SitesBLAST

I23 (≠ M21) binding ; binding
S26 (≠ G24) binding
Y93 (= Y94) mutation to L: Greatly decreased Arg uptake into liposomes.
A96 (≠ S97) binding ; binding
C97 (≠ A98) binding
N101 (= N102) binding ; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
M104 (≠ Y105) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
W202 (≠ F209) binding ; mutation to L: Halves Arg uptake into liposomes.
S203 (≠ V210) binding
I205 (= I212) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
W293 (= W300) binding ; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
S357 (= S364) binding ; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.

P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
28% identity, 88% coverage: 5:423/475 of query aligns to 7:413/445 of P60063

query
sites
P60063

A

A

Q

H

K

K

L

V

R

G

L

L

S

I

A

P

L

V

I

T

A

L

L

M

V

V

V

S

G

G

S
x
N

M
x
I

I

M

G
|
G

G
x
S

G
|
G

I

V

F

F

S

L

L

L

P

P

Q

A

N

N

M

L

A

A

A

S

R

T

A

G

E

-

V

-

G

G

A

I

V

A

L

I

I

Y

G

G

W

W

A

L

I

V

T

T

A

I

V

I

G

G

M

A

L

L

T

G

L

L

A

S

F

M

V

V

F

Y

Q

A

T

K

L

M

A

S

N

F

R

L

K

D

P

P

E

S

L

-

D

P

S

G

G

G

V

S

Y
|
Y

A

A

Y

Y

A

A

K

R

A

R

G

C

F

F

G

G

D

P

Y

F

M

L

G

G

F
x
Y

S

Q

S

T

A

N

W

V

G

L

Y
|
Y

W

W

I

L

S
x
A

A
x
C

W

W

M

I

G

G

N
|
N

V

I

G

A

Y

M

F

V

V

V

L

I

L

G

F

V

S

G

T

Y

L

L

G

S

Y

Y

F

F

P

P

I

I

F

L

G

-

Q

K

G

D

N

P

T

L

P

V

V

L

A

T

I

I

G

T

C

C

A

V

S

-

L

V

L

L

W

W

A

I

V

F

H

V

F

L

L

L

V

N

L

I

R

V

G

G

I

P

K

K

E

M

A

I

A

T

F

R

I

V

N

Q

Q

A

I

V

T

A

T

T

V

V

A

L

K

A

I

L

V

I

P

P

L

I

L

V

M

G

F

I

I

A

V

V

I

F

A

G

G

W

V

F

A

W

F

F

K

R

A

G

E

E

I

T

F

Y

T

M

R

A

-

A

-

W

D

N

I

V

W

S

G

G

V

L

G

G

N

T

P

-

N

-

M

-

G

-

N

-

V

-

V

F

D

G

Q

A

V

I

R

Q

N

S

M

T

M

L

L

N

V

V

T

T

V

L

F
x
W

V

S

F

F

I
|
I

G
|
G

I
x
V

E
|
E

G
x
S

A
|
A

S

S

V

V

Y

A

S

A

A

G

R

V

A

V

E

K

K

N

-

P

