SitesBLAST

Comparing WP_037454711.1 NCBI__GCF_000576635.1:WP_037454711.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

2d62A Crystal structure of multiple sugar binding transport atp-binding protein
50% identity, 98% coverage: 1:354/362 of query aligns to 4:366/375 of 2d62A

• binding pyrophosphate 2-: G42 (= G39), C43 (= C40), G44 (= G41), K45 (= K42), T46 (≠ S43), T47 (= T44)

1g291 Malk (see paper)
48% identity, 99% coverage: 1:360/362 of query aligns to 1:369/372 of 1g291

• binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (= K73), D80 (≠ E74), E292 (≠ G284), D293 (≠ H285), K359 (≠ N350)
• binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)

8hprD Lpqy-sugabc in state 4 (see paper)
50% identity, 100% coverage: 2:362/362 of query aligns to 1:359/362 of 8hprD

• binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (= Q133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
• binding magnesium ion: S43 (= S43), Q82 (= Q82)

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
52% identity, 89% coverage: 1:321/362 of query aligns to 1:318/369 of P19566

• L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• D165 (= D165) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• E306 (= E309) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.

8hprC Lpqy-sugabc in state 4 (see paper)
49% identity, 100% coverage: 2:362/362 of query aligns to 1:360/363 of 8hprC

• binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (= S43), Q82 (= Q82), Q133 (= Q133), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
• binding magnesium ion: S43 (= S43), Q82 (= Q82)

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
52% identity, 89% coverage: 1:321/362 of query aligns to 1:320/371 of P68187

• A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (≠ D106) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (≠ D119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (≠ V124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
• D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
• R228 (≠ T228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• F241 (= F241) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• W267 (≠ R262) mutation to G: Normal maltose transport but constitutive mal gene expression.
• G278 (= G274) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• S282 (≠ T278) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G284 (= G280) 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 (= E309) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.

Sites not aligning to the query:

• 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.

8hplC Lpqy-sugabc in state 1 (see paper)
58% identity, 79% coverage: 2:286/362 of query aligns to 1:284/384 of 8hplC

• binding adenosine-5'-triphosphate: Y12 (= Y13), G37 (= G39), C38 (= C40), G39 (= G41), K40 (= K42), S41 (= S43), T42 (= T44)

2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
51% identity, 88% coverage: 2:321/362 of query aligns to 1:319/374 of 2awnB

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), S37 (= S38), G38 (= G39), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44)

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, 88% coverage: 2:321/362 of query aligns to 1:319/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ Q133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
• binding magnesium ion: S42 (= S43), Q81 (= Q82)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
51% identity, 88% coverage: 2:321/362 of query aligns to 1:319/371 of 3puxA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (= Q138)
• binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
• binding magnesium ion: S42 (= S43), Q81 (= Q82)

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
51% identity, 88% coverage: 2:321/362 of query aligns to 1:319/371 of 3puwA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), S134 (= S135), Q137 (= Q138)
• binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
• binding magnesium ion: S42 (= S43), Q81 (= Q82)

3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
51% identity, 88% coverage: 2:321/362 of query aligns to 1:319/371 of 3puvA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), S134 (= S135), Q137 (= Q138)
• binding magnesium ion: S42 (= S43), Q81 (= Q82)

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)
52% identity, 88% coverage: 1:318/362 of query aligns to 1:321/393 of P9WQI3

• H193 (= H192) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.

1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
51% identity, 88% coverage: 4:321/362 of query aligns to 1:317/367 of 1q12A