SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010529741.1 NCBI__GCF_000224785.1:WP_010529741.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 10 hits to proteins with known functional sites (download)

P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 6 papers)
45% identity, 97% coverage: 10:489/496 of query aligns to 63:548/595 of P54582

query
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P54582

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W101 (= W46) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
E135 (≠ D80) mutation to A: Strongly decreased betaine transport.
G149 (= G94) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
M150 (= M95) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
G151 (= G96) mutation to A: Nearly abolishes betaine transport.
I152 (= I97) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
IG 152:153 (= IG 97:98) binding glycine betaine
G153 (= G98) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
F156 (= F101) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
W189 (= W137) mutation to C: Mildly decreased betaine transport.
W194 (= W142) mutation to L: Strongly decreased betaine transport.
Y197 (= Y145) mutation to L: Nearly abolishes betaine transport.
R210 (= R158) mutation to A: Nearly abolishes betaine transport.
S253 (= S200) binding glycine betaine
G301 (= G247) mutation to L: Strongly decreased betaine transport.
N309 (= N255) mutation to A: Decreases affinity for sodium ions.
T351 (= T297) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
W362 (= W307) mutation to C: Strongly decreased betaine transport.
W366 (= W311) mutation to C: No effect on betaine transport.
F369 (= F314) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
W371 (= W316) mutation to L: No effect on betaine transport.
W373 (= W318) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
WWISW 373:377 (= WWISW 318:322) binding glycine betaine
W374 (= W319) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
W377 (= W322) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
F380 (= F325) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
F384 (= F329) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
R387 (= R332) mutation to A: Mildly decreased betaine transport.
R392 (= R337) mutation to K: Moderately decreased betaine transport.

3p03C Crystal structure of betp-g153d with choline bound (see paper)
44% identity, 98% coverage: 10:495/496 of query aligns to 7:494/508 of 3p03C

query
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3p03C

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binding choline ion: A92 (= A93), M94 (= M95), D97 (≠ G98), F320 (= F325)

4llhA Substrate bound outward-open state of the symporter betp (see paper)
45% identity, 98% coverage: 10:495/496 of query aligns to 7:495/524 of 4llhA

