SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_090442102.1 NCBI__GCF_900100495.1:WP_090442102.1 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)
35% identity, 94% coverage: 22:342/343 of query aligns to 1:318/318 of P15029

query
sites
P15029

L

M

R

K

L

I

G

A

L

L

A

V

L

I

A

F

I

I

T

T

L

L

L

A

L

L

M

A

-

G

-

C

-

A

L

L

A

L

S

S

L

L

S

H

L

M

G

G

K

V

V

I

N

P

L

V

S

P

P

W

L

R

A

A

V

L

L

L

R

T

I

D

L

W

F

Q

A

A

G

G

G

H

D

E

A

H

S

-

L

-

V

Y

F

Y

I

V

V

L

E

M

Q

E

L

Y

R
|
R

M

L

P

P

R
|
R

I

L

A

L

L

L

A

A

T

L

L

F

V

V

G

G

A

A

L

L

A

A

V

V

S

A

G

G

L

V

I

L

L

I

Q

Q

S

G

I

I

V

V

R

R

N

N

P

P

L

L

A

A

S

S

P

P

D

D

L

I

L

L

G

G

I

V

T

N

S

H

G

A

A

A

S

S

A

L

A

A

A

S

V

V

L

G

Y

A

L

L

S

-

F

L

C

L

A

M

A

P

A

S

L

L

G

P

P

V

Q

M

F

V

L

L

P

P

L

L

A

L

A

A

M

F

L

A

G

G

A

G

A

M

L

A

A

G

A

L

L

I

A

L

I

L

Y

K

L

M

L

L

A

A

W

-

K

-

Q

K

G

T

A

H

S

Q

P

P

L

M

R

K

L

L

V

A

L

L

I

T

G

G

V

V

G

A

V

L

S

S

A

A

M

C

L

W

A

A

A

S

A

L

T

T

T

D

F

Y

V

L

L

M

V

L

F

S

S

R

P

P

L

Q

T

D

T

V

T

N

L

-

S

N

A

A

Y

L

V

L

W

W

L

L

T

T

G

G

S

S

V

L

Y

W

G

G

A

R

S

D

W

W

P

S

E

F

P

V

R

K

A

I

L

A

A

I

G

P

W

L

L

M

L

I

A

L

I

F

L

L

P

P

L

L

L

S

L

L

L

S

L

F

A

C

R

R

H

D

V

L

R

D

V

L

Q

L

Q

A

L

L

D

G

D

D

G

A

L

R

A

A

Q

T

G

T

I

L

G

G

V

V

R

S

V

V

Q

P

W

H

L

T

R

R

A

F

G

W

L

A

L

L

V

L

S

A

V

V

A

A

L

M

A

T

G

S

A

T

A

G

I

V

A

A

W

A

G

C

G

G

A

P

M

I

A

S

F

F

V

I

G

G

L

L

I

V

A

V

P

P

H

H

I

M

A

M

K

R

R

S

L

I

V

T

A

G

P

G

G

R

F

H

A

R

G

R

Q

L

A

L

A

P

M

V

A

S

A

A

L

L

A

T

G

G

A

A

N

L

L

L

V

L

M

V

L

V

A

A

D

D

L

L

A

L

G

A

R
|
R

T

I

L

I

F

H

L

P

P

P

L

L

D

E

L

L

P

P

A

V

G

G

I

V

F

L

V

T

A

A

V

I

L

I

G

G

T

A

P

P

F

W

F

F

L

V

Y

W

L

L

I

V

K

R

Q

M

R

R

R51 (= R71) 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 (= R74) 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 (= R312) 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)
32% identity, 80% coverage: 66:341/343 of query aligns to 55:331/332 of P15030

