SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_068692422.1 NCBI__GCF_001660385.1:WP_068692422.1 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 4 hits to proteins with known functional sites (download)

P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
36% identity, 92% coverage: 25:335/338 of query aligns to 12:318/318 of P15029

query
sites
P15029

A

A

L

L

A

A

G

G

A

C

L

A

L

L

S

S

L

L

A

H

V

M

G

G

S

V

K

I

P

P

T

V

A

P

P

-

D

-

Q

-

V

-

W

W

A

R

A

A

L

L

T

L

G

T

T

D

A

W

D

Q

-

A

-

G

-

H

P

E

H

H

T

Y

A

V

V

L

V

M

E

E

S

Y

R
|
R

H

L

P

P

R
|
R

T

L

A

L

L

L

G

A

V

L

L

F

A

V

G

G

A

A

L

L

A

A

L

V

A

A

G

G

L

V

L

L

M

I

Q

Q

G

G

I

I

T

V

R

R

N

N

P

P

L

L

A

A

D

S

P

P

G

D

L

I

L

L

G

G

V

V

N

N

A

H

G

A

A

A

A

S

A

L

A

A

V

S

V

V

T

G

A

A

T

L

A

L

I

L

L

M

G

P

P

S

A

L

S

P

T

V

A

M

A

V

T

L

V

P

W

L

A

A

L

F

P

A

G

G

A

G

L

M

A

A

A

-

G

G

L

L

V

I

A

L

Y

L

S

K

V

M

G

L

G

A

R

K

E

T

S

H

G

Q

G

-

T

P

V

M

R

K

L

L

V

A

L

L

A

T

G

G

A

V

V

A

V

L

S

S

A

A

V

C

L

W

T

A

A

S

Y

L

V

T

Q

D

A

Y

V

L

S

M

L

L

N

S

M

R

P

P

E

Q

V

D

F

V

D

N

S

N

Y

A

R

L

Y

L

W

W

V

L

V

T

G

G

S

S

L

L

A

W

G

G

R

R

G

D

F

W

D

S

A

F

A

V

V

K

A

I

V

A

L

I

P

P

F

L

V

M

A

I

V

L

G

F

A

L

L

P

L

L

A

S

L

L

L

S

L

F

A

C

G

R

G

D

L

L

N

D

A

L

L

L

A

A

L

L

G

G

E

D

E

A

T

R

A

A

T

T

S

T

L

L

G

G

A

V

N

S

P

V

V

P

L

H

V

T

R

R

S

F

G

W

G

A

L

L

V

L

A

L

A

A

T

V

L

A

L

M

A

T

A

S

G

T

A

G

T

V

A

A

A

C

G

G

P

P

I

I

A

S

F

F

V

I

G

G

L

L

A

V

V

V

P

P

H

H

V

M

R

R

A

S

L

I

V

T

G

G

D

R

F

H

R

R

H

R

Q

L

V

L

P

P

L

V

A

S

L

A

L

L

A

T

G

G

P

A

A

L

L

L

L

V

A

A

D

D

V

L

G

A

R
|
R

F

I

V

I

L

H

R

P

P

P

T

L

E

E

L

L

M

P

V

V

G

G

V

V

V

L

T

T

A

A

F

I

V

I

G

G

A

A

P

P

F

W

L

F

F

V

Y

W

A

L

V

L

R

V

R

R

M

M

R

R

R51 (= R65) mutation to C: Retains 32% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 14% of wild-type citrate-mediated Fe(3+) transport.
R54 (= R68) mutation to C: Retains 19% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 24% of wild-type citrate-mediated Fe(3+) transport.
R288 (= R305) mutation to C: Retains 65% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 35% of wild-type citrate-mediated Fe(3+) transport.

