SitesBLAST
Comparing PP_1722 PP_1722 ABC transporter, ATP-binding protein to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
55% identity, 80% coverage: 3:264/329 of query aligns to 17:278/378 of P69874
- C26 (≠ S12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ E262) mutation to A: Lower ATPase activity and transport efficiency.
Sites not aligning to the query:
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 74% coverage: 1:242/329 of query aligns to 4:253/375 of 2d62A
1g291 Malk (see paper)
45% identity, 84% coverage: 1:276/329 of query aligns to 1:285/372 of 1g291
- binding magnesium ion: D69 (= D63), E71 (≠ H65), K72 (≠ D66), K79 (≠ Q73), D80 (≠ K74)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)
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)
39% identity, 89% coverage: 1:292/329 of query aligns to 1:318/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ S280) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 90% coverage: 1:295/329 of query aligns to 1:323/371 of P68187
- A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L239) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) 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 (≠ A258) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A274) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ S280) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ E294) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/374 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)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ Q133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 89% coverage: 4:295/329 of query aligns to 3:322/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ Q133), S134 (= S135), Q137 (= Q138)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 88% coverage: 4:292/329 of query aligns to 1:317/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (= R129), A130 (≠ Q133), S132 (= S135), G134 (= G137), Q135 (= Q138)
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 71% coverage: 4:236/329 of query aligns to 3:234/384 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)
47% identity, 72% coverage: 1:236/329 of query aligns to 1:237/393 of P9WQI3
- H193 (= H192) 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)
45% identity, 71% coverage: 4:236/329 of query aligns to 3:236/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (= S43), Q82 (= Q82), Q133 (= Q133), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
8hprD Lpqy-sugabc in state 4 (see paper)
45% identity, 71% coverage: 4:236/329 of query aligns to 3:236/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (= Q133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 76% coverage: 1:250/329 of query aligns to 4:247/353 of 1vciA
3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 72% coverage: 3:240/329 of query aligns to 1:234/348 of 3d31A
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
40% identity, 97% coverage: 6:325/329 of query aligns to 6:344/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y13), Q14 (≠ A14), T16 (≠ S16), V18 (= V18), S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44), R133 (= R129), E137 (≠ Q133), S139 (= S135), G141 (= G137), Q142 (= Q138)
- binding calcium ion: T43 (≠ S43), Q86 (= Q82)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 1:268/329 of query aligns to 1:285/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 1:268/329 of query aligns to 1:285/353 of 1oxvA
Query Sequence
>PP_1722 PP_1722 ABC transporter, ATP-binding protein
MSFVSVQKLQKSYAGSPVFERIDCHIERGEFVTLLGPSGCGKSTLLRCIAGLTSVDSGQI
LLDGHDIVPLSPQKRGIGMVFQSYALFPNMTVEQNVAFGLRMQKVKADESQLRVREVLEL
VELGKFAGRYPHQLSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQIRAIQ
RELGLTTIFVTHDQEEALTMSDRIFLMNQGRIVQSGDAETLYTAPVDLFAAGFIGNYNLL
DADSASRLLQRPVASRLAIRPESITLGEHGELDAEVRSHSLLGNVIRYRVRVREVELVVD
VLNRSPADLHADGKRVSVSIDPTALREVA
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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