SitesBLAST
Comparing BWI76_RS11365 BWI76_RS11365 iron ABC transporter to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
46% identity, 95% coverage: 14:254/255 of query aligns to 23:264/265 of P07821
- K50 (= K41) mutation to Q: Lack of activity.
- D172 (= D163) mutation to E: Lack of activity.
- E173 (= E164) mutation to A: Lack of activity.
5x40A Structure of a cbio dimer bound with amppcp (see paper)
36% identity, 88% coverage: 3:227/255 of query aligns to 5:229/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y12), V18 (≠ K15), A20 (≠ V17), N40 (= N37), G41 (= G38), G43 (= G40), K44 (= K41), S45 (= S42), T46 (= T43), Q88 (= Q83), H139 (≠ T137), M140 (≠ A138), L141 (= L139), S142 (= S140), G144 (= G142), Q145 (= Q143), Q166 (≠ E164), H198 (= H196)
- binding magnesium ion: S45 (= S42), Q88 (= Q83)
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
30% identity, 88% coverage: 3:227/255 of query aligns to 3:225/241 of 4u00A
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
31% identity, 86% coverage: 3:221/255 of query aligns to 4:217/369 of P19566
- L86 (≠ V87) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 86% coverage: 3:221/255 of query aligns to 4:217/371 of P68187
- A85 (≠ H86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ L111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 3:216/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 1:214/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y12), S35 (≠ N37), G36 (= G38), C37 (= C39), G38 (= G40), K39 (= K41), S40 (= S42), T41 (= T43), R126 (≠ Q134), A130 (= A138), S132 (= S140), G134 (= G142), Q135 (= Q143)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 3:216/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y12), S37 (≠ N37), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), Q81 (= Q83), R128 (≠ Q134), A132 (= A138), S134 (= S140), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H196)
- binding magnesium ion: S42 (= S42), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 3:216/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ Q134), S134 (= S140), Q137 (= Q143)
- binding beryllium trifluoride ion: S37 (≠ N37), G38 (= G38), K41 (= K41), Q81 (= Q83), S134 (= S140), G136 (= G142), H191 (= H196)
- binding magnesium ion: S42 (= S42), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 3:216/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ Q134), A132 (= A138), S134 (= S140), Q137 (= Q143)
- binding tetrafluoroaluminate ion: S37 (≠ N37), G38 (= G38), K41 (= K41), Q81 (= Q83), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H196)
- binding magnesium ion: S42 (= S42), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
32% identity, 86% coverage: 3:221/255 of query aligns to 3:216/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ Q134), A132 (= A138), S134 (= S140), Q137 (= Q143)
- binding magnesium ion: S42 (= S42), Q81 (= Q83)
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
26% identity, 85% coverage: 11:226/255 of query aligns to 10:224/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y12), V16 (= V17), S36 (≠ N37), G37 (= G38), S38 (≠ C39), G39 (= G40), K40 (= K41), S41 (= S42), T42 (= T43), E162 (= E164), H194 (= H196)
- binding magnesium ion: S41 (= S42), E162 (= E164)
7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp (see paper)
30% identity, 91% coverage: 3:233/255 of query aligns to 4:229/262 of 7chaI
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 82% coverage: 12:221/255 of query aligns to 27:231/378 of P69874
- F27 (≠ Y12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ T126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
30% identity, 89% coverage: 1:228/255 of query aligns to 5:220/353 of 1vciA
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
32% identity, 78% coverage: 28:227/255 of query aligns to 52:252/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
32% identity, 78% coverage: 28:227/255 of query aligns to 52:252/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
4hluC Structure of the ecfa-a' heterodimer bound to adp (see paper)
29% identity, 89% coverage: 3:230/255 of query aligns to 5:224/249 of 4hluC
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
36% identity, 84% coverage: 3:216/255 of query aligns to 4:216/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y12), Q14 (≠ G13), T16 (≠ K15), V18 (= V17), S38 (≠ N37), G39 (= G38), C40 (= C39), G41 (= G40), K42 (= K41), T43 (≠ S42), T44 (= T43), R133 (≠ Q134), E137 (≠ A138), S139 (= S140), G141 (= G142), Q142 (= Q143)
- binding calcium ion: T43 (≠ S42), Q86 (= Q83)
P0A9R7 Cell division ATP-binding protein FtsE from Escherichia coli (strain K12) (see paper)
30% identity, 84% coverage: 3:216/255 of query aligns to 2:215/222 of P0A9R7
- K41 (= K41) mutation to R: Does not bind ATP.
- C49 (≠ S49) mutation to A: Prevents dimer formation. Does not alter ATP-binding.
Query Sequence
>BWI76_RS11365 BWI76_RS11365 iron ABC transporter
MELQTQKLTAGYGGKHVINHLDLTLPGGKITALLGPNGCGKSTLLKCFSRLLTPLAGEIW
LGDVALTRLSVRQLARRLALLPQQHHVPEGVSVRELVGYGRSPWLPLWGRLTEHDRQLVD
SALQRTGIAALAEQPLTALSGGQRQRAFLALLLAQDTPLVLLDEPTTWLDINHQVELMTL
MRELQRMGKTVVTVLHDLNQASRYCDHLVVLEGGQVRAQGSAETVLTPEMLREIFHLEAE
IHPEPVSQRPMCVVK
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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