R

K

S

R

D

N

V

V

G

P

R

I

A

A

T

T

V

I

I

G

G

G

F

V

L

L

G

I

V

A

L

A

A

V

L

C

L

Y

V

V

L

L

V

S

N

T

V

T

L

A

S

I

L

M

G

G

I

M

M

I

S

P

Q

N

P

A

Q

A

L

L

A

R

Q

V

L

S

Q

A

N

S

P

P

S

-

L

F

A

G

G

D

V

A

L

A

E

R

H

M

I

A

V

L

G

G

P

D

W

T

G

A

A

G

M

A

A

I

I

V

S

S

I

F

G

C

L

A

A

A

V

A

S

G

L

C

L

L

G

G

A

S

L

L

L

G

S

G

W
|
W

A

T

L

L

C

A

A

G

E

Q

I

T

L

A

Y

K

A

A

T

A

A

A

H

D

D

D

K

G

T

L

M

F

P

P

A

P

F

I

L

F

K

A

K

R

E

V

N

N

A

K

N

A

Q

G

V

T

P

P

V

V

N

A

A

G

L

L

W

I

L

I

T

V

N

G

V

I

M

L

I

M

Q

T

V

I

F
|
F

L

Q

V

L

I

S

T

S

L

I

F

S

S

P

H

N

S

A

T

T

Y

K

T

E

T

F

L

G

I

L

Y

V

L

S

A

S

S

V

S
|
S

M

V

I

I

-

F

-

T

L

L

V

V

P

P

Y
|
Y

L

L

W

Y

S

T

A

C

A

A

Y

-

A

A

V

L

L

L

S

L

G

G

R

H

G

G

E

H

T

F

Y

G

Q

K

G

-

A

-

H

-

G

-

Q

A

R

R

I

P

K

A

D

Y

L

L

L

A

V

V

G

T

L

T

I

I

A

A

L

F

G

L

Y

Y

A

C

V

I

W

W

L

A

L

V

Y

V

A

G

G

S

G

G

L

A

K

K

Y

E

L

V

L

M

L

W

S

S

N22 (≠ S20) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
I23 (≠ M21) binding
GSG 25:27 (≠ GGG 23:25) Helix-breaking GSG motif TM1
S26 (≠ G24) binding ; mutation to K: 5% Agm antiport.
G27 (= G25) binding
Y74 (= Y75) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
Y87 (≠ F88) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
Y93 (= Y94) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
A96 (≠ S97) binding
C97 (≠ A98) binding
N101 (= N102) binding
W202 (≠ F209) Periplasmic (proximal) gate; binding
I205 (= I212) binding
GVESA 206:210 (≠ GIEGA 213:217) Helix-breaking GVESA motif TM6
E208 (= E215) mutation E->A,D: 5-10% Agm antiport.
W293 (= W300) binding
F337 (= F344) mutation to A: Severely decreased antiport.
S357 (= S364) binding
Y365 (= Y370) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.

3l1lA Structure of arg-bound escherichia coli adic (see paper)
27% identity, 88% coverage: 5:423/475 of query aligns to 1:396/423 of 3l1lA

query
sites
3l1lA

A

A

Q

H

K

K

L

V

R

G

L

L

S

I

A

P

L

V

I

T

A

L

L

M

V

V

V

S

G

G

S
x
A

M
x
I

I
x
M

G

G

G
x
S

G
|
G

I

V

F

F

S

L

L

L

P

P

Q

A

N

N

M

L

A

A

A

S

R

T

A

G

E

-

V

-

G

G

A

I

V

A

L

I

I

Y

G

G

W

W

A

L

I

V

T

T

A

I

V

I

G

G

M

A

L

L

T

G

L

L

A

S

F

M

V

V

F

Y

Q

A

T

K

L

M

A

S

N

F

R

L

K

D

P

P

E

S

L

-

D

P

S

G

G

G

V

S

Y

Y

A

A

Y

Y

A

A

K

R

A

R

G

C

F

F

G

G

D

P

Y

F

M

L

G

G

F

Y

S

Q

S

T

A

N

W

V

G

L

Y

Y

W

W

I

L

S
x
A

A
x
C

W

W

M

I

G
|
G

N
|
N

V

I

G

A

Y
x
M

F

V

V

V

L

I

L

G

F

V

S

G

T

Y

L

L

G

S

Y

Y

F

F

P

P

I

I

F

L

G

-

Q

K

G

D

N

P

T

W

P

V

V

L

A

T

I

I

G

T

C

C

A

V

S

-

L

V

L

L

W

W

A

I

V

F

H

V

F

L

L

L

V

N

L

I

R

V

G

G

I

P

K

K

E

M

A

I

A

T

F

R

I

V

N

Q

Q

A

I

V

T

A

T

T

V

V

A

L

K

A

I

L

V

I

P

P

L

I

L

V

M

G

F

I

I

A

V

V

I

F

A

G

G

W

V

F

A

W

F

F

K

R

A

G

E

E

I

T

F

Y

T

-

R

-

D

-

I

-

W

-

G

-

V

-

G

-

N

-

P

-

N

-

M

-

G

-

N

-

V

-

V

M

D

A

Q

A

V

I

R

Q

N

S

M

T

M

L

L

N

V

V

T

T

V

L

F
x
W

V
x
S

F
|
F

I
|
I

G

G

I

V

E

E

G

S

A

A

S

S

V

V

Y

A

S

A

A

G

R

V

A

V

E

K

K

N

-

P

R

K

S

R

D

N

V

V

G

P

R

I

A

A

T

T

V

I

I

G

G

G

F

V

L

L

G

I

V

A

L

A

A

V

L

C

L

Y

V

V

L

L

V

S

N

T

V

T

L

A

S

I

L

M

G

G

I

M

M

I

S

P

Q

N

P

A

Q

A

L

L

A

R

Q

V

L

S

Q

A

N

S

P

P

S

-

L

F

A

G

G

D

V

A

L

A

E

R

H

M

I

A

V

L

G

G

P

D

W

T

G

A

A

G

M

A

A

I

I

V

S

S

I

F

G

C

L

A

A

A

V

A

S

G

L

C

L

L

G

G

A

S

L

L

L

G

S

G

W
|
W

A

T

L

L

C

A

A

G

E

Q

I

T

L

A

Y

K

A

A

T

A

A

A

H

D

D

D

K

G

T

L

M

F

P

P

A

P

F

I

L

F

K

A

K

R

E

V

N

N

A

K

N

A

Q

G

V

T

P

P

V

V

N

A

A

G

L

L

W

I

L

I

T

V

N

G

V

I

M

L

I

M

Q

T

V

I

F

F

L

Q

V

L

I

S

T

S

L

I

F

S

S

P

H

N

S

A

T

T

Y

K

T

E

T

F

L

G

I

L

Y

V

L

S

A

S

S

V

S
|
S

M

V

I

I

-

F

-

T

L

L

V

V

P

P

Y

Y

L

L

W

Y

S

T

A

C

A

A

Y

-

A

A

V

L

L

L

S

L

G

G

R

H

G

G

E

H

T

F

Y

G

Q

K

G

-

A

-

H

-

G

-

Q

A

R

R

I

P

K

A

D

Y

L

L

L

A

V

V

G

T

L

T

I

I

A

A

L

F

G

L

Y

Y

A

C

V

I

W

W

L

A

L

V

Y

V

A

G

G

S

G

G

L

A

K

K

Y

E

L

V

L

M

L

W

S

S

binding arginine: A16 (≠ S20), I17 (≠ M21), M18 (≠ I22), S20 (≠ G24), G21 (= G25), A90 (≠ S97), C91 (≠ A98), G94 (= G101), N95 (= N102), M98 (≠ Y105), W185 (≠ F209), S186 (≠ V210), F187 (= F211), I188 (= I212), W276 (= W300), S340 (= S364)

P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
25% identity, 92% coverage: 1:436/475 of query aligns to 1:427/439 of P0AAF1

query
sites
P0AAF1

M

M

S

S

Q

Q

-

A

P

K

A

S

Q

N

K

K

L

M

R

G

L

V

S

V

A

Q

L

L

I

T

A

I

L

L

V

T

V

M

G

V

S

N

M

M

I

M

G

G

G

S

G

G

I

I

F

I

S

M

L

L

P

P

Q

T

N

K

M

L

A

A

A

-

R

-

A

-

E

E

V

V

G

G

A

T

V

I

-

S

L

I

I

I

G

S

W

W

A

L

I

V

T

T

A

A

V

V

G

G

M

S

L

M

T

A

L

L

A

A

F

W

V

A

F

F

Q

A

T

K

L
x
C

A

G

-

M

-

F

N

S

R

R

K
|
K

P

-

E

-

L

-

D

S

S

G

G

G

V

M

Y

G

A

G

Y

Y

A

A

K
x
E

A
x
Y

G

A

F

F

G

G

D
x
K

Y

S

M

G

G

N

F

F

S

M

S

A

A

N

W
x
Y

G

T

Y
|
Y

W

G

I

V

S

S

A

L

W

L

M

I

G

A

N

N

V

V

G

A

Y

-

F

-

V

-

L

I

L

A

F

I

S

S

T

A

L

V

G

G

Y

Y

F

G

F

T

P

E

I

L

F

L

G

G

Q

A

G

S

N

L

T

S

P

P

V

V

A

Q

I

I

G

G

C

L

A

A

S

T

L

I

-

G

L

V

L

L

W

W

A

I

V

C

H

T

F

V

L

A

V

N

L

F

R

G

G

G

I

A

K

R

E

I

A

T

A

G

F

Q

I

I

N

S

Q

S

I

I

T

T

T

V

V

W

A

G

K

V

I

I

V

I

P

P

L

V

M

G

F

L

I

C

V

I

I

I

A

G

G

W

V

F

A

W

F

F

K

S

A

P

E

T

I

L

F

Y

T

V

R

-

D

D

I

S

W

W

G

-

V

-

G

-

N

N

P

P

N

H

M

H

G

A

N

P

V

F

D

S

Q

A

V

V

R

G

N

S

M

S

M

I

L

A

V

M

T

T

V

L

F
x
W

V

A

F

F

I

L

G

G

I

L

E
|
E

G

S

A

A

S
x
C

V

A

Y

N

S

T

A

D

R

V

A

V

E

E

K

N

-

P

R

E

S

R

D

N

V

V

G

P

R

I

A

A

T

V

V

L

I

G

G

G

F

T

L

L

G

G

V

A

L

A

A

V

L

I

L

Y

V

I

L

V

V

S

N

T

V

N

L

V

S

I

L

A

G

G

I

I

M

V

S

P

Q

N

P

M

Q

E

L

L

A

A

Q

N

L

S

Q

T

N

A

P

P

S

-

L

F

A

G

G

L

V

A

L

F

E

A

H

Q

I

M

V

F

G

T

P

P

W

E

G

V

A

G

M

K

A

V

I

I

S

M

I

A

G

L

L

M

A

V

V

M

S

S

L
x
C

G

G

A

S

L

L

S

G

W
|
W

A

Q

L

F

L

T

C

I

A

A

E

Q

I

V

L

F

Y
x
K

A

S

T

S

A

S

H

D

D

E

K

G

T
x
Y

M

F

P

P

A

K

F

I

L

F

K

S

K

R

E

V

N

T

A

K

N

V

Q

D

V

A

P

P

V

V

N

Q

A

G

L

M

W

-

L

L

T

T

N

I

V

V

M

I

I

I

Q

Q

V

S

F

G

L

L

V

A

I

L

T

M

L

T

F

I

S

S

-

P

-

S

-

L

H

N

S

S

T

Q

Y

F

T

N

T

V

L

L

I

V

Y

N

L

L

A

A

S

V

M

T

I

N

L

I

V

I

P

P

Y

Y

L

I

W

L

S

S

A

M

A

A

Y

A

A

L

V

V

L

I

S

Q

G

K

R

V

G

A

E

N

T

V

Y

P

Q

P

G

S

A

K

H

-

G

-

Q

A

R

K

I

V

K

A

D

N

L

-

L

F

V

V

G

A

L

F

I

V

A

G

L

A

G

M

Y

Y

A

S

V

F

W

Y

L

A

L

L

Y

Y

A

S

G

S

G

G

L

E

K

E

Y

A

L

M

L

L

L

Y

S

G

A

S

L

I

L

V

Y

T

A

F

P

L

G

G

V
x
W

I

T

L

L

F
x
Y

A

G

L

L

C62 (≠ L63) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
K68 (= K67) mutation to A: Slight decrease in both uptake and excretion activities.
E77 (≠ K79) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
Y78 (≠ A80) mutation to L: Uptake activity decreases more than excretion activity.
K82 (≠ D84) mutation to A: Slight decrease in both uptake and excretion activities.
Y90 (≠ W92) mutation to L: Uptake activity decreases more than excretion activity.
Y92 (= Y94) mutation to L: Moderate decrease in both uptake and excretion activities.
W201 (≠ F209) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
E207 (= E215) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
C210 (≠ S218) mutation to A: Moderate decrease in both uptake and excretion activities.
C285 (≠ L293) mutation to A: Moderate decrease in both uptake and excretion activities.
C286 (≠ L294) mutation to A: Moderate decrease in both uptake and excretion activities.
W292 (= W300) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
K301 (≠ Y309) mutation to A: Excretion activity decreases more than uptake activity.
Y308 (≠ T316) mutation to L: Excretion activity decreases more than uptake activity.
W422 (≠ V431) mutation to L: Uptake activity decreases more than excretion activity.
Y425 (≠ F434) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.

Sites not aligning to the query:

433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.

P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
26% identity, 80% coverage: 5:382/475 of query aligns to 4:378/444 of P0AAE8

query
sites
P0AAE8

A

A

Q

K

K

K

L

I

R

G

L

L

S

F

A

A

L
x
C

I

T

A

G

L

V

V

V

V

A

G

G

S

N

M

M

I

M

G

G

G

S

G

G

I

I

F

A

S

L

L

L

P

P

Q

A

N

N

M

L

A

A

A

S

R

I

A

G

E

-

V

-

G

G

A

I

V

A

L

I

I
x
W

G

G

W
|
W

A

I

I

I

T

S

A

I

V

I

G

G

M

A

L

M

T

S

L

L

A

A

F
x
Y

V

V

F
x
Y

Q

A

T

R

L

L

A

A

N

T

R

K

K

N

P

P

E

Q

L

-

D

Q

S

G

G

G

V

P

Y

I

A

A

Y
|
Y

A

A

K

G

A
x
E

G

-

F

I

G

S

D

P

Y

A

M

F

G

G

F

F

S

Q

S

T

A

G

W

V

G

L

Y
|
Y

W
x
Y

I

H

S

A

A

N

W

W

M

I

G

G

N

N

V

L

G

A

Y

I

F

G

V

I

L

T

L

A

F

V

S

S

T
x
Y

L

L

G

S

Y

T

F

F

P

P

I

V

F

L

G

-

Q

-

G

-

N

N

T

D

P

P

V

V

A

P

I

A

G

G

C

I

A

A

S
x
C

L

I

-

A

L

I

L

V

W

W

A

V

V

F

H

T

F

F

L

V

V

N

L

M

R

L

G

G

I

G

K

T

E

W

A

V

A

S

F

R

I

L

N

T

Q

T

I

I

T

G

T

L

V

V

A

L

K

V

I

L

V

I

P

P

L

V

M

M

F

T

I

A

V

I

I

V

A

G

G

W

V

H

A

W

F

F

K

D

A

A

E

A

I

T

F
x
Y

T

A

R

A

D

N

I

-

W

W

G

N

V

T

G

A

N

D

P

T

N

T

M
x
D

G

G

N

H

V

A

V

I

D

I

Q

K

V

-

R

-

N

-

M

S

M

I

L

L

V

L

T
x
C

V

L

F

W

V

A

F

F

I

V

G

G

I

V

E
|
E

G

S

A

A

S

A

V

V

Y

S

S

T

A

G

R

M

A

V

E

K

K

N

-

P

R

K

S

R

D

T

V

V

G

P

R

L

A

A

T

T

V

M

I

L

G

G

F

-

L

T

G

G

V

L

L

A

A

G

L

I

L

V

V
x
Y

L

I

V

A

N

A

V

T

L

Q

S

V

L

L

G

S

I

G

M

M

S
x
Y

Q

P

P

S

Q

S

L

V

A

M

Q

A

L

A

Q

S

N

G

P

A

S

P

L

F

A

A

G

I

V

S

L

A

E

S

H

T

I

I

V

L

G

G

P

N

W

W

G

A

A

A

M

P

A

L

I

V

S

S

I

A

G

F

L

T

A

A

V

F

S

A

L
x
C

L

L

G

T

A

S

L

L

L

G

S

S

W

W

A

M

L

M

L

L

C

V

A

G

E

Q

I

A

L

G

Y

V

A
x
R

T

A

A

A

H

N

D
|
D

K

G

T

N

M

F

P

P

A

K

F

V

L
x
Y

K

G

K

E

E

V

N

D

A

S

N

N

Q

G

V

I

P

P

V

K

N

K

A

G

L

L

W

L

L

L

T

A

N

A

V

V

-

K

M

M

I

T

Q

A

V

L

F

M

L

I

V

L

I

I

T

T

L

L

F

M

S

N

H

S

S

A

-

G

-

K

-

A

-

S

-

D

T

L

Y

F

T

G

T

E

L

L

I

T

Y

G

L

I

A

A

S

V

S

L

M

L

I

T

L

M

V

L

P

P

Y
|
Y

L

F

W
x
Y

S

S

A
x
C

A

V

Y

D

A

L

V

I

L

R

L

F

S
x
E

G

G

C12 (≠ L13) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
W41 (≠ I44) mutation to L: Moderate decrease in cadaverine uptake.
W43 (= W46) mutation to L: Strong decrease in cadaverine uptake.
Y55 (≠ F58) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Y57 (≠ F60) mutation to L: Strong decrease in cadaverine uptake.
Y73 (= Y77) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
E76 (≠ A80) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Y89 (= Y94) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
Y90 (≠ W95) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
Y107 (≠ T112) mutation to L: Strong decrease in cadaverine uptake.
C125 (≠ S133) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
Y174 (≠ F181) mutation to L: Moderate decrease in cadaverine uptake.
D185 (≠ M193) mutation to N: Moderate decrease in cadaverine uptake.
C196 (≠ T207) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
E204 (= E215) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
Y235 (≠ V246) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
Y246 (≠ S257) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
C282 (≠ L293) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
R299 (≠ A310) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
D303 (= D314) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
Y310 (≠ L321) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Y366 (= Y370) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
Y368 (≠ W372) mutation to L: Strong decrease in cadaverine uptake.
C370 (≠ A374) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
E377 (≠ S381) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.

Sites not aligning to the query:

389 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
394 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
397 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
408 E→Q: Moderate decrease in cadaverine uptake.
423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.

O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 80% coverage: 14:391/475 of query aligns to 18:384/438 of O34739

query
sites
O34739

I

L

A

T

L

L

V

V

V

I

G

G

S

T

M

I

I

I

G

G

G

S

G

G

I

V

F

F

S

M

L

K

P

P

Q

G

N

A

M

V

A

L

A

A

-

Y

-

S

-

G

-

D

-

S

R

K

A

M

E

A

V

L

G

F

A

A

V

W

L

L

I

L

G

G

W

G

A

I

I

L

T

T

A

L

V

A

G

G

M

G

L

L

T

T

L

I

A

A

F

-

V

-

F

-

Q

-

T

E

L

I

A

G

N

T

R

Q

K

I

P

P

E

K

L

-

D

T

S

G

G

G

V

L

Y

Y

A

T

Y

Y

A

L

K

E

A

E

G

V

F

Y

G

G

D

E

Y

F

M

W

G

G

F

F

S

L

S
x
C

A

G

W

W

G

V

Y

Q

W

I

I

I

S

I

A

Y

W

G

M

P

G

A

N

I

V

I

G

G

Y

A

F

L

V

G

L

L

L

Y

F

F

S

G

T

S

L

L

G

M

Y

A

F

N

F

L

P

F

I

G

F

W

G

G

Q

S

G

G

N

L

T

S

P

K

V

V

A

-

I

I

G

G

C

I

A

I

S

A

L

V

L

L

L

F

W

L

A
x
C

V

V

H

I

F

N

L

I

V

I

L

-

R

-

G

G

I

T

K

K

E

Y

A

G

F

F

I

V

N

Q

Q

T

I

L

T

T

V

I

A

G

K

K

I

L

V

I

P

P

L

I

L

A

M
x
C

F

I

I

I

V

V

I

F

A

G

G

L

V

W

A

K

F

G

K

D

A

Q

E

H

I

I

F

F

T

T

R

A

D

V

I

N

W

E

G

S

V

I

G

S

N

D

P

M

N

N

M

F

G

G

N

A

V

A

V

I

D

-

Q

-

V

-

R

-

N

-

M

-

L

L

V

A

T

T

V

L

F

F

V

A

F

Y

I

D

G

G

-

W

I

I

E

L

G

L

A

A

S

A

V

L

Y

G

S

G

A

E

R

M

A

K

E

N

K

P

R

E

S

K

D

L

V

L

G

P

R

R

A

A

T

M

V

T

I

G

G

G

F

L

L

L

G

I

V

V

L

T

A

A

L

I

L

Y

V

I

L

F

V

I

N

N

V

F

L

A

S

L

L

L

G

H

I

I

M

L

S

S

Q

A

P

N

Q

E

L

I

A

V

Q

T

L

L

Q

G

N

E

P

N

S

A

L

T

A

S

G

T

V

A

L

A

E

T

H

M

I

L

V

F

G

G

P

S

W

I

G

G

A

G

M

K

A

L

I

I

S

S

I

V

G

G

L

I

A

I

V

V

S

S

L

I

L

F

G

G

A
x
C

L

L

L

N

S

G

W

K

A

V

L

L

L

S

C

F

A

P

E

R

I

V

L

S

Y

F

A

A

T

M

A

A

H

E

D

R

K

K

T

Q

M

L

P

P

A

-

F

F

L

A

K

E

K

K

E

L

N

S

A

H

N

V

Q

H

V

P

P

S

V

F

N

R

A

T

L

P

W

W

L

I

T

A

N

-

V

I

M

S

I

F

Q

Q

V

I

F

A

L

L

V

A

I

L

T

I

L

M

F

M

S

L

H

I

S

S

T

N

Y

P

T

D

T

K

L

L

I

S

Y

E

L

I

A

S

S

I

S

F

M

M

I

I

L

Y

V

I

P

F

Y

Y

L

V

W

M

S

A

A

F

Y

A

A

V

V

F

L

I

L

L

S

R

G

K

R

R

G

A

E

K

T

G

Y

E

Q

K

G

R

A

A

H

Y

C94 (≠ S90) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
C141 (≠ A138) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
C168 (≠ M167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
C291 (≠ A296) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.

Sites not aligning to the query:

415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.

6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 67% coverage: 14:332/475 of query aligns to 10:325/433 of 6f2wA

query
sites
6f2wA

I

L

A

T

L

V

V

V

G

G

S

T

M
x
V

I

I

G
|
G

G
x
A

G
|
G

I

I

F

F

S

F

L

K

P

P

Q

T

N

A

M

V

-

Y

A

G

A

A

R

A

A

G

E

A

V

P

G

G

A

L

V

G

L

L

I

L

G

A

W

W

-

F

-

V

-

A

-

G

A

I

I

I

T

T

A

I

V

A

G

G

M

G

L

L

T

T

L

V

A

A

F

-

V

-

F

-

Q

-

T

E

L

I

A

G

N

T

R

I

K

Y

P

P

E

Q

L

-

D

T

S

G

G

G

V

M

Y

M

A

I

Y

Y

A

L

K

E

A

K

G

V

F

Y

G

G

D

R

Y

W

M

L

G

G

F

F

S

L

S

V

A

G

W

W

G

A

Y

Q

W

M

I

V

S

I

A

Y

W

Y

M

P

G

A

N

N

V

I

G

A

Y

A

F

L

V

A

L

I

F

F

S

A

T

T

L

-

G

-

Y

Q

F

F

F

V

P

N

I

L

F

F

G

A

Q

L

G

S

N

D

T

S

-

T

-

I

-

V

P

P

V

T

A

A

I

I

G

-

C

L

A

T

S

S

L

I

L

F

L

L

W

M

A

G

V

V

H

N

F

F

L

L

V

-

L

-

R

-

G

G

I

T

K

K

E

Y

A

S

A

G

F

W

I

I

N

Q

Q

T

I

L

T

A

T

T

V

I

A

L

K

K

I

L

V

I

P

P

L

L

L

V

M

V

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-

I

I

V

I

I

V

A

A

G

G

V

L

A

L

F

Y

K

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A

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E

G

I

G

F

V

T

I

R

R

D

L

I

V

W

-

G

-

V

P

G

F

N

S

P

V

N

E

M

T

G

H

N

P

V

V

V

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D

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N

S

M

A

M

L

L

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F
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F

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x
A

F

Y

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x
D

G

G

I

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E

I

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N

A

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G

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Y

L

S

A

A

G

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E

A

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E

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K

N

R

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G

D

K

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M

G

L

R

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A

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T

V

V

I

I

I

G

G

F

G

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L

G

S

-

I

V

V

L

M

A

A

L

V

L

Y

V

L

L

L

V

T

N

N

V

I

L

A

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Y

L

L

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F

I

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L

S

D

Q

S

P

S

Q

Q

L

L

A

A

Q

G

L

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D

N

T

P

P

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A

L

-

A

A

G

L

V

V

L

A

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H

H

I

L

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F

G

E

P

G

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I

G

G

A

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K

A

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I

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G

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I

A

L

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L

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G

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A

G

L

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S

G

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x
Y

A

I

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C

G

A

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Y

Y

A

A

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A

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M

L

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P

A

F

-

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-

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N

N

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L

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N

N

binding alpha-aminoisobutyric acid: V17 (≠ M21), G19 (= G23), A20 (≠ G24), G21 (= G25), F199 (= F209), A200 (≠ V210), D202 (≠ I212), Y290 (≠ W300)

P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 73% coverage: 6:354/475 of query aligns to 15:369/489 of P25737

query
sites
P25737

Q

R

K

E

L

L

R

K

L

A

S

R

A

H

L

L

I

T

A

M

L

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A

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S

I

I

G

G

G

T

G

G

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L

A

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N

A

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A

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A

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G

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A

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A

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Y

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I

A

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L

G

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M

V

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Y

T

F

L

L

A

M

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F

L

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G

T

E

L

L

A

A

N

A

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P

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V

L

-

D

-

S

S

G

G

V

S

Y

F

A

A

-

T

-

Y

-

G

-

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-

N

Y

Y

A

V

K

E

A

E

G

G

F

F

G

G

D

-

Y

-

M

-

G

-

F

F

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A

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L

A

G

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W

G

N

Y
|
Y

W

W

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Y

S

N

A

-

W
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W

M

A

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N

T

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Y

V

F

D

V

L

L

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L

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F

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-

L

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M

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S

Y

W

F

W

F

F

P

P

I

-

F

-

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-

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-

G

-

N

D

T

T

P

P

V

G

A

W

I

I

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W

C

S

A

A

S

L

L

F

L

L

-

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-

V

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A

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K

G

A

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D

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W

W

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V

I

G

G

N

E

-

A

P

P

N

F

M

A

G

G

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F

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A

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M

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F
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F

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F

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E
|
E

G

L

A

I

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G

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I

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A

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A

A

G

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x
E

A

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E

E

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D

R

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S

A

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K

D

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x
D

S

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L

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-

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E
x
D

H

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A

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H

I

A

G

G

L

L

-

L

-

S

A

A

V

A

S

A

L

V

L

M

G

N

A

A

L

V

L

I

S

L

W

T

A

A

L

V

L

L

C

S

A

A

-

G

-

N

-

S

-

G

-

M

-

Y

-

A

-

S

-

T

E

R

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M

L

L

Y

Y

A

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T

L

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A

H

C

D

D

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A

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A

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K

E

L

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N

A

A

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L

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T

Y102 (= Y94) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
W106 (= W99) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
K163 (≠ T158) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
F216 (= F209) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
E222 (= E215) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
E230 (≠ R223) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
D275 (≠ P267) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
D278 (≠ E274) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.

Query Sequence

>GFF4359 FitnessBrowser__WCS417:GFF4359
MSQPAQKLRLSALIALVVGSMIGGGIFSLPQNMAARAEVGAVLIGWAITAVGMLTLAFVF
QTLANRKPELDSGVYAYAKAGFGDYMGFSSAWGYWISAWMGNVGYFVLLFSTLGYFFPIF
GQGNTPVAIGCASLLLWAVHFLVLRGIKEAAFINQITTVAKIVPLLMFIVIAGVAFKAEI
FTRDIWGVGNPNMGNVVDQVRNMMLVTVFVFIGIEGASVYSARAEKRSDVGRATVIGFLG
VLALLVLVNVLSLGIMSQPQLAQLQNPSLAGVLEHIVGPWGAMAISIGLAVSLLGALLSW
ALLCAEILYATAHDKTMPAFLKKENANQVPVNALWLTNVMIQVFLVITLFSHSTYTTLIY
LASSMILVPYLWSAAYAVLLSGRGETYQGAHGQRIKDLLVGLIALGYAVWLLYAGGLKYL
LLSALLYAPGVILFALAKREQDQPLFTHVEKGIFSCVIAGAGLAAYGLYSGVLSL

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