SitesBLAST
Comparing PP_3817 PP_3817 Polyamine ABC transporter, ATP-binding protein 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)
47% identity, 72% coverage: 14:289/382 of query aligns to 17:297/378 of P69874
- C26 (≠ H23) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y24) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F42) 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 (≠ V73) 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 (≠ V268) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E289) 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
48% identity, 66% coverage: 11:263/382 of query aligns to 3:263/375 of 2d62A
1g291 Malk (see paper)
47% identity, 65% coverage: 15:263/382 of query aligns to 4:260/372 of 1g291
- binding magnesium ion: D69 (= D74), E71 (≠ Q76), K72 (≠ S77), K79 (≠ H84), D80 (≠ K85)
- binding pyrophosphate 2-: S38 (= S49), G39 (= G50), C40 (≠ S51), G41 (= G52), K42 (= K53), T43 (≠ S54), T44 (= T55)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 90% coverage: 15:357/382 of query aligns to 7:334/353 of 1vciA
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, 75% coverage: 15:301/382 of query aligns to 4:300/393 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.
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 72% coverage: 15:289/382 of query aligns to 3:284/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y24), 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)
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 72% coverage: 15:289/382 of query aligns to 3:284/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y24), 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)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
44% identity, 64% coverage: 15:258/382 of query aligns to 4:249/369 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.
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 68% coverage: 29:289/382 of query aligns to 16:282/384 of 8hplC
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 64% coverage: 15:259/382 of query aligns to 3:249/374 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)
42% identity, 64% coverage: 15:259/382 of query aligns to 3:249/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y24), 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)
42% identity, 64% coverage: 15:259/382 of query aligns to 3:249/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), 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)
42% identity, 64% coverage: 15:259/382 of query aligns to 3:249/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), 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)
42% identity, 64% coverage: 15:259/382 of query aligns to 3:249/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), 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)
42% identity, 64% coverage: 15:259/382 of query aligns to 4:250/371 of P68187
- A85 (≠ S96) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G117) 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 (≠ A239) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F250) 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, 64% coverage: 15:259/382 of query aligns to 1:247/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y24), S35 (= S49), G36 (= G50), C37 (≠ S51), G38 (= G52), K39 (= K53), S40 (= S54), T41 (= T55), R126 (= R140), A130 (≠ Q144), S132 (= S146), G134 (= G148), Q135 (= Q149)
3d31A Modbc from methanosarcina acetivorans (see paper)
33% identity, 92% coverage: 14:366/382 of query aligns to 1:346/348 of 3d31A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 69% coverage: 25:289/382 of query aligns to 16:279/353 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)
39% identity, 69% coverage: 25:289/382 of query aligns to 16:279/353 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)
39% identity, 69% coverage: 25:289/382 of query aligns to 16:279/353 of 1oxuA
Sites not aligning to the query:
Query Sequence
>PP_3817 PP_3817 Polyamine ABC transporter, ATP-binding protein
MSAVIKDNAHGKTLVSLRGLNKHYGDFTAVDNLDLEIQDGEFLTFLGSSGSGKSTTLSML
AGFETPSSGEILVDGQSLVNVPPHKRDIGMVFQRYSLFPHLNVRDNIAFPLAIRKLGAAE
TAKRVDAMLKLVQLEQFAHRKPSQMSGGQQQRVAIARALVYEPRILLMDEPLGALDKKLR
EDLQDELRQLHRRLGITIVYVTHDQEEAMRLSQRIAIFSHGKIVGLGTGYDLYQNPPNAF
VASFLGNSNFLRIKASSNGAGSFEGQPVAIRLTPGLAASQDALIMVRPEKAVAMSAEQAM
REPLPAGWNEVTAKVGEVLFLGESQTCHVVTAGGTELTVKALSAAGMPMQPGDSVKVRWA
VADACIYTEWAESDLSKSAGAH
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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