SitesBLAST
Comparing GFF960 HP15_939 spermidine/putrescine ABC transporter ATPase subunit 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)
45% identity, 88% coverage: 14:341/372 of query aligns to 17:342/378 of P69874
- C26 (≠ S23) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F24) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I42) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S51) mutation to T: Loss of ATPase activity and transport.
- L60 (= L57) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L73) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V132) mutation to M: Loss of ATPase activity and transport.
- D172 (= D169) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ A272) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E296) 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
46% identity, 64% coverage: 20:258/372 of query aligns to 12:258/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 3:321/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 3:321/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F24), S37 (= S49), G38 (= G50), C39 (≠ S51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), Q81 (= Q93), R128 (= R140), A132 (≠ Q144), S134 (= S146), G136 (= G148), Q137 (= Q149), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S54), Q81 (= Q93)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 3:321/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F24), G38 (= G50), C39 (≠ S51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (= R140), S134 (= S146), Q137 (= Q149)
- binding beryllium trifluoride ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q93), S134 (= S146), G136 (= G148), H191 (= H203)
- binding magnesium ion: S42 (= S54), Q81 (= Q93)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 3:321/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ A29), G38 (= G50), C39 (≠ S51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (= R140), A132 (≠ Q144), S134 (= S146), Q137 (= Q149)
- binding tetrafluoroaluminate ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q93), S134 (= S146), G135 (= G147), G136 (= G148), E158 (= E170), H191 (= H203)
- binding magnesium ion: S42 (= S54), Q81 (= Q93)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 3:321/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ A29), G38 (= G50), C39 (≠ S51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (= R140), A132 (≠ Q144), S134 (= S146), Q137 (= Q149)
- binding magnesium ion: S42 (= S54), Q81 (= Q93)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 86% coverage: 15:334/372 of query aligns to 4:322/371 of P68187
- A85 (= A96) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V125) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M128) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K130) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E135) 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 (= R239) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ I250) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ T281) 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 (≠ A292) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G314) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A320) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S334) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 86% coverage: 15:334/372 of query aligns to 1:319/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F24), S35 (= S49), G36 (= G50), C37 (≠ S51), G38 (= G52), K39 (= K53), S40 (= S54), T41 (= T55), R126 (= R140), A130 (≠ Q144), S132 (= S146), G134 (= G148), Q135 (= Q149)
1g291 Malk (see paper)
45% identity, 64% coverage: 22:258/372 of query aligns to 11:255/372 of 1g291
- binding magnesium ion: D69 (= D74), E71 (≠ Q76), K72 (≠ D77), K79 (≠ F84), D80 (≠ L85)
- binding pyrophosphate 2-: S38 (= S49), G39 (= G50), C40 (≠ S51), G41 (= G52), K42 (= K53), T43 (≠ S54), T44 (= T55)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
42% identity, 63% coverage: 15:247/372 of query aligns to 4:236/369 of P19566
- L86 (= L97) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
47% identity, 65% coverage: 13:255/372 of query aligns to 5:241/353 of 1vciA
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 77% coverage: 11:298/372 of query aligns to 1:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F24), S38 (= S49), C40 (≠ S51), G41 (= G52), K42 (= K53), S43 (= S54), T44 (= T55), Q82 (= Q93), R129 (= R140), Q133 (= Q144), S135 (= S146), G136 (= G147), G137 (= G148), Q159 (≠ E170), H192 (= H203)
- binding magnesium ion: S43 (= S54), Q82 (= Q93)
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 77% coverage: 11:298/372 of query aligns to 1:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F24), S38 (= S49), G39 (= G50), G41 (= G52), K42 (= K53), S43 (= S54), Q82 (= Q93), Q133 (= Q144), G136 (= G147), G137 (= G148), Q138 (= Q149), H192 (= H203)
- binding magnesium ion: S43 (= S54), Q82 (= Q93)
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 77% coverage: 11:298/372 of query aligns to 1:284/384 of 8hplC
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)
44% identity, 66% coverage: 11:255/372 of query aligns to 2:247/393 of P9WQI3
- H193 (= H203) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 84% coverage: 13:323/372 of query aligns to 2:308/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 84% coverage: 13:323/372 of query aligns to 2:308/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 84% coverage: 13:323/372 of query aligns to 2:308/353 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)
36% identity, 84% coverage: 13:323/372 of query aligns to 2:308/353 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+).
Query Sequence
>GFF960 HP15_939 spermidine/putrescine ABC transporter ATPase subunit
MENGNNTSAQAEVLLSIRGISKSFDGTLAVDNVNLDIHKGEIFALLGGSGSGKSTLLRML
AGFETPNAGSIMLDGQDVTALPPFLRPTNMMFQSYALFPHMTVEQNIAMGLKQDKLPKSE
IRDRVAAMLKLVKMEPYARRKPQQLSGGQQQRVALARSLAKRPKLLLLDEPMGALDKKLR
TEMQLELVEILENVGATCLMVTHDQEEAMTMASRIAIMAQGRIAQIGSPIDIYESPNSRM
TAEFIGSVNIFEAHIREDEADSVTLTSDLLDAPVFIDRGVTTPAESTATLVALRPEKIYL
TPDKPDGENNWSCGTVDNIAYLGDITSYYVKLASGKRVQATMANVERRGERPTWGDRVFV
SWEASSPILLWN
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory