SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_009127655.1 NCBI__GCF_000315485.1:WP_009127655.1 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)
31% identity, 92% coverage: 21:339/345 of query aligns to 18:318/318 of P15029

query
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P15029

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R51 (= R58) 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 (≠ Q61) 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)
31% identity, 84% coverage: 51:341/345 of query aligns to 57:332/332 of P15030

query
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P15030

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R60 (= R58) 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 (≠ Q61) 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.

5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
31% identity, 92% coverage: 24:339/345 of query aligns to 25:328/330 of 5b57A

query
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5b57A

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binding decyl-beta-d-maltopyranoside: D56 (≠ K56), L67 (≠ V67), W190 (≠ M203), A194 (≠ V207), A197 (≠ M210)

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)
26% identity, 82% coverage: 58:340/345 of query aligns to 390:660/660 of P06972

query
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P06972

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R

R390 (= R58) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ V162) 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 (≠ A170) 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 (≠ G173) 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 (≠ A186) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ I189) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
S515 (= S194) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
Y517 (≠ A196) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ A316) 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_009127655.1 NCBI__GCF_000315485.1:WP_009127655.1
MKRPTLLLMLVILVSIFLFFLLNLLLGSVHIPLRSVWNILWGSTDESIIWQNIIWKSRVP
QALTALVAGAGLSVSGLQMQTVFRNPLAGPSVLGISSGASLGVACVVLLSGAMGGVALSK
LGYMGEVALSIAAIIGALSVMALIVYVSQKVKGNVTLLIIGVMIGYVASAIIGVLKYFSV
EEDIRAYVIWGLGSFARVSGDQMILFVCIMAVLLPLSFLLIKTMNLLLLGDGYARNLGLN
IKRARLLVISCSGVLVAIVTAYCGPIMFVGLAVPHLCRAIFHTSDHRILMPSTLLVGASL
ALVCNLIARMPGFEGALPVNSVTALVGAPVVASVLFRKRKGELEE

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