SitesBLAST
Comparing WP_017220841.1 NCBI__GCF_000276805.1:WP_017220841.1 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)
37% identity, 95% coverage: 12:340/346 of query aligns to 7:318/318 of P15029
- 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 (= R310) 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.
5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
36% identity, 95% coverage: 16:344/346 of query aligns to 15:330/330 of 5b57A
P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
34% identity, 81% coverage: 59:338/346 of query aligns to 51:330/332 of P15030
- 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 (= R310) 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)
35% identity, 79% coverage: 68:341/346 of query aligns to 390:660/660 of P06972
- R390 (= R68) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
- M484 (≠ L164) 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 (≠ G176) 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 (≠ L179) 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 (= Q188) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
- T510 (≠ F191) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
- S515 (≠ G196) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
- Y517 (≠ D198) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
- Q636 (≠ E317) 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_017220841.1 NCBI__GCF_000276805.1:WP_017220841.1
MPFYRLTAVQTLFSVLLFCGLFLLYLSFGAIHIPISDILALFKAYFVGGSELALTEQPLA
SAVVLHIRLPRACAAILAGGSLALAGACTQGLFRNPLASPDVLGVSAGSSFGAVLAIVTG
FSFMNPMWLPIFTTVGALAAAAVIYLLASRHASTQILFLILTGLALSSLLGGARMGLLLM
AQQYEMSQFVFWAMGGLDGRTWSQLMWPAPIIVVVSALLLRECRALNLLALGEENAHGMG
LNIKKTRLKLLMFSTLLTAMSIAVAGPIGFIGLMVPHLVRLIVGPTHEKLLPFSALFGVI
FLLACDLLGRWIIAPNELKVGIITSFIGGCYFIALIIRFQRKGSFV
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