P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
35% identity, 96% coverage: 9:333/338 of query aligns to 1:330/332 of P15030

query
sites
P15030

Q

M

T

T

G

A

T

I

A

K

R

H

T

P

T

V

L

L

L

W

G

G

G

L

A

P

A

V

A

A

L

L

A

I

G

I

A

I

L

F

L

W

L

L

S

S

L

L

A

F

V

C

G

Y

S

S

K

A

P

I

-

P

-

V

T

S

A

G

P

A

D

D

Q

A

V

T

W

R

A

A

A

L

L

L

T

P

G

G

T

H

A

T

D

P

P

T

H

L

T

P

T

E

A

A

V

L

V

V

E

Q

S

N

-

L

R
|
R

H

L

P

P

R
|
R

T

S

A

L

L

V

G

A

V

V

L

L

A

I

G

G

A

A

A

S

L

L

A

A

L

L

A

A

G

G

L

T

L

L

M

L

Q

Q

G

T

I

L

T

T

R

H

N

N

P

P

L

M

A

A

D

S

P

P

G

S

L

L

G

G

V

I

N

N

A

S

G

G

A

A

A

L

A

A

V

M

V

A

T

L

A

T

T

S

A

A

I

-

L

L

G

S

P

P

-

T

-

P

-

I

A

A

S

G

T

Y

A

S

A

L

T

S

V

F

W

I

W

A

A

A

L

C

P

G

G

G

A

G

L

V

A

S

A

W

G

L

L

L

V

V

A

M

Y

T

S

A

V

G

G

G

R

F

E

R

S

H

G

T

G

H

G

D

T

R

V

N

R

K

L

L

V

I

L

L

A

A

G

G

A

I

V

A

V

L

S

S

A

A

V

F

L

C

T

M

A

G

Y

L

V

T

Q

R

A

I

V

T

S

L

L

L

N

L

M

A

P

E

E

D

V

H

F

A

D

Y

S

G

Y

I

R

F

Y

Y

W

W

V

L

V

A

G

G

S

G

L

V

A

S

G

H

R

A

G

R

F

W

D

Q

A

D

A

V

V

W

A

Q

V

L

L

L

P

P

F

V

V

V

A

V

V

T

G

A

A

V

L

P

L

V

A

V

L

L

A

A

G

N

G

Q

L

L

N

N

A

L

L

L

A

N

L

L

G

S

E

D

E

S

T

T

A

A

T

H

S

T

L

L

G

G

A

V

N

N

P

L

V

T

L

R

V

L

R

R

S

L

G

V

G

I

L

N

V

M

A

L

A

V

T

L

L

L

A

V

A

G

G

A

A

C

T

V

A

S

A

V

A

A

G

G

P

P

I

V

A

A

F

F

V

I

G

G

L

L

A

L

V

V

P

P

H

H

V

L

V

A

R

R

A

F

L

W

V

A

G

G

G

F

D

D

F

Q

R

R

H

N

Q

V

V

L

P

P

L

V

A

S

L

M

L

L

A

L

G

G

P

A

A

T

L

L

L

M

L

L

A

A

D

D

V

V

V

L

G

A

R
|
R

F

A

V

L

L

A

R

F

P

P

T

G

E

D

L

L

M

P

V

A

G

G

V

A

V

V

T

L

A

A

F

L

V

I

G

G

A

S

P

P

F

C

L

F

F

V

Y

W

A

L

V

V

R

R

R60 (= R65) mutation to C: Retains 33% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 29% of wild-type citrate-mediated Fe(3+) transport.
R63 (= R68) mutation to C: Retains 74% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 30% of wild-type citrate-mediated Fe(3+) transport.
R302 (= R305) mutation to C: Retains 24% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 28% of wild-type citrate-mediated Fe(3+) transport.

5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
36% identity, 93% coverage: 22:335/338 of query aligns to 12:328/330 of 5b57A

