R

A

D

E

A

R

S

G

R

-

Y

-

H

-

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binding adenosine-5'-diphosphate: W12 (≠ F16), G38 (= G42), C39 (≠ A43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (≠ S47), R128 (≠ K145), S134 (= S151), Q137 (≠ E154)
binding beryllium trifluoride ion: S37 (≠ N41), G38 (= G42), K41 (= K45), Q81 (= Q88), S134 (= S151), G136 (≠ A153), H191 (= H207)
binding magnesium ion: S42 (= S46), Q81 (= Q88)

Query Sequence

>WP_011914604.1 NCBI__GCF_000013785.1:WP_011914604.1
MSNLNAIQLSGVSKSFDGFMALSQADFTARWGEVHALLGENGAGKSSLMNIAAGLYAPES
GSLLINDNAVRLSGPRDASRYHIGMVHQHFKLVKPFTVAENIQLALPEGPGNHAFSGSHR
QRLAALEQRISDKAAELGFSIDPRKITESLSVAEQQRVEILKVLLAGARILILDEPTAVL
TDGEAERLLETVRAFARQGAAVILVTHKMSDVKRFADRVTVMRGGRTIQTLDPQTVSVPE
LVRLTVGESAPASEYQPAIPGEVRLQVRDLRSTGAGGQGVLNGVNLSLRAGEIYGIAGVG
GNGQSELANVLMGLPEPCDGTLELTGFGDLRRASAEQRRELRIAAIPADRYGAALAGELS
VAENFGVGQVHSGRYGSFFRLRRKRLEAEAAEAVAGFDVQGVRSLKQKAALLSGGNAQKL
VIAREFSRDPLLVLVHSPSRGLDVRATAAVHARLRAAREAGAAVLVISEDLDEVLALADR
IGVMSGGRIVAEFDRPADRQAIGSAMVSHDEPGHAEPVAEGASHE

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory