SitesBLAST

E190 (≠ D194) mutation E->A,C,K,L: Reduction of transport rate.
A192 (= A196) mutation A->D,S,L: Loss of transport and MalK dissociation from the membrane.
G196 (= G200) mutation to A: No effect.; mutation to P: Loss of transport and MalK dissociation from the membrane.
P209 (= P213) mutation to A: No effect.

P02916 Maltose/maltodextrin transport system permease protein MalF from Escherichia coli (strain K12) (see 4 papers)
34% identity, 24% coverage: 162:234/300 of query aligns to 369:441/514 of P02916

query
sites
P02916

R

R

S

T

G

M

L
|
L

V

I

L

I

V

V

Y
x
N

A

T

A

W

T

L

G
|
G

I

Y

P

P

F

Y

S

M

V

M

F

I

I

L

L

C

T

M

A

G

F

L

R

K

Q

A

L

I

P

P

G

D

D

D

L

L

A

Y

D
x
E

A

A

A
x
S

A

A

I

M

D

D

G
|
G

A

A

G

G

E

P

F

F

Q

Q

I

N

F

F

S

F

R

K

V

I

M

T

L

L

P
|
P

L

L

V

L

R

I

P

K

A

P

L

L

S

T

T

P

V

L

M

M

V

I

F

A

Q

S

F

F

V

A

P

F

L

N

W

F

N

N

D

N

F

F

L372 (= L165) mutation to W: Growth on maltose but not on media containing either maltoheptaose or maltoheptaose plus maltose.
N376 (≠ Y169) mutation N->K,H: No growth on maltose.
G380 (= G173) mutation G->C,S: No growth on maltose.
E401 (≠ D194) mutation E->A,C,K,L: Reduction of transport rate.
S403 (≠ A196) mutation S->C,D,K,L: Reduction of transport rate.
G407 (= G200) mutation G->A,P: No effect.
P420 (= P213) mutation to A: No effect.

Sites not aligning to the query:

334 L→W: Ability to transport lactose in a saturable manner.

4ki0F Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to maltohexaose (see paper)
34% identity, 24% coverage: 162:234/300 of query aligns to 354:426/490 of 4ki0F

query
sites
4ki0F

R

R

S

T

G

M

L

L

V

I

L

I

V

V

Y
x
N

A

T

A

W

T

L

G
|
G

I

Y

P

P

F
x
Y

S

M

V

M

F

I

I

L

L

C

T

M

A

G

F

L

R

K

Q

A

L

I

P

P

G

D

D

D

L

L

A

Y

D

E

A

A

A

S

A

A

I

M

D

D

G

G

A

A

G

G

E

P

F

F

Q

Q

I

N

F

F

S

F

R

K

V

I

M

T

L

L

P

P

L

L

V

L

R

I

P

K

A

P

L

L

S

T

T

P

V

L

M

M

V

I

F

A

Q
x
S

F

F

V

A

P

F

L
x
N

W

F

N

N

D

N

F

F

binding alpha-D-glucopyranose: N361 (≠ Y169), G365 (= G173), Y368 (≠ F176), S418 (≠ Q226), N422 (≠ L230)

Sites not aligning to the query:

binding alpha-D-glucopyranose: 310

7cagA Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
28% identity, 51% coverage: 74:226/300 of query aligns to 49:216/285 of 7cagA

query
sites
7cagA

E

E

R

F

V

I

S

G

L

L

D

A

S

N

Y

Y

A

V

T

T

A

V

W

L

T

T

D

D

A

G

N

Y

F

W

G

W

R

T

Y

A

F

F

F

A

N

V

S

T

L

L

G

G

I

I

T

T

I

V

A

V

S

S

V

V

L

A

L

I

A

E

T

F

T

A

V

L

S

G

V

L

L

A

A

L

A

A

Y

L

P

V

L

M

G

H

R

R

Y

T

R

I

F

F

-

G

R

K

G

G

S

A

S

V

A

R

L

T

S

A

L

I

F

L

F

I

L

P

S

Y

G

G

L

I

M

V

-

T

-

V

-

A

-

S

L

Y

P

S

F

W

R

Y

L

Y

A

A

I

W

L

T

P

P

-

G

-

T

-

G

-

Y

-

L

L

A

F

N

L

L

L

P

D

E

G

G

L

S

N

A

-

P

L

L

V

T

D

D

T

Q

R

L

S

P

G

S

L

L

V

A

L

I

V

V

Y

V

A

L

A

A

-
x
E

-

V

-

W

T
x
K

G

T

I

T

P

P

F

F

S

M

V

A

F

L

I

L

L

L

T

L

A

A

F

G

F

L

R

A

Q

L

L

V

P

P

G

Q

D

D

L

L

A

L

D

N

A

A

A

Q

I

V

D

D

G

G

A

A

G

G

E

P

F

W

Q

K

I

R

F

L

S

T

R

K

V

V

M

I

L

L

P

P

L

M

V

I

R

K

P

P

A

A

L

I

S

L

T

V

V

A

M

L

V

L

F

F

Q
x
R

binding alpha-D-glucopyranose: E159 (vs. gap), K162 (≠ T172), R216 (≠ Q226)

Sites not aligning to the query:

binding alpha-D-glucopyranose: 219

Query Sequence

>WP_211262496.1 NCBI__GCF_000969705.1:WP_211262496.1
MSGLTEVRTRPEETDAPPRATHRRTRRRPTVSSLAIGAVLWGYALVVVAPLLLVVLNSLR
PTSEIFADPIALPERVSLDSYATAWTDANFGRYFFNSLGITIASVLLATTVSVLAAYPLG
RYRFRGSSALSLFFLSGLMLPFRLAILPLFLLLDGLNLVDTRSGLVLVYAATGIPFSVFI
LTAFFRQLPGDLADAAAIDGAGEFQIFSRVMLPLVRPALSTVMVFQFVPLWNDFFFPLVL
LRSSDKWTLPVGMTRFFGEYQTDWSTLFAGLLIATLPLIVLFLAATRQIIAGLTAGIGKM

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