SitesBLAST
Comparing WP_015448118.1 NCBI__GCF_000230695.2:WP_015448118.1 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)
1g291 Malk (see paper)
38% identity, 92% coverage: 14:247/255 of query aligns to 6:242/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ L75), K72 (≠ Q76), K79 (≠ L83), D80 (≠ R84)
- binding pyrophosphate 2-: S38 (= S46), G39 (= G47), C40 (≠ S48), G41 (= G49), K42 (= K50), T43 (≠ S51), T44 (= T52)
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
36% identity, 89% coverage: 19:246/255 of query aligns to 9:237/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y21), V16 (≠ A26), S36 (= S46), G37 (= G47), S38 (= S48), G39 (= G49), K40 (= K50), S41 (= S51), T42 (= T52), E162 (= E170), H194 (= H203)
- binding magnesium ion: S41 (= S51), E162 (= E170)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
37% identity, 92% coverage: 14:247/255 of query aligns to 9:245/375 of 2d62A
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
37% identity, 92% coverage: 11:245/255 of query aligns to 19:263/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
37% identity, 92% coverage: 11:245/255 of query aligns to 19:263/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 10:237/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y21), S37 (= S46), G38 (= G47), C39 (≠ S48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), Q81 (= Q92), R128 (= R140), A132 (≠ E144), S134 (= S146), G136 (= G148), Q137 (= Q149), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S51), Q81 (= Q92)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 10:237/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), G38 (= G47), C39 (≠ S48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (= R140), S134 (= S146), Q137 (= Q149)
- binding beryllium trifluoride ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q92), S134 (= S146), G136 (= G148), H191 (= H203)
- binding magnesium ion: S42 (= S51), Q81 (= Q92)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 10:237/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (≠ A26), G38 (= G47), C39 (≠ S48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (= R140), A132 (≠ E144), S134 (= S146), Q137 (= Q149)
- binding tetrafluoroaluminate ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q92), S134 (= S146), G135 (= G147), G136 (= G148), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S51), Q81 (= Q92)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 10:237/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (≠ A26), G38 (= G47), C39 (≠ S48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (= R140), A132 (≠ E144), S134 (= S146), Q137 (= Q149)
- binding magnesium ion: S42 (= S51), Q81 (= Q92)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 10:237/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 8:235/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y21), S35 (= S46), G36 (= G47), C37 (≠ S48), G38 (= G49), K39 (= K50), S40 (= S51), T41 (= T52), R126 (= R140), A130 (≠ E144), S132 (= S146), G134 (= G148), Q135 (= Q149)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 91% coverage: 19:249/255 of query aligns to 11:238/371 of P68187
- A85 (≠ G95) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L127) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A129) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T135) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G148) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D169) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A239) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 91% coverage: 19:249/255 of query aligns to 11:238/369 of P19566
- L86 (= L96) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P171) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D176) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 85% coverage: 20:237/255 of query aligns to 14:233/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 85% coverage: 20:237/255 of query aligns to 14:233/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 85% coverage: 20:237/255 of query aligns to 14:233/353 of 1oxuA
Sites not aligning to the query:
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)
38% identity, 85% coverage: 20:237/255 of query aligns to 14:233/353 of Q97UY8
- S142 (= S146) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G148) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E170) 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+).
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 89% coverage: 19:245/255 of query aligns to 25:248/378 of P69874
- C26 (≠ R20) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y21) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ T39) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S48) mutation to T: Loss of ATPase activity and transport.
- L60 (= L54) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ T131) mutation to M: Loss of ATPase activity and transport.
- D172 (= D169) 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.
7ahdC Opua (e190q) occluded (see paper)
36% identity, 91% coverage: 11:241/255 of query aligns to 19:259/260 of 7ahdC