query
sites
5b57A

A

A

A

L

A

A

A

I

L

L

A

M

G

G

A

A

L

M

-

S

L

V

S

A

L

L

A

C

V

V

G

G

S

A

K

Y

P

R

T

I

A

P

P

L

D

A

Q

E

V

A

W

W

A

A

L

L

T

S

G

G

T

D

-

P

-

A

A

A

D

Q

P

Q

H

A

T

R

T

A

A

V

V

L

E
x
D

S

I

R

R

H

A

P

P

R

R

T

V

A

V

L

L

G

A

V

L

L
|
L

A

V

G

G

A

G

L

F

A

G

L

A

A

T

G

G

L

A

M

M

Q

Q

G

A

I

L

T

F

R

R

N

N

P

P

L

L

A

A

D

D

P

P

G

G

L

L

L

V

G

G

V

V

N

S

A

S

G

G

A

A

A

L

A

G

V

A

V

T

T

T

A

L

T

I

A

-

I

V

L

L

G

G

P

P

A

A

S

S

T

A

A

A

T

L

V

P

W

V

W

A

A

A

L

F

P

A

G

G

A

G

L

L

A

A

A

V

G

A

L

A

V

L

A

V

Y

Y

S

R

V

L

G

A

R

S

E

R

S

G

G

R

G

L

G

A

T

L

V

P

R

L

L

L

V

L

L

L

A

A

G

G

A

I

V

A

V

I

S

N

A

A

V

L

L

V

T

G

A

A

Y

A

V

I

Q

G

A

L

V

L

S

T

L

F

N

V

M

A

P

D

E

D

V

A

-

Q

F

L

D

R

S

S

Y

L

R

T

Y

F

W

W

V

S

V

L

G

G

S

S

L

L

A

G

G

G

R

A

G

Q

F
x
W

D

P

A

T

A

L

V
x
A

A

A

V

V

L
x
A

P

P

F

C

V

V

A

A

V

L

G

G

A

G

L

V

L

L

A

L

L

V

L

R

L

E

A

R

G

D

G

A

L

L

N

N

A

A

L

L

A

Q

L

L

G

G

E

E

E

T

T

E

A

A

T

L

S

H

L

L

G

G

A

V

N

P

P

V

V

Q

L

R

V

L

R

K

S

R

G

R

G

V

L

L

V

V

A

A

A

V

T

A

L

L

L

A

A

V

A

G

G

A

A

L

T

V

A

S

A

C

A

A

G

G

P

I

I

I

A

G

F

F

V

I

G

G

L

L

A

V

V

A

P

P

H

H

V

C

V

V

R

R

A

L

L

A

V

C

G

G

G

P

D

D

F

Q

R

R

H

I

Q

V

V

L

P

P

L

G

A

A

L

A

L

L

A

L

G

G

P

A

A

L

L

L

L

T

L

L

L

A

A

A

D

D

V

L

V

A

G

A

R

R

F

T

V

V

L

A

R

A

P

P

T

A

E

D

L

I

M

P

V

L

G

G

V

V

V

L

T

T

A

A

F

L

V

L

G

G

A

A

P

P

F

F

L

F

F

L

Y

A

A

L

V

L

R

W

R

K

M

N

R

R

binding decyl-beta-d-maltopyranoside: D56 (≠ E63), L67 (= L74), W190 (≠ F197), A194 (≠ V201), A197 (≠ L204)

P06972 Iron(3+)-hydroxamate import system permease protein FhuB; Ferric hydroxamate uptake protein B; Ferrichrome transport system permease protein FhuB; Ferrichrome uptake protein FhuB; Iron(III)-hydroxamate import system permease protein FhuB from Escherichia coli (strain K12) (see paper)
33% identity, 92% coverage: 23:333/338 of query aligns to 349:657/660 of P06972

query
sites
P06972

A

A

A

F

A

A

L

L

A

A

G

G

A

G

L

V

L

L

S

L

L

M

A

A

V

V

G

V

S

-

K

-

P

-

T

-

A

-

P

-

D

-

Q

-

V

-

W

-

A

V

A

A

L

L

T

S

G

F

T

G

A

R

D

D

P

A

H

H

-

G

-

W

-

T

-

W

-

A

T

S

T

G

A

A

V

L

E

E

S

D

-

L

-

M

-

P

-

W

R
|
R

H

W

P

P

R

R

T

I

A

M

L

A

G

A

V

L

L

F

A

A

G

G

A

V

A

M

L

L

A

A

L

V

A

A

G

G

L

C

L

I

M

I

Q

Q

G

R

I

L

T

T

R

G

N

N

P

P

L

M

A

A

D

S

P

P

G

E

L

V

L

L

G

G

V

I

N

S

A

S

G

G

A

A

A

F

A

G

V

V

T

L

A

M

T

L

A

-

I

F

L

L

G

V

P

P

A

G

S

N

T

A

A

F

A

G

T

-

V

-

W

-

W

W

A

L

L

L

P

P

-

A

G

G

A

S

L

L

A

G

A

A

G

A

-

V

-

T

L

L

V

L

A

I

Y

I

S

M

V

I

G

A

R

G

E

R

S

G

G

G

G

F

G

S

T

P

V

H

R

R

L

M

V

L

L

L

A

A

G

G

A
x
M

V

A

V

L

S

S

A

T

V

A

L

F

T

T

A
x
M

Y

L

V

L

Q
x
M

A

M

V

L

S

Q

L

A

N

S

M

G

P

D

E

P

V

R

F

M

D

A

S
x
Q

Y

V

R

L

Y
x
T

W

W

V

I

V

S

G

G

S
|
S

L

-

A

T

G
x
Y

R

N

G

A

F

T

D

D

A

A

A

Q

V

V

A

W

V

R

L

T

P

G

F

I

V

V

A

M

V

V

G

-

A

I

L

L

A

A

L

I

-

T

-

P

L

L

L

C

A

R

G

R

G

W

L

L

N

T

A

I

L

L

A

P

L

L

G

G

E

G

E

D

T

T

A

A

T

R

S

A

L

V

G

G

A

M

N

A

P

L

V

T

L

P

V

T

R

R

S

I

G

A

G

L

L

L

V

L

A

L

A

A

T

A

L

C

L

L

A

T

A

A

G

T

A

A

T

T

A

M

A

T

A

I

G

G

P

P

I

L

A

S

F

F

V

V

G

G

L

L

A

M

V

A

P

P

H

H

V

I

V

A

R

R

A

M

L

M

V

-

G

-

D

G

F

F

R

R

H

R

Q

T

V

M

P

P

-

H

-

I

-

V

L

I

A

S

L

A

L

L

A

V

G

G

P

G

A

L

L

L

L

V

L

F

A

A

D

D

V

W

V

C

G

G

R

R

F

M

V

V

L

L

R

F

P

P

T

F

E
x
Q

L

I

M

P

V

A

G

G

V

L

T

S

A

T

F

F

V

I

G

G

A

A

P

P

F

Y

L

F

F

I

Y

Y

A

L

V

L

R

R

R

K

R390 (= R65) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ A160) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-492 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-492 and L-495.
M492 (≠ A168) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-495.
M495 (≠ Q171) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-492.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-492.
Q507 (≠ S183) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ Y186) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (= S191) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (≠ G194) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ E312) mutation to A: Decreased binding to ferrichrome-FhuD.

Sites not aligning to the query:

57 S→A: Decreased binding to ferrichrome-FhuD.
170 D→A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
171 Q→A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
175 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-484; A-492 and A-495.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-484; L-492 and L-495.
182 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
184 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
304 Interaction with FhuD; E→A: Decreased binding to ferrichrome-FhuD.

Query Sequence

>WP_068692422.1 NCBI__GCF_001660385.1:WP_068692422.1
MTTTTAPPQTGTARTTLLLGGAAAALAGALLLSLAVGSKPTAPDQVWAALTGTADPHTTA
VVESRHPRTALGVLAGAALALAGLLMQGITRNPLADPGLLGVNAGAAAAVVTATAILGPA
STAATVWWALPGALAAGLVAYSVGGRESGGGTVRLVLAGAVVSAVLTAYVQAVSLNMPEV
FDSYRYWVVGSLAGRGFDAAVAVLPFVAVGALLALLLAGGLNALALGEETATSLGANPVL
VRSGGLVAATLLAAGATAAAGPIAFVGLAVPHVVRALVGGDFRHQVPLALLAGPALLLLA
DVVGRFVLRPTELMVGVVTAFVGAPFLFYAVRRMRETP

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