SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_089751459.1 NCBI__GCF_900113125.1:WP_089751459.1 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)
34% identity, 92% coverage: 19:329/338 of query aligns to 5:313/318 of P15029

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P15029

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R51 (= R63) 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 (= R66) 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 (= R304) 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, 82% coverage: 56:332/338 of query aligns to 53:330/332 of P15030

query
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P15030

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R60 (= R63) 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 (= R66) 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 (= R304) 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)
33% identity, 96% coverage: 7:329/338 of query aligns to 2:323/330 of 5b57A

query
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5b57A

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binding decyl-beta-d-maltopyranoside: D56 (≠ T61), L67 (≠ T72), W190 (≠ L196), A194 (≠ L200), A197 (≠ L203)

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)
30% identity, 81% coverage: 63:335/338 of query aligns to 390:660/660 of P06972

query
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P06972

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R390 (= R63) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ A159) 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 (≠ S167) 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 (≠ Q170) 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 (≠ S182) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ F185) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (= S190) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (vs. gap) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ E311) 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_089751459.1 NCBI__GCF_900113125.1:WP_089751459.1
MSKFIINRHFKWTILLGIIVIFLTAGFLSIAIGKTSIPLSTVWDAFIHYDPSSTNQVIIR
TSRITRTLIAMTVGASLSIAGALMQALTRNPLASPDIFGVNAGALFFIVAAATFFSVESL
SGYMWIGFVGAGVAGTIVYLLGSMGEDGLSPIRIVLAGAAISALFISFTQGMLVLDEQRM
QSVLFWLSGSVAGRELDILLPVLPFLLGAIVLSFFIGKPLNILMSGDDVAKNLGQNTGLL
KLVIGITIVFLAGGSVAVAGSIGFIGLVVPHIVKGITGPNYQWIIPISGLCGATLLLGAD
IAARLIIAPQEMPIGVMTALFGTPFFIYIARKGVKKSG

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