SitesBLAST

Comparing PP_5137 PP_5137 ferric iron 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

1g291 Malk (see paper)
43% identity, 87% coverage: 8:314/352 of query aligns to 2:316/372 of 1g291

• binding magnesium ion: D69 (= D75), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q79), D80 (≠ A80), Y228 (= Y226), D229 (= D227), E292 (= E291), D293 (≠ N292)
• binding pyrophosphate 2-: P37 (= P43), S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50)

Sites not aligning to the query:

• binding magnesium ion: 341, 342, 359

2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 85% coverage: 8:305/352 of query aligns to 5:324/375 of 2d62A

• binding pyrophosphate 2-: P40 (= P43), S41 (= S44), G42 (= G45), C43 (= C46), G44 (= G47), K45 (= K48), T46 (= T49), T47 (= T50)

1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 66% coverage: 8:239/352 of query aligns to 5:230/353 of 1vciA

• binding adenosine-5'-triphosphate: F16 (= F19), F19 (= F22), P40 (= P43), S41 (= S44), G42 (= G45), C43 (= C46), G44 (= G47), K45 (= K48), T46 (= T49), T47 (= T50)

2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 1:249/374 of 2awnB

• binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ A24), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50)

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 70% coverage: 8:252/352 of query aligns to 2:250/371 of P68187

• A85 (= A91) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (≠ G110) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (= V118) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (≠ M121) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (= E123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (≠ S128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
• D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
• R228 (≠ P232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• F241 (≠ W243) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.

Sites not aligning to the query:

• 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.

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 1:249/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F19), V17 (≠ A24), P36 (= P43), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), Q81 (= Q88), R128 (≠ K133), A132 (≠ Q137), S134 (= S139), G135 (= G140), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
• binding magnesium ion: S42 (≠ T49), Q81 (= Q88), D157 (= D162)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 1:249/371 of 3puxA

• binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ A24), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (≠ K133), A132 (≠ Q137), L133 (= L138), S134 (= S139), Q137 (= Q142)
• binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
• binding magnesium ion: S42 (≠ T49), Q81 (= Q88), D157 (= D162)

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 1:249/371 of 3puwA

• binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ A24), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (≠ K133), A132 (≠ Q137), S134 (= S139), Q137 (= Q142)
• binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), N162 (≠ A167), H191 (= H196)
• binding magnesium ion: S42 (≠ T49), Q81 (= Q88)

2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 1:249/372 of 2awoA

• binding adenosine-5'-diphosphate: W12 (≠ F19), V17 (≠ A24), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50)
• binding magnesium ion: S42 (≠ T49), D157 (= D162)

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
45% identity, 70% coverage: 8:252/352 of query aligns to 2:250/369 of P19566

• L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• P160 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• D165 (= D169) 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.

1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
45% identity, 69% coverage: 10:252/352 of query aligns to 1:247/367 of 1q12A

• binding adenosine-5'-triphosphate: W10 (≠ F19), V15 (≠ A24), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (≠ T49), T41 (= T50), R126 (≠ K133), K129 (≠ G136), A130 (≠ Q137), L131 (= L138), S132 (= S139), G133 (= G140), G134 (= G141), Q135 (= Q142), N160 (≠ A167), H189 (= H196)

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
49% identity, 66% coverage: 10:242/352 of query aligns to 18:252/378 of P69874

• C26 (≠ R18) mutation to A: Lower ATPase activity and transport efficiency.
• F27 (= F19) mutation to L: Lower ATPase activity and transport efficiency.
• F45 (≠ L37) mutation to L: Lower ATPase activity and transport efficiency.
• C54 (= C46) mutation to T: Loss of ATPase activity and transport.
• L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
• L76 (≠ I68) mutation to P: Lower ATPase activity and transport efficiency.
• V135 (= V125) mutation to M: Loss of ATPase activity and transport.
• D172 (= D162) mutation to N: Loss of ATPase activity and transport.

Sites not aligning to the query:

• 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.

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)
45% identity, 68% coverage: 8:245/352 of query aligns to 2:244/393 of P9WQI3

• H193 (= H196) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.

7cagC Mycobacterium smegmatis lpqy-sugabc complex in the catalytic intermediate state (see paper)
38% identity, 98% coverage: 8:351/352 of query aligns to 1:351/362 of 7cagC

• binding adenosine-5'-triphosphate: A14 (= A21), P34 (= P43), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (≠ T49), T41 (= T50), Q79 (= Q88), L123 (≠ S130), R126 (≠ K133), Q130 (= Q137), S132 (= S139), G133 (= G140), G134 (= G141), Q135 (= Q142)
• binding magnesium ion: S40 (≠ T49), Q79 (= Q88)

1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 87% coverage: 8:312/352 of query aligns to 2:315/353 of 1oxvD

• binding phosphoaminophosphonic acid-adenylate ester: F13 (= F19), V18 (≠ F22), A20 (= A24), P39 (= P43), S40 (= S44), G41 (= G45), A42 (≠ C46), G43 (= G47), K44 (= K48), T45 (= T49), T46 (= T50), Q89 (= Q88), E166 (= E163)
• binding magnesium ion: T45 (= T49), Q89 (= Q88)

1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 87% coverage: 8:312/352 of query aligns to 2:315/353 of 1oxvA

• binding phosphoaminophosphonic acid-adenylate ester: F13 (= F19), V18 (≠</