SitesBLAST
Comparing Synpcc7942_1406 Synpcc7942_1406 ATPase 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 85% coverage: 12:322/368 of query aligns to 23:341/378 of P69874
- C26 (≠ Q15) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F16) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ T272) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E284) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
42% identity, 76% coverage: 9:286/368 of query aligns to 9:297/375 of 2d62A
1g291 Malk (see paper)
46% identity, 66% coverage: 12:254/368 of query aligns to 9:257/372 of 1g291
- binding magnesium ion: D69 (≠ T74), E71 (≠ Q76), K72 (≠ R77), K79 (≠ E82), D80 (≠ T83), Y228 (≠ F227), D229 (≠ Q228)
- binding pyrophosphate 2-: P37 (= P42), S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49)
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
43% identity, 78% coverage: 4:291/368 of query aligns to 1:287/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F16), Q14 (≠ S17), T16 (≠ S19), V18 (≠ L21), S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49), Q86 (= Q91), R133 (= R134), E137 (= E138), S139 (= S140), G140 (= G141), G141 (= G142), Q142 (= Q143)
- binding calcium ion: T43 (= T48), Q86 (= Q91)
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, 63% coverage: 7:239/368 of query aligns to 4:235/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
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, 63% coverage: 27:257/368 of query aligns to 22:254/369 of P19566
- L86 (= L95) 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.
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 5:261/372 of 2awoA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 5:261/374 of 2awnB
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 7:288/368 of query aligns to 4:283/353 of 1oxvD
- binding phosphoaminophosphonic acid-adenylate ester: F13 (= F16), V18 (≠ L21), A20 (= A23), P39 (= P42), S40 (= S43), G41 (= G44), A42 (≠ C45), G43 (= G46), K44 (= K47), T45 (= T48), T46 (= T49), Q89 (= Q91), E166 (= E164)
- binding magnesium ion: T45 (= T48), Q89 (= Q91)
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 7:288/368 of query aligns to 4:283/353 of 1oxvA
- binding phosphoaminophosphonic acid-adenylate ester: F13 (= F16), V18 (≠ L21), A20 (= A23), P39 (= P42), S40 (= S43), G41 (= G44), A42 (≠ C45), G43 (= G46), K44 (= K47), T45 (= T48), T46 (= T49), E166 (= E164)
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 7:288/368 of query aligns to 4:283/353 of 1oxuA
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
37% identity, 77% coverage: 7:288/368 of query aligns to 4:283/353 of Q97UY8
- S142 (= S140) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G142) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E164) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 5:261/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F16), V17 (≠ A22), P36 (= P42), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q91), R128 (= R134), A132 (≠ E138), S134 (= S140), G135 (= G141), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91), D157 (= D163)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 5:261/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F16), V17 (≠ A22), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R134), A132 (≠ E138), L133 (= L139), S134 (= S140), Q137 (= Q143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q91), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91), D157 (= D163)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 5:261/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F16), V17 (≠ A22), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R134), A132 (≠ E138), S134 (= S140), Q137 (= Q143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q91), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), N162 (= N168), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 70% coverage: 9:265/368 of query aligns to 6:262/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E129) 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.
- R228 (= R233) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F244) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 70% coverage: 9:265/368 of query aligns to 3:259/367 of 1q12A