query
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F

L

G

G

A

A

V

L

Q

Q

I

I

N

G

G

A

G

G

L

L

S

S

H

A

L

A

F

E

N

D

F

P

E

S

-

D

-

W

-

T

-

I

V

V

G

G

F

-

T

-

S

-

Q

-

F

-

I

-

I

I

I

V

T

S

V

V

V

L

T

T

L

L

L

A

F

F

L

I

I

F

S

S

A

A

W

I

S

S

G

G

L

V

S

G

K

K

G

G

I

I

K

Q

Y

Y

L

L

S

S

N

N

T

A

N

N

M

M

V

V

L

L

S

A

I

A

I

L

L

L

L

A

I

I

A

F

V

V

L

F

V

V

G

G

P

P

T

T

L

V

L

S

I

I

L

L

N

N

M

L

F

L

T

P

E

G

T

S

F

I

G

G

M

N

Y

Y

M

L

Q

S

N

N

I

F

Q

Q

T

M

S

A

F

G

R

R

T

T

S

A

P

M

L

S

E

A

S

D

D

G

N

T

R

A

G

G

-

E

W

W

L

L

D

G

A

S

W

W

T

T

I

I

F

F

Y

Y

W

W

A

A

W
|
W

I

I

S

S

W
|
W

A

S

P

P

F

F

V

V

G

G

M

M

F

F

I

L

A

A

R

R

V

I

S

S

R

R

G

G

R

R

T

S

I

I

R

R

Q

E

F

F

M

I

T

L

G

G

V

V

L

L

I

L

L

V

P

P

T

A

L

G

L

V

V

S

S

T

I

V

W

W

Y

F

A

S

T

I

F

F

G

G

T

G

T

T

A

A

G

I

N

V

V

F

Q

E

N

Q

S

N

G

G

V

E

E

S

L

I

-

W

T

G

Q

D

Y

G

T

A

E

E

L

E

V

Q

L

L

F

F

N

G

M

L

F

L

D

H

Q

A

L

L

P

P

L

G

S

G

L

Q

V

I

L

M

S

G

V

I

I

I

A

A

I

M

L

I

L

L

I

L

G

G

S

T

F
|
F

F

F

I

I

T
|
T

S
|
S

A

A

D

D

S

S

A

A

T

S

F

T

V

V

L

M

G

G

M

T

Q

M

S

S

T

Q

H

H

G

G

S

Q

L

L

E

E

P

A

A

N

N

K

K

W

I

V

K

T

I

A

A

A

W

W

G

G

I

V

A

A

Q

T

S

A

V

I

A

G

L

L

I

T

L

L

Y

L

V

S

G

G

-

D

-

N

-

A

L

L

Q

S

A

N

I

L

Q

Q

N

N

T

V

I

T

I

I

V

V

A

A

L

T

P

P

F

F

S

L

F

F

V

V

M

V

I

I

L

G

M

L

I

M

I

F

A

A

L

L

F

V

K

K

A

D

L

L

N

S

K

N

E

D

V

V

Q

I

A

Y

I

L

K

E

G

Y

R
|
R

binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M95), G95 (= G96), D97 (≠ G98), W314 (= W318), W315 (= W319), W318 (= W322)
binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (= R495)
binding sodium ion: A91 (≠ S92), M94 (= M95), G95 (= G96), F405 (= F408), T408 (= T411), S409 (= S412)

Sites not aligning to the query:

binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: 499

8ybqA Choline transporter bett - cht bound (see paper)
36% identity, 98% coverage: 5:490/496 of query aligns to 7:498/502 of 8ybqA

query
sites
8ybqA

S

A

R

P

V

V

F

F

Y

Y

I

F

T

A

V

A

A

S

L

F

V

I

I

L

I

I

T

F

V

G

I

I

F

I

G

V

A

I

I

A

F

F

P

P

T

Q

Q

A

F

S

E

G

A

A

I

W

T

L

G

L

S

A

I

A

K

Q

S

N

Y

W

V

A

A

A

T

N

T

T

F

V

G

G

W

W

Y

Y

M

M

L

M

L

V

M

M

S

T

A

L

L

Y

V

L

I

V

V

F

A

V

I

V

F

V

I

T

A

A

V

L

S

S

P

G

M

F

G

G

K

K

I

I

R

K

L

L

G

G

K

A

D

D

N

H

D

D

R

E

P

P

D

E

F

F

S

S

T

Y

A

L

T

S

W

W

V

A

A

G

M

M

L

L

F

F

S

A

A

A

G
|
G

M

I

G

S

I

I

G

T

L

L

V

F

F

F

Y

F

G

C

A

V

A

S

E

E

P

P

L

L

F

T

H

H

Y

L

M

L

S

-

D

Q

A

P

P

P

T

Q

A

G

E

E

E

G

G

G

S

T

G

A

Q

E

A

A

F

A

K

R

E

Q

G

G

L

M

S

Q

Y

L

A

L

Y

F

F

L

H

H

W

W

G

G

L

L

H

H

V

G

W

W

A

G

M

V

Y

F

G

A

V

F

T

V

A

G

L

M

A

A

L

L

A

A

F

Y

F

F

Q

A

F

Y

R

R

K

H

D

N

E

L

P

P

G

L

L

A

I

L

S

R

S

S

T

A

L

L

K

Y

P

P

L

L

F

I

G

G

K

K

K

R

M

I

D

N

G

G

P

P

L

I

G

G

T

Y

L

A

I

V

D

D

V

G

L

F

A

G

V

I

F

I

A

A

T

T

V

I

F

F

G

G

V

L

A

G

T

A

S

D

L

M

G

G

F

F

G

G

A

V

V

L

Q

H

I

L

N

N

G

S

G

G

L

L

S

D

H

Y

L

L

F

F

N

G

F

V

E

P

V

-

G

-

F

-

T

H

S

T

Q

Q

F

W

I

I

I

Q

I

V

T

G

V

L

V

I

T

T

L

L

L

M

F

M

-

G

-

A

L

I

I

L

S

V

A

A

W

I

S

A

G

G

L

V

S

D

K

K

G

G

I

V

K

R

Y

V

L

M

S

S

N

D

T

I

N

N

M

M

V

L

L

L

S

A

I

C

I

A

L

L

I

L

A

F

V

V

L

L

V

F

V

A

G

G

P

P

T

T

L

Q

L

H

I

L

L

L

N

N

M

T

F

L

T

V

E

Q

T

N

F

I

G

G

M

D

Y

Y

M

L

Q

G

N

A

I

L

I

P

Q

S

T

K

S

S

F

F

R

D

T

V

S

Y

P

A

L

Y

E

N

S

K

D

P

N

S

R

D

G

-

W

W

L

L

D

G

A

G

W

W

T

T

I

V

F

F

Y

Y

W

W

A

A

W
|
W

I

I

S

A

W

W

A

A

P

P

F

F

V

V

G

G

M

L

F

F

I

I

A

A

R

R

V

I

S

S

R

R

G

G

R

R

T

T

I

I

R

R

Q

E

F

F

M

V

T

F

G

G

V

V

L

L

I

L

L

I

P

P

T

L

L

G

L

F

V

T

S

L

I

A

W

W

Y

M

A

S

T

I

F

F

G

G

T

N

T

S

A

A

-

I

G

D

N

Q

V

V

Q

L

N

N

S

H

G

G

V

M

-

A

E

A

L

L

T

G

Q

Q

Y

S

T

A

T

I

E

D

-

D

-

P

-

S

L

M

V

T

L

L

F

Y

N

L

M

L

F

L

D

E

Q

T

L

Y

P

P

L

W

S

S

L

K

V

T

L

V

S

I

V

A

I

V

A

T

I

V

L

F

L

I

I

S

G

F

S

V

F

F

I

V

T

T

S

S

A

A

D

D

S

S

A

G

T

T

F

V

V

V

L

L

G

S

M

T

Q

L

S

S

T

A

H

K

G

G

S

G

L

N

E

P

P

D

A

E

N

D

K

G

-

P

-

K

-

W

I

L

K

R

I

V

A

F

W

W

G

G

I

V

A

A

Q

T

S

A

S

L

V

I

A

T

L

S

I

G

L

L

Y

F

V

S

G

G

G

S

L

I

Q

D

A

A

I

L

Q

K

N

S

T

A

I

V

V

L

A

T

A

S

L

L

P

P

F

F

S

S

F

L

V

I

M

L

I

L

L

L

M

M

I

M

I

W

A

G

L

L

F

H

K

K

A

A

L

F

N

V

K

M

E

E

V

S

Q

Q

binding choline ion: G96 (= G94), W318 (= W318), W319 (= W319)

3hfxA Crystal structure of carnitine transporter (see paper)
31% identity, 93% coverage: 30:488/496 of query aligns to 26:490/493 of 3hfxA