query
sites
P15030

I

L

V

V

E

Q

Q

N

L

L

R
|
R

M

L

P

P

R
|
R

I

S

A

L

L

V

A

A

T

V

L

L

V

I

G

G

A

A

A

S

L

L

A

A

V

L

S

A

G

G

L

T

I

L

L

L

Q

Q

S

T

I

L

V

T

R

H

N

N

P

P

L

M

A

A

S

S

P

P

D

S

L

L

G

G

I

I

T

N

S

S

G

G

A

A

S

A

A

L

A

A

A

M

V

A

L

L

Y

T

L

S

S

A

F

L

C

S

A

P

A

T

A

P

L

I

G

A

P

G

Q

Y

F

S

L

L

P

S

L

F

A

I

A

A

M

A

L

C

G

G

A

G

L

V

A

S

A

W

L

L

A

L

I

V

Y

M

L

T

L

A

-

G

A

G

W

F

K

R

Q

H

G

T

A

H

S

D

P

R

L

N

R

K

L

L

V

I

L

L

I

A

G

G

V

I

G

A

V

L

S

S

A

A

M

F

L

C

A

M

A

G

A

L

T

T

T

R

F

I

V

T

L

L

V

L

F

L

S

A

P

E

L

-

T

D

T

H

T

A

L

Y

S

G

A

I

Y

F

V

Y

W

W

L

L

T

A

G

G

S

G

V

V

Y

S

G

H

A

A

S

R

W

W

P

Q

E

D

P

V

R

W

A

Q

L

L

A

L

G

P

W

V

L

V

A

T

I

A

L

V

P

P

L

V

L

L

A

A

R

N

H

Q

V

L

R

N

V

L

Q

L

Q

N

L

L

D

S

D

D

G

S

L

T

A

A

Q

H

G

T

I

L

G

G

V

V

R

N

V

L

Q

T

W

R

L

L

R

R

A

L

G

V

L

I

L

N

L

M

V

L

S

V

V

L

A

L

L

L

A

V

G

G

A

A

A

C

I

V

A

S

W

V

G

A

G

G

A

P

M

V

A

A

F

F

V

I

G

G

L

L

I

L

A

V

P

P

H

H

I

L

A

A

K

R

R

F

L

W

V

A

A

G

P

F

G

D

F

Q

A

R

G

N

Q

V

A

L

A

P

M

V

A

S

A

M

L

L

A

L

G

G

A

A

N

T

L

L

V

M

M

L

L

L

A

A

D

D

L

V

A

L

G

A

R
|
R

T

A

L

L

F

A

L

F

P

P

L

G

D

D

L

L

P

P

A

A

G

G

I

A

F

V

V

L

A

A

V

L

L

I

G

G

T

S

P

P

F

C

F

F

L

V

Y

W

L

L

L

V

I

R

K

R

Q

R

R60 (= R71) 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 (= R74) 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 (= R312) 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.

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)
35% identity, 80% coverage: 71:343/343 of query aligns to 390:660/660 of P06972

query
sites
P06972

R
|
R

M

W

P

P

R

R

I

I

A

M

L

A

A

A

T

L

L

F

V

A

G

G

A

V

A

M

L

L

A

A

V

V

S

A

G

G

L

C

I

I

L

I

Q

Q

S

R

I

L

V

T

R

G

N

N

P

P

L

M

A

A

S

S

P

P

D

E

L

V

L

L

G

G

I

I

T

S

S

S

G

G

A

A

S

A

A

F

A

G

A

V

V

V

L

L

Y

M

L

L

S

F

F

L

C

V

A

P

A

G

A

N

L

A

G

F

P

G

Q

W

F

L

L

L

P

P

L

-

A

A

A

G

M

S

L

L

G

G

A

A

L

V

A

T

A

L

L

L

A

I

I

I

Y

M

L

I

L

A

A

A

W

G

K

R

Q

G

G

G

A

F

S

S

P

P

L

H

R

R

L

M

V

L

L

L

I

A

G

G

V
x
M

G

A

V

L

S

S

A

-

M

-

L

-

A

T

A

A

A

F

T

T

T
x
M

F

L

V

L

L
x
M

V

M

F

L

S

Q

P

A

L

S

T

G

T

D

T

P

L

R

S

M

A

A

Y
x
Q

V

V

-

L

-
x
T

W

W

L

I

T

S

G

G

S
|
S

V

T

Y
|
Y

G

N

A

A

S

T

-

D

-

A

-

Q

-

V

W

W

P

R

E

T

P

G

R

I

A

V

L

M

A

V

G

I

W

-

L

L

A

A

I

I

L

T

P

P

L

-

L

L

L

C

A

R

R

R

H

W

V

L

R

T

V

I

Q

L

Q

P

L

L

D

G

G

D

L

T

A

A

Q

R

G

A

I

V

G

G

V

M

R

A

V

L

Q

T

W

P

L

T

R

R

A

I

G

A

L

L

V

L

S

A

V

A

A

C

L

L

A

T

G

A

A

T

A

A

I

T

A

M

W

T

G

I

G

G

A

P

M

L

A

S

F

F

V

V

G

G

L

L

I

M

A

A

P

P

H

H

I

I

A

A

K

R

R

M

L

M

V

G

A

F

P

R

G

R

F

T

A

M

G

P

Q

H

A

I

A

V

M

I

A

S

A

A

L

L

A

V

G

G

A

G

N

L

L

L

V

L

M

V

L

F

A

A

D

D

L

W

A

C

G

G

R

R

T

M

L

V

F

L

L

F

P

P

L

F

D
x
Q

L

I

P

P

A

A

G

G

I

L

F

L

V

S

A

T

V

F

L

I

G

G

T

A

P

P

F

Y

F

F

L

I

Y

Y

L

L

I

R

K

K

Q

Q

R

S

H

R

R390 (= R71) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ V166) 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 (≠ T177) 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 (≠ L180) 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 (≠ Y192) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (vs. gap) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (= S198) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (= Y200) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ D319) 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.

