SitesBLAST
Comparing WP_085638891.1 NCBI__GCF_002115805.1:WP_085638891.1 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)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
51% identity, 99% coverage: 1:358/362 of query aligns to 1:361/371 of P68187
- A85 (= A86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A118) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K120) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D125) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G138) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D159) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L243) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ V266) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G277) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ N281) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G283) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G300) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E306) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ G320) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G338) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G344) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F353) mutation to 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)
51% identity, 99% coverage: 2:358/362 of query aligns to 1:360/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
51% identity, 99% coverage: 2:358/362 of query aligns to 1:360/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S39), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), Q81 (= Q83), R128 (= R130), A132 (= A134), S134 (= S136), G136 (= G138), Q137 (= Q139), E158 (= E160), H191 (= H194)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
51% identity, 99% coverage: 2:358/362 of query aligns to 1:360/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), S134 (= S136), Q137 (= Q139)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G136 (= G138), H191 (= H194)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
51% identity, 99% coverage: 2:358/362 of query aligns to 1:360/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V19), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), A132 (= A134), S134 (= S136), Q137 (= Q139)
- binding tetrafluoroaluminate ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S136), G135 (= G137), G136 (= G138), E158 (= E160), H191 (= H194)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
51% identity, 99% coverage: 2:358/362 of query aligns to 1:360/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V19), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (= R130), A132 (= A134), S134 (= S136), Q137 (= Q139)
- binding magnesium ion: S42 (= S44), Q81 (= Q83)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
49% identity, 100% coverage: 1:362/362 of query aligns to 1:362/369 of P19566
- L86 (= L87) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P161) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D166) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E306) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
51% identity, 98% coverage: 4:358/362 of query aligns to 1:358/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S39), G36 (= G40), C37 (= C41), G38 (= G42), K39 (= K43), S40 (= S44), T41 (= T45), R126 (= R130), A130 (= A134), S132 (= S136), G134 (= G138), Q135 (= Q139)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
48% identity, 94% coverage: 17:358/362 of query aligns to 8:330/344 of 2awnC
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
49% identity, 87% coverage: 1:316/362 of query aligns to 1:322/393 of P9WQI3
- H193 (= H194) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC Lpqy-sugabc in state 4 (see paper)
44% identity, 99% coverage: 2:359/362 of query aligns to 1:358/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), G39 (= G40), G41 (= G42), K42 (= K43), S43 (= S44), Q82 (= Q83), Q133 (≠ A134), G136 (= G137), G137 (= G138), Q138 (= Q139), H192 (= H194)
- binding magnesium ion: S43 (= S44), Q82 (= Q83)
8hprD Lpqy-sugabc in state 4 (see paper)
44% identity, 99% coverage: 2:359/362 of query aligns to 1:357/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), C40 (= C41), G41 (= G42), K42 (= K43), S43 (= S44), T44 (= T45), Q82 (= Q83), R129 (= R130), Q133 (≠ A134), S135 (= S136), G136 (= G137), G137 (= G138), Q159 (≠ E160), H192 (= H194)
- binding magnesium ion: S43 (= S44), Q82 (= Q83)
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 99% coverage: 2:359/362 of query aligns to 1:379/384 of 8hplC