query
sites
3hfxA

E

N

A

V

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

V

L

M

V

L

I

F

V

G

A

W

I

F

F

W

I

L

A

V

V

F

S

G

P

P

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

-

D

-

N

N

D

E

R

P

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E

E

P

-

L

I

F

Y

H
x
Y

Y

Y

M

I

S

S

D

T

A

P

P

P

T

F

A

G

E

L

E

E

G

P

S

N

G

S

Q

T

A

G

F

A

K

K

E

E

-

L

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W
|
W

G

G

L

P

H

L

V

P

W

W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

V

P

P

L

L

F

V

G

G

K

E

K

K

M

H

-

A

D

K

G

G

P

L

L

F

G

G

T

T

L

I

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

F

G

A

V

M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

M

S

Q

H

W

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

T

V

C

V

W

T

I

L

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

C

G

G

L

L

S

Q

K

K

G

G

I

V

K

R

Y

I

L

A

S

S

N

D

T

V

N

R

M

S

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

S

P

G

T

A

L

S

L

F

I

I

L

M

N

N

M

Y

F

F

T

T

E

D

T

S

F

V

G

G

M

M

Y

L

M

L

Q

M

N

Y

I

L

I

P

Q

R

T

M

S

L

F

F

R

Y

T

T

S

D

P

P

L

I

E

A

S

K

D

G

N

-

R

-

G

G

W

F

L

P

D

Q

A

G

W
|
W

T

T

I

V

F

F

Y

Y

W

W

A

A

W
|
W

I

V

S

I

W
x
Y

A

A

P

I

F
x
Q

V

M

G

S

M

I

F
|
F

I

L

A

A

R

R

V

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

M

C

T

F

G

G

V

M

L

V

I

L

L

G

P

L

T

T

L

A

L

S

V

T

S

W

I

I

W

L

Y

W

A

T

T

V

F

L

G

G

T

S

T

N

A

T

-

L

-

I

-

D

G

K

N

N

V

I

Q

I

N

N

S

I

G

P

V

N

E

L

L

I

T

E

Q

Q

Y

Y

T

G

T

V

E

A

L

R

V

A

L

I

F

I

N

E

M

T

F

W

D

A

Q

A

L

L

P

P

L

L

S

S

-

T

-

A

-

T

-

M

-

W

-

G

-

F

L

F

V

I

L

L

S

C

V

F

I

I

A

A

I

T

L

-

I

-

G

-

S

-

F

-

I

V

T

T

S

L

A

V

D

N

S

A

A

C

T

S

F

Y

V

T

L

L

G

A

M

M

-

S

-

T

-

C

Q

R

S

E

T

V

H

R

G

D

S

G

L

E

E

E

P

P

A

P

N

L

K

L

I

V

K

R

I

I

A

G

W

W

G

S

I

I

A

L

Q

V

S

G

S

I

V

I

A

G

L

I

I

V

L

L

Y

A

V

L

G

G

L

L

Q

K

A

P

I

I

Q

Q

N

T

T

A

I

I

V

A

A

G

L

C

P

P

F

L

S

F

F

F

V

V

M

N

I

I

L

M

M

V

I

T

I

L

A

S

L

F

F

I

K

K

A

D

L

A

N

K

K

Q

E

N

binding carnitine: Y103 (≠ H110), W131 (= W137), W305 (= W311), W312 (= W318), W313 (= W319), Y316 (≠ W322), Y316 (≠ W322), Q319 (≠ F325), F323 (= F329)

P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
31% identity, 93% coverage: 30:488/496 of query aligns to 37:501/504 of P31553

query
sites
P31553

E

N

A

V

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

V

L

M

V

L

I

F

V

G

A

W

I

F

F

W

I

L

A

V

V

F

S

G

P

P

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

-

D

-

N

N

D

E

R

P

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E

E

P

-

L

I

F

Y

H
x
Y

Y

Y

M

I

S

S

D

T

A

P

P

P

T

F

A

G

E

L

E

E

G

P

S

N

G

S

Q

T

A

G

F

A

K

K

E

E

-

L

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W
|
W

G

G

L

P

H

L

V

P

W

W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

V

P

P

L

L

F

V

G

G

K

E

K

K

M

H

-

A

D

K

G

G

P

L

L

F

G

G

T

T

L

I

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

F

G

A

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M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

M

S

Q

H

W

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

T

V

C

V

W

T

I

L

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

C

G

G

L

L

S

Q

K

K

G

G

I

V

K

R

Y

I

L

A

S

S

N

D

T

V

N

R

M

S

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

S

P

G

T

A

L

S

L

F

I

I

L

M

N

N

M

Y

F

F

T

T

E
x
D

T

S

F

V

G

G

M

M

Y

L

M

L

Q
x
M

N

Y

I

L

I

P

Q
x
R

T

M

S

L

F

F

R

Y

T
|
T

S

D

P

P

L

I

E

A

S

K

D

G

N

-

R

-

G

G

W

F

L

P

D

Q

A
x
G

W
|
W

T

T

I

V

F

F

Y

Y

W

W

A

A

W
|
W

I

V

S

I

W
x
Y

A
|
A

P
x
I

F
x
Q

V
x
M

G

S

M

I

F

F

I

L

A

A

R

R

V

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

M

C

T

F

G

G

V

M

L

V

I

L

L

G

P

L

T

T

L

A

L

S

V

T

S

W

I

I

W

L

Y

W

A

T

T

V

F

L

G

G

T

S

T

N

A

T

-

L

-

I

-

D

G

K

N

N

V

I

Q

I

N

N

S

I

G

P

V

N

E

L

L

I

T

E

Q

Q

Y

Y

T

G

T

V

E

A

L

R

V

A

L

I

F

I

N

E

M

T

F

W

D

A

Q

A

L

L

P

P

L

L

S

S

-

T

-

A

-

T

-

M

-

W

-

G

-

F

L

F

V

I

L

L

S

C

V

F

I

I

A

A

I

T

L

-

I

-

G

-

S

-

F

-

I

V

T

T

S

L

A

V

D

N

S

A

A

C

T

S

F

Y

V

T

L

L

G

A

M

M

-

S

-

T

-

C

Q

R

S

E

T

V

H

R

G

D

S

G

L

E

E

E

P

P

A

P

N

L

K

L

I

V

K

R

I

I

A

G

W

W

G

S

I

I

A

L

Q

V

S

G

S

I

V

I

A

G

L

I

I

V

L

L

Y

A

V

L

G

G

L

L

Q

K

A

P

I

I

Q

Q

N

T

T

A

I

I

V

A

A

G

L

C

P

P

F

L

S

F

F

F

V

V

M

N

I

I

L

M

M

V

I

T

I

L

A

S

L

F

F

I

K

K

A

D

L

A

N

K

K

Q

E

N

Y114 (≠ H110) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
W142 (= W137) binding (R)-carnitine
D288 (≠ E281) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
M295 (≠ Q288) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
R299 (≠ Q292) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
T304 (= T297) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
GW 315:316 (≠ AW 310:311) binding 4-(trimethylamino)butanoate
W316 (= W311) mutation to L: Decrease in transport activity.
W323 (= W318) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
WW 323:324 (= WW 318:319) binding (R)-carnitine
W324 (= W319) mutation to L: Abolishes transport activity.
Y327 (≠ W322) mutation to L: Strong decrease in transport activity.
YAIQ 327:330 (≠ WAPF 322:325) binding (R)-carnitine
Q330 (≠ F325) mutation to L: Decrease in transport activity.
M331 (≠ V326) binding 4-(trimethylamino)butanoate

2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
30% identity, 93% coverage: 30:488/496 of query aligns to 30:494/496 of 2wsxA