5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
37% identity, 80% coverage: 69:342/343 of query aligns to 56:328/330 of 5b57A

query
sites
5b57A

Q
x
D

L

I

R

R

M

A

P

P

R

R

I

V

A

V

L

L

A

A

T

L

L
|
L

V

V

G

G

A

G

L

F

A

G

V

A

S

T

G

G

L

A

I

A

L

M

Q

Q

S

A

I

L

V

F

R

R

N

N

P

P

L

L

A

A

S

D

P

P

D

G

L

L

L

V

G

G

I

V

T

S

S

S

G

G

A

A

S

A

A

L

A

G

A

A

V

T

L

T

Y

L

L

I

S

-

F

-

C

-

A

-

A

V

L

L

G

G

P

P

Q

A

F

S

L

A

P

A

L

A

A

L

A

P

M

V

L

A

-

A

-

F

-

A

-

G

G

G

A

L

A

A

L

V

A

A

L

L

A

V

I

Y

Y

R

L

L

L

A

A

A

W

S

K

R

Q

G

G

R

A

L

S

A

P

L

L

P

R

L

L

L

V

L

L

L

I

A

G

G

V

I

G

A

V

I

S

N

A

A

M

L

L

V

A

G

A

A

T

I

T

G

F

L

V

L

L

T

V

F

F

V

S

A

P

D

L

D

T

A

T

Q

T

L

L

R

S

S

A

L

Y

T

V

F

W

W

L

S

T

L

G

G

S

S

V

L

Y

G

G

G

A

A

S

Q

W
|
W

P

P

E

T

P

L

R
x
A

A

A

L

V

A
|
A

G

P

W

-

L

C

L

V

A

A

I

L

L

G

P

G

L

V

L

L

L

V

L

R

A

E

R

R

H

D

-

A

V

L

R

N

V

A

Q

L

Q

Q

L

L

D

G

D

E

G

T

L

E

A

A

Q

L

G

H

I

L

G

G

V

V

R

P

V

V

Q

Q

W

R

L

L

R

K

A

R

G

-

L

R

L

V

L

L

V

V

S

A

V

V

A

A

L

L

A

A

-

V

G

G

A

A

A

L

I

V

A

S

W

C

G

A

G

G

A

I

M

I

A

G

F

F

V

I

G

G

L

L

I

V

A

A

P

P

H

H

I

C

A

V

K

R

R

L

L

A

V

C

A

G

P

P

G

D

F

Q

A

R

G

I

Q

V

A

L

A

P

M

G

A

A

L

L

A

L

G

G

A

A

N

L

L

L

V

T

M

L

L

A

A

A

D

D

L

L

A

A

G

A

R

R

T

T

L

V

F

A

L

A

P

P

L

A

D

D

L

I

P

P

A

L

G

G

I

V

F

L

V

T

A

A

V

L

L

L

G

G

T

A

P

P

F

F

L

L

Y

A

L

L

I

W

K

K

Q

N

R

R

binding decyl-beta-d-maltopyranoside: D56 (≠ Q69), L67 (= L80), W190 (= W204), A194 (≠ R208), A197 (= A211)

Query Sequence

>WP_090442102.1 NCBI__GCF_900100495.1:WP_090442102.1
MDRLLTLRAVGFSRQLDLAALLRLGLALAITLLLMLASLSLGKVNLSPLAVLRILFAGGD
ASLVFIVEQLRMPRIALATLVGAALAVSGLILQSIVRNPLASPDLLGITSGASAAAVLYL
SFCAAALGPQFLPLAAMLGAALAALAIYLLAWKQGASPLRLVLIGVGVSAMLAAATTFVL
VFSPLTTTLSAYVWLTGSVYGASWPEPRALAGWLLAILPLLLLLARHVRVQQLDDGLAQG
IGVRVQWLRAGLLLVSVALAGAAIAWGGAMAFVGLIAPHIAKRLVAPGFAGQAAMAALAG
ANLVMLADLAGRTLFLPLDLPAGIFVAVLGTPFFLYLLIKQRH

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