SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_097141823.1 NCBI__GCF_900220975.1:WP_097141823.1 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)
39% identity, 89% coverage: 34:339/343 of query aligns to 18:318/318 of P15029

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P15029

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R51 (= R68) 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 (= R71) 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 (= R309) 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)
38% identity, 93% coverage: 19:338/343 of query aligns to 9:331/332 of P15030

query
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P15030

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R60 (= R68) 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 (= R71) 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 (= R309) 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)
32% identity, 79% coverage: 68:338/343 of query aligns to 390:658/660 of P06972

query
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P06972

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R390 (= R68) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ A164) 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 (≠ S172) 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 (≠ I175) 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 (≠ G187) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ A190) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (≠ G195) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (≠ G197) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ E316) 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)
36% identity, 93% coverage: 22:339/343 of query aligns to 10:328/330 of 5b57A

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A

L

L

A

Q

L

L

G

G

D

E

D

T

L

E

A

A

A

L

G

H

L

L

G

G

E

V

R

P

V

V

A

Q

L

R

A

L

R

K

A

R

F

R

A

V

A

L

F

V

G

A

A

V

I

A

L

L

L

A

C

V

G

G

A

A

T

L

T

V

A

S

V

C

C

A

G

G

P

I

I

I

G

G

F

F

L

I

G

G

L

L

V

V

V

A

P

P

H

H

L

C

C

V

R

R

L

L

L

A

V

C

G

G

V

P

D

D

H

Q

R

R

W

I

L

V

L

L

P

P

F

G

S

A

A

A

V

L

A

L

G

G

A

A

C

L

L

L

L

T

L

L

G

A

A

A

D

D

I

L

V

A

G

A

R

R

I

T

I

V

A

A

R

A

P

P

A

A

E

D

L

I

D

P

V

L

G

G

I

V

V

L

T

T

A

A

F

L

V

L

G

G

A

A

P

P

F

F

I

L

W

A

V

L

R

W

R

K

Q

N

R

R

binding decyl-beta-d-maltopyranoside: D56 (vs. gap), L67 (= L77), W190 (≠ F201), A194 (≠ S205), A197 (≠ L208)

Query Sequence

>WP_097141823.1 NCBI__GCF_900220975.1:WP_097141823.1
MISESIGGAVAPRAGGNRMLWLAVVAAVLVLLCILSVAIGTREVAWADIVAAIGGREDTI
AQAAVAMRIPRTLLALLAGAALGLAGAIMQGVTRNPLADPGILGVNMGASLAVVVGVAWF
NIASADAYIFAAVLGAGASAVFVYAIGSLGRGGATPLKLALAGAATSVAFSSLVIALVLP
RNDIAGGIRAWQIGGVGGATFERMSHVLPFLVAGFIISLLSARKLNSLALGDDLAAGLGE
RVALARAFAAFGAILLCGATTAVCGPIGFLGLVVPHLCRLLVGVDHRWLLPFSAVAGACL
LLGADIVGRIIARPAELDVGIVTAFVGAPFFIWVVRRQRVREL

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