query
sites
2wsxA

E

N

A

V

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

V

L

M

V

L

I

F

V

G

A

W

I

F

F

W

I

L

A

V

V

F

S

G

P

P

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

E

D

E

N

P

D

-

R

-

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E

E

P

-

L

I

F

Y

H

Y

Y

Y

M

I

S

S

D

T

A

P

P

P

T

F

A

G

E

L

E

E

G

P

S

N

G

S

Q

T

A

G

F

A

K

K

E

E

-

L

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W
|
W

G

G

L

P

H

L

V

P

W

W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

V

P

P

L

L

F

V

G

G

K

E

K

K

M

H

-

A

D

K

G

G

P

L

L

F

G

G

T

T

L

I

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

F

G

A

V

M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

M

S

Q

H

W

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

T

V

C

V

W

T

I

L

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

C

G

G

L

L

S

Q

K

K

G

A

I

V

K

R

Y

I

L

A

S

S

N

D

T

V

N

R

M

S

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

S

P

G

T

A

L

S

L

F

I

I

L

M

N

N

M

Y

F

F

T

T

E

D

T

S

F

V

G

G

M

M

Y

L

M

L

Q

M

N

Y

I

L

I

P

Q

R

T

M

S

L

F

F

R

Y

T

T

S

D

P

P

L

I

E

A

S

K

D

G

N

-

R

-

G
|
G

W

F

L

P

D

Q

A
x
G

W

W

T

T

I

V

F

F

Y

Y

W

W

A

A

W
|
W

W

W

I

V

S

I

W
x
Y

A

A

P

I

F

Q

V
x
M

G

S

M

I

F

F

I

L

A

A

R

R

V

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

M

C

T

F

G

G

V

M

L

V

I

L

L

G

P

L

T

T

L

A

L

S

V

T

S

W

I

I

W

L

Y

W

A

T

T

V

F

L

G

G

T

S

T

N

A

T

-

L

-

I

-

D

G

K

N

N

V

I

Q

L

N

N

S

I

G

P

V

N

E

L

L

I

T

E

Q

Q

Y

Y

T

G

T

V

E

A

L

R

V

A

L

I

F

I

N

E

M

T

F

W

D

A

Q

A

L

L

P

P

L

L

S

S

-

T

-

A

-

T

-

M

-

W

-

G

-

F

L

F

V

I

L

L

S

C

V

F

I

I

A

A

I

T

L

-

I

-

G

-

S

-

F

-

I

V

T

T

S

L

A

V

D

N

S

A

A

C

T

S

F

Y

V

T

L

L

G

A

M

M

-

S

-

T

-

C

Q

R

S

E

T

V

H

R

G

D

S

G

L

E

E

D

P

P

A

P

N

L

K

L

I

V

K

R

I

I

A

G

W

W

G

S

I

I

A

L

Q

V

S

G

S

I

V

I

A

G

L

I

I

V

L

L

Y

A

V

L

G

G

L

L

Q

K

A

P

I

I

Q
|
Q

N

T

T

A

I

I

V

A

A

G

L

C

P

P

F

L

S

F

F

F

V

V

M

N

I

I

L

M

M

V

I

T

I

L

A

S

L

F

F

I

K

K

A

D

L

A

N

K

K

Q

E

N

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W135 (= W137), G304 (= G306), G308 (≠ A310), W316 (= W318), Y320 (≠ W322), M324 (≠ V326), Q466 (= Q460)

B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
32% identity, 92% coverage: 30:483/496 of query aligns to 37:496/514 of B4EY22

