SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_007154649.1 NCBI__GCF_000170835.1:WP_007154649.1 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)
41% identity, 81% coverage: 64:344/348 of query aligns to 42:318/318 of P15029

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P15029

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R51 (= R73) 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 (= R76) 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 (= R314) 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.

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, 96% coverage: 11:345/348 of query aligns to 337:660/660 of P06972

query
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P06972

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R390 (= R73) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ V168) 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 (≠ T179) 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 (≠ L182) 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 (≠ N192) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ I195) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (= S200) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (= Y202) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ D321) 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.

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, 79% coverage: 68:342/348 of query aligns to 55:330/332 of P15030

query
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P15030

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R60 (= R73) 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 (= R76) 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 (= R314) 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)
38% identity, 92% coverage: 24:344/348 of query aligns to 8:328/330 of 5b57A

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5b57A

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A

L

L

V

I

R

K

E

L

R

R

D

H

A

L

L

D

N

A

A

Q

L

S

Q

M

L

G

G

E

E

E

T

M

E

A

A

L

L

G

H

L

L

G

G

S

V

A

P

L

V

Q

Q

G

R

H

L

R

K

L

R

F

V

L

L

V

V

L

-

A

A

V

V

A

A

L

L

A

A

-

V

G

G

S

A

A

L

V

V

A

S

Y

C

A

A

G

G

A

I

I

I

G

G

F

F

I

I

G

G

L

L

I

V

A

A

P

P

H

H

M

C

A

V

R

R

R

L

L

A

V

C

N

G

S

P

G

D

H

Q

T

R

G

I

L

V

L

L

P

P

I

G

A

A

L

L

I

L

G

G

A

A

L

L

I

L

L

T

L

L

Y

A

A

A

D

D

W

L

V

A

G

A

R

R

V

T

A

V

F

A

I

A

P

P

R

A

D

D

L

I

P

P

A

L

G

G

I

V

F

L

V

T

A

A

G

L

I

L

G

G

A

A

P

P

F

F

V

L

Y

A

L

L

Y

W

R

K

L

N

R

R

binding decyl-beta-d-maltopyranoside: D56 (≠ E71), L67 (= L82), W190 (= W206), A194 (≠ I210), A197 (= A213)

Query Sequence

>WP_007154649.1 NCBI__GCF_000170835.1:WP_007154649.1
MNRTLILRSRNDRWSVKLNARVLLVTVVLAALLAISSVLALTSGSHPTSVTDVLGTLVAP
NQSELALIILEIRLPRILMAILVGAALGSAGLILQGLVRNPLASPDVIGITSGASAAAVL
FLWLGGITGTSLLLAPVAMGGAFVVALGITALAWQRGISPARLVLVGVGLAAGLTAVTTL
LLVLSPDATAMNAYIWLTGSLYASQWHDVIALAPWLMVCWPLALIKLRHLDAQSMGEEMA
LGLGSALQGHRLLFLVLAVALAGSAVAYAGAIGFIGLIAPHMARRLVNSGHTGLLPIAAL
IGALILLYADWVGRVAFIPRDLPAGIFVAGIGAPFFVYLLYRLRRELG

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