SitesBLAST
Comparing H281DRAFT_05492 FitnessBrowser__Burk376:H281DRAFT_05492 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)
44% identity, 87% coverage: 6:327/372 of query aligns to 17:336/378 of P69874
- C26 (≠ S15) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y16) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F35) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S44) mutation to T: Loss of ATPase activity and transport.
- L60 (= L50) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ M66) 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.
- C276 (≠ L266) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E288) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
53% identity, 60% coverage: 18:239/372 of query aligns to 14:241/372 of 1g291
- binding magnesium ion: D69 (≠ T73), E71 (vs. gap), K72 (vs. gap), K79 (≠ H77), D80 (≠ K78)
- binding pyrophosphate 2-: S38 (= S42), G39 (= G43), C40 (≠ S44), G41 (= G45), K42 (= K46), T43 (= T47), T44 (= T48)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
48% identity, 67% coverage: 7:254/372 of query aligns to 7:261/375 of 2d62A
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, 81% coverage: 12:313/372 of query aligns to 9:304/393 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.
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 68% coverage: 12:263/372 of query aligns to 8:256/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y16), S38 (= S42), G39 (= G43), G41 (= G45), K42 (= K46), S43 (≠ T47), Q82 (= Q86), Q133 (≠ E137), G136 (= G140), G137 (= G141), Q138 (= Q142), H192 (= H196)
- binding magnesium ion: S43 (≠ T47), Q82 (= Q86)
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 68% coverage: 12:263/372 of query aligns to 8:256/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y16), S38 (= S42), C40 (≠ S44), G41 (= G45), K42 (= K46), S43 (≠ T47), T44 (= T48), Q82 (= Q86), R129 (= R133), Q133 (≠ E137), S135 (= S139), G136 (= G140), G137 (= G141), Q159 (≠ E163), H192 (= H196)
- binding magnesium ion: S43 (≠ T47), Q82 (= Q86)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 94% coverage: 18:368/372 of query aligns to 17:352/353 of 1vciA
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
49% identity, 65% coverage: 12:252/372 of query aligns to 8:248/384 of 8hplC
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
44% identity, 65% coverage: 18:260/372 of query aligns to 13:255/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S42), G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), Q81 (= Q86), R128 (= R133), A132 (≠ E137), S134 (= S139), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q86)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
44% identity, 65% coverage: 18:260/372 of query aligns to 13:255/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R133), S134 (= S139), Q137 (= Q142)
- binding beryllium trifluoride ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q86), S134 (= S139), G136 (= G141), H191 (= H196)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q86)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
44% identity, 65% coverage: 18:260/372 of query aligns to 13:255/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V22), G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R133), A132 (≠ E137), S134 (= S139), Q137 (= Q142)
- binding tetrafluoroaluminate ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q86), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q86)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
44% identity, 65% coverage: 18:260/372 of query aligns to 13:255/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V22), G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R133), A132 (≠ E137), S134 (= S139), Q137 (= Q142)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q86)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
44% identity, 65% coverage: 18:260/372 of query aligns to 13:255/374 of 2awnB
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
44% identity, 65% coverage: 18:260/372 of query aligns to 14:256/371 of P68187
- A85 (= A89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ H128) 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 (≠ L232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ T245) 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)
44% identity, 65% coverage: 18:260/372 of query aligns to 11:253/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S42), G36 (= G43), C37 (≠ S44), G38 (= G45), K39 (= K46), S40 (≠ T47), T41 (= T48), R126 (= R133), A130 (≠ E137), S132 (= S139), G134 (= G141), Q135 (= Q142)
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)
45% identity, 60% coverage: 18:239/372 of query aligns to 14:235/369 of P19566
- L86 (= L90) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 82% coverage: 18:322/372 of query aligns to 16:315/353 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)
37% identity, 82% coverage: 18:322/372 of query aligns to 16:315/353 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)
37% identity, 82% coverage: 18:322/372 of query aligns to 16:315/353 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)
37% identity, 82% coverage: 18:322/372 of query aligns to 16:315/353 of Q97UY8
- S142 (= S139) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G141) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E163) 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
>H281DRAFT_05492 FitnessBrowser__Burk376:H281DRAFT_05492
VESKSIIDFVGVQKSYDGENLVVKDLNLSIRRGEFLTLLGASGSGKTTTLMMLAGFETPT
LGGIWMNGKPIETVPAHKRGIGMVFQNYALFPHMTVEQNLAYPLRMRNVSRNETVAKVKR
AVDMVRLHGMERRRPSELSGGQQQRVALARAMVFEPELILMDEPLGALDKNLREHMQYEI
KQLHHELGVTVVYVTHDQAEAMTMSDRIAVFQQGVISQIGSPDELYERPANLDVASFIGE
SNRLTGTVVSVGSMVDTVRLTSGLSLEVPSTSPVREIDRVVEIVVRPERVSIEQGSADDQ
WQWLQGRVSDLTYLGDHLRVLLVTDSGDSFIAKVSGAYRALPSVGQELRFGWRTQDAHAF
QRSMHQPLSSLK
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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