SitesBLAST

Comparing PP_1722 PP_1722 ABC transporter, ATP-binding protein to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
55% identity, 80% coverage: 3:264/329 of query aligns to 17:278/378 of P69874

• C26 (≠ S12) mutation to A: Lower ATPase activity and transport efficiency.
• F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
• F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
• C54 (= C40) mutation to T: Loss of ATPase activity and transport.
• L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
• L76 (= L62) mutation to P: Lower ATPase activity and transport efficiency.
• V135 (= V121) mutation to M: Loss of ATPase activity and transport.
• D172 (= D158) mutation to N: Loss of ATPase activity and transport.
• C276 (≠ E262) mutation to A: Lower ATPase activity and transport efficiency.

Sites not aligning to the query:

• 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.

2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 74% coverage: 1:242/329 of query aligns to 4:253/375 of 2d62A

• binding pyrophosphate 2-: P40 (= P37), S41 (= S38), G42 (= G39), C43 (= C40), G44 (= G41), K45 (= K42), T46 (≠ S43), T47 (= T44)

1g291 Malk (see paper)
45% identity, 84% coverage: 1:276/329 of query aligns to 1:285/372 of 1g291

• binding magnesium ion: D69 (= D63), E71 (≠ H65), K72 (≠ D66), K79 (≠ Q73), D80 (≠ K74), Y228 (= Y222), D229 (≠ T223)
• binding pyrophosphate 2-: P37 (= P37), S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)

Sites not aligning to the query:

• binding magnesium ion: 292, 293, 341, 342, 359

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
39% identity, 89% coverage: 1:292/329 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 (≠ S280) mutation to 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)
39% identity, 90% coverage: 1:295/329 of query aligns to 1:323/371 of P68187

• A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (= K106) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (= V117) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (= E119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (≠ G124) 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 (≠ L228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• F241 (≠ L239) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
• G278 (vs. gap) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• S282 (vs. gap) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G284 (≠ A258) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G302 (≠ A274) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• E308 (≠ S280) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
• S322 (≠ E294) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.

Sites not aligning to the query:

• 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)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/374 of 2awnB

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), S37 (= S38), G38 (= G39), C39 (= C40), 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)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), V17 (= V18), P36 (= P37), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ Q133), S134 (= S135), G135 (= G136), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
• binding magnesium ion: S42 (= S43), Q81 (= Q82), D157 (= D158)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puxA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), L133 (= L134), S134 (= S135), Q137 (= Q138)
• binding beryllium trifluoride 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), D157 (= D158)

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puwA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), S37 (= S38), 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), N162 (≠ A163), H191 (= H192)
• binding magnesium ion: S42 (= S43), Q81 (= Q82)

2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/372 of 2awoA

• binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44)
• binding magnesium ion: S42 (= S43), D157 (= D158)

1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 88% coverage: 4:292/329 of query aligns to 1:317/367 of 1q12A

• binding adenosine-5'-triphosphate: W10 (≠ Y13), V15 (= V18), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (= R129), K129 (≠ H132), A130 (≠ Q133), L131 (= L134), S132 (= S135), G133 (= G136), G134 (= G137), Q135 (= Q138), N160 (≠ A163), H189 (= H192)

7cagC Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
45% identity, 71% coverage: 4:236/329 of query aligns to 3:233/362 of 7cagC

• binding adenosine-5'-triphosphate: A14 (≠ G15), P34 (= P37), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), Q79 (= Q82), L123 (≠ F126), R126 (= R129), Q130 (= Q133), S132 (= S135), G133 (= G136), G134 (= G137), Q135 (= Q138)
• binding magnesium ion: S40 (= S43), Q79 (= 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)
47% identity, 72% coverage: 1:236/329 of query aligns to 1:237/393 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.

1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 76% coverage: 1:250/329 of query aligns to 4:247/353 of 1vciA

• binding adenosine-5'-triphosphate: F16 (≠ Y13), F19 (≠ S16), P40 (= P37), S41 (= S38), G42 (= G39), C43 (= C40), G44 (= G41), K45 (= K42), T46 (≠ S43), T47 (= T44)

3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 72% coverage: 3:240/329 of query aligns to 1:234/348 of 3d31A

Sites not aligning to the query:

• binding tungstate(vi)ion: 286, 287, 288, 319, 320, 323, 340, 341, 342

3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
40% identity, 97% coverage: 6:325/329 of query aligns to 6:344/350 of 3fvqB