query
sites
B4EY22

E

N

A

E

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

I

L

M

V

F

I

G

V

G

A

W

I

F

F

W

I

L

A

V

V

F

S

G

P

R

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

-

D

-

N

D

D

E

R

K

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E
|
E

P

-

L

I

F

Y

H

Y

Y

Y

M

I

S

S

D

S

A

P

P

P

T

F

A

G

E

M

E

E

G

G

S

Y

G

S

Q

A

A

P

F

A

K

K

E

E

-

I

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W

W

G

G

L

P

H

L

V

P

W

W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

T

P

P

L

L

F

V

G

G

K

E

K

K

-

H

M

V

D

N

G

G

P

L

L

F

G

G

T

T

L

V

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

L

G

A

V

M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

I

S

Q

H

Y

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

S

V

C

V

W

T

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

F

G

G

L

L

S

Q

K

K

G

G

I

V

K

K

Y

I

L

A

S

S

N

D

T

V

N
x
R

M

T

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

G

P

G

T

A

L

S

L

F

I

I

L

V

N

N

M

Y

F

F

T

T

E

D

T

S

F

V

G

G

M

T

Y

L

M

L

Q

M

N

Y

I

M

I

P

Q

R

T

M

S

L

F

F

R

Y

T

T

S

D

P

P

L

I

E

-

S

-

D

G

N

K

R

G

G

G

W

F

L

P

D

Q

A

A

W
|
W

T

T

I

V

F

F

Y

Y

W

W

A

A

W

W

I

V

S

I

W

Y

A

A

P

I

F

Q

V
x
M

G

S

M

I

F

F

I

L

A

A

R

R

V

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

M

C

T

L

G

G

V

M

-

V

-

S

-

G

L

L

I

T

L

A

P

G

T

T

L

W

L

L

V

-

S

-

I

I

W

W

Y

T

A

I

T

L

F

G

G

G

T

N

T

T

-

L

-

Q

-

L

-

I

A

D

G

Q

N

N

V

I

Q

L

N

N

S

I

G

P

V

Q

E

L

L

I

T

D

Q

Q

Y

Y

T

G

T

V

E

P

L

R

V

A

L

I

F

I

N

E

M

T

F

W

D

A

Q

A

L

L

P

P

L

L

S

S

L

T

V

A

L

T

S

M

V

W

I

G

A

F

I

F

L

I

L

L

I

C

G

F

S

I

F

A

F

T

I

V

T

T

S

L

A

I

D

N

S

A

A

C

T

S

F

Y

V

T

L

L

G

A

M

M

-

S

-

T

-

C

Q

R

S

S

T

M

H

K

G

E

S

G

L

A

E

E

P

P

A

P

N

L

K

L

I

V

K

R

I

I

A

G

W

W

G

S

I

V

A

L

Q

V

S

G

S

I

V

I

A

G

L

I

I

I

L

L

Y

A

V

L

G

G

L

L

Q

K

A

P

I

I

Q

Q

N

T

T

A

I

I

V

A

A

G

L

C

P

P

F

L

S

F

F

F

V

V

M

N

I

I

L

M

M

V

I

T

I

L

A

S

L

F

F

I

K

K

E111 (= E106) mutation to A: Abolishes transport activity.
R262 (≠ N255) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
W316 (= W311) mutation to A: 2.5-fold decrease in Vmax.
M331 (≠ V326) mutation to V: 10-fold decrease in Vmax.

2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
32% identity, 92% coverage: 30:483/496 of query aligns to 42:501/508 of 2wswA

query
sites
2wswA

E

N

A

E

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

I

L

M

V

F

I

G

V

G

A

W

I
x
F

F

W

I

L

A

V

V
x
F

S

G

P
x
R

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

-

D

-

N

D

D

E

R

K

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E

E

P

-

L

I

F

Y

H

Y

Y

Y

M

I

S

S

D

S

A

P

P

P

T

F

A

G

E

M

E

E

G

G

S

Y

G

S

Q

A

A

P

F

A

K

K

E

E

-

I

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W

W

G

G

L

P

H

L

V

P

W

W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

V

P

P

L

L

F

V

G

G

K

E

K

K

-

H

M

V

D

N

G

G

P

L

L

F

G

G

T

T

L

V

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

L

G

A

V

M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

I

S

Q

H

Y

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

S

V

C

V

W

T

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

F

G

G

L

L

S

Q

K

K

G

G

I

V

K

K

Y

I

L

A

S

S

N

D

T

V

N

R

M

T

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

G

P

G

T

A

L

S

L

F

I

I

L

V

N

N

M

Y

F

F

T

T

E

D

T

S

F

V

G

G

M

T

Y

L

M

L

Q

M

N

Y

I

M

I

P

Q

R

T

M

S

L

F

F

R

Y

T

T

S

D

P

P

L

I

E

-

S

-

D

G

N

K

R

G

G

G

W

F

L

P

D

Q

A

A

W

W

T

T

I

V

F

F

Y

Y

W

W

A

A

W

W

I

V

S

I

W

Y

A

A

P

I

F

Q

V

M

G

S

M

I

F

F

I

L

A

A

R

R

V

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

M

C

T

L

G

G

V

M

-

V

-

S

-

G

L

L

I

T

L

A

P

G

T

T

L

W

L

L

V

-

S

-

I

I

W

W

Y

T

A

I

T

L

F

G

G

G

T

N

T

T

-

L

-

Q

-

L

-

I

A

D

G

Q

N

N

V

I

Q

L

N

N

S

I

G

P

V

Q

E

L

L

I

T

D

Q

Q

Y

Y

T

G

T

V

E

P

L

R

V

A

L

I

F

I

N

E

M

T

F

W

D

A

Q

A

L

L

P

P

L

L

S

S

L

T

V

A

L

T

S

M

V

W

I

G

A

F

I

F

L

I

L

L

I

C

G

F

S

I

F

A

F

T

I

V

T

T

S

L

A

I

D

N

S

A

A

C

T

S

F

Y

V

T

L

L

G

A

M

M

Q

S

S

T

T

C

H

R

G

S

S

M

L

K

E

E

P

G

A

A

N

D

K

P

-

P

-

L

I

V

K

R

I

I

A

G

W

W

G

S

I

V

A

L

Q

V

S

G

S

I

V

I

A

G

L

I

I

I

L

L

Y

A

V

L

G

G

L

L

Q

K

A

P

I

I

Q

Q

N

T

T

A

I

I

V

A

A

G

L

C

P

P

F

L

S

F

F

F

V

V

M

N

I

I

L

M

M

V

I

T

I

L

A

S

L

F

F

I

K

K

binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: F72 (≠ I60), F76 (≠ V64), R78 (≠ P66)

4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
32% identity, 92% coverage: 30:483/496 of query aligns to 29:488/495 of 4m8jA

query
sites
4m8jA

E

N

A

E

I

V

T

I

G

N

S

A

I

V

K

F

S

S

Y

Y

V

V

A

T

T

N

T

V

F

W

G

G

W

W

Y

A

Y

F

M

E

L

W

L

Y

M

M

S

V

A

I

L

M

V

F

I

G

V

G

A

W

I

F

F

W

I

L

A

V

V

F

S

G

P

R

M

Y

G

A

K

K

I

K

R

R

L

L

G

G

K

-

D

-

N

D

D

E

R

K

P

P

D

E

F

F

S

S

T

T

A

A

T

S

W

W

V

I

A

F

M

M

L

M

F

F

S

A

A

S

G

C

M

T

G

S

I

A

G

A

L

V

V

L

F

F

Y

W

G

G

A

S

A

I

E

E

P

-

L

I

F

Y

H

Y

Y

Y

M

I

S

S

D

S

A

P

P

P

T

F

A

G

E

M

E

E

G

G

S

Y

G

S

Q

A

A

P

F

A

K

K

E

E

-

I

G

G

L

L

S

A

Y

Y

A

S

Y

L

F

F

H

H

W

W

G

G

L

P

H

L

V

P

W
|
W

A

A

M

T

Y

Y

G

S

V

F

T

L

A

S

L

V

A

A

L

F

A

A

F

Y

F

F

Q

F

F

F

-

V

R

R

K

K

D

M

E

E

P

V

G

I

L

R

I

P

S

S

T

T

L

L

K

V

P

P

L

L

F

V

G

G

K

E

K

K

-

H

M

V

D

N

G

G

P

L

L

F

G

G

T

T

L

V

I

V

D

D

V

N

L

F

A

Y

V

L

F

V

A

A

T

L

V

I

F

L

G

A

V

M

A

G

T

T

S

S

L

L

G

G

F

L

G

A

A

T

V

P

Q

L

I

V

N

T

G

E

G

C

L

I

S

Q

H

Y

L

L

F

F

N

G

F

I

E

P

V

H

G

T

F

L

T

Q

S

L

Q

D

F

A

I

I

T

S

V

C

V

W

T

I

L

L

F

N

L

A

I

I

S

C

A

V

W

A

S

F

G

G

L

L

S

Q

K

K

G

G

I

V

K

K

Y

I

L

A

S

S

N

D

T

V

N

E

M

T

V

Y

L

L

S

S

I

F

I

L

L

M

L

L

I

G

A

W

V

V

L

F

V

I

V

V

G

G

P

G

T

A

L

S

L

F

I

I

L

V

N

N

M

Y

F

F

T

T

E

D

T

S

F

V

G

G

M

T

Y

L

M

L

Q

M

N

Y

I

M

I

P

Q

R

T

M

S

L

F

F

R

Y

T

T

S

D

P

P

L

I

E

-

S

-

D

G

N

K

R

G

G

G

W

F

L

P

D

Q

A

A