SitesBLAST

P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
37% identity, 84% coverage: 56:344/345 of query aligns to 41:318/318 of P15029

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P15029

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R51 (= R66) 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 (= R69) 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.

P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
37% identity, 85% coverage: 49:342/345 of query aligns to 49:330/332 of P15030

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R60 (= R66) 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 (= R69) 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.

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, 80% coverage: 66:342/345 of query aligns to 390:657/660 of P06972

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P06972

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R390 (= R66) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
M484 (≠ I168) 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 (≠ A177) 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 (≠ T192) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
T510 (≠ F195) 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 (≠ N202) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
Q636 (≠ E321) 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

>Pf1N1B4_2867 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2867
MTFLVKPRALFIGLSLLCLLAIWLSLALGPVSLPLFDTLRASLRLIGLPIAPDGLEQAEL
ILGQIRLPRTLLGLAVGGVLALSGVAMQGLFRNPLADPGLVGVSSGAALGAAIAIVGGSV
FGGLPESFGPYLLSLCAFLGGLGVTALVYRLGRRNGQTNVATMLLAGIALTALAGSAVGL
FTYLADDATLRTLTFWNLGSLNGASYSRLWPLLLVSTGVALWLPRRAKALNALLLGESEA
GHLGIDVEGLKRELVFCTALGVGAAVAAAGMIGFVGLVVPHLVRLLAGPDHRVLLPASVL
AGASLLLFADLVARLALAPAELPIGIVTAFIGAPFFLYLLLRGRA

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