SitesBLAST
Comparing 3608192 Dshi_1597 ABC transporter related (RefSeq) 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)
46% identity, 86% coverage: 3:306/355 of query aligns to 15:324/378 of P69874
- C26 (≠ Y14) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y15) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ V260) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E282) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 87% coverage: 6:315/355 of query aligns to 3:319/374 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, 87% coverage: 6:315/355 of query aligns to 3:319/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y15), S37 (= S40), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), Q81 (= Q84), R128 (= R132), A132 (= A136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 87% coverage: 6:315/355 of query aligns to 3:319/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R132), S134 (= S138), Q137 (= Q141)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 87% coverage: 6:315/355 of query aligns to 3:319/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R132), A132 (= A136), S134 (= S138), Q137 (= Q141)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 87% coverage: 6:315/355 of query aligns to 3:319/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R132), A132 (= A136), S134 (= S138), Q137 (= Q141)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q84)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 87% coverage: 6:315/355 of query aligns to 4:320/371 of P68187
- A85 (= A87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R231) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F242) 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 (= G270) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T274) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G278) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G297) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E303) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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, 87% coverage: 6:315/355 of query aligns to 1:317/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y15), S35 (= S40), G36 (= G41), C37 (= C42), G38 (= G43), K39 (= K44), S40 (≠ T45), T41 (= T46), R126 (= R132), A130 (= A136), S132 (= S138), G134 (= G140), Q135 (= Q141)
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, 87% coverage: 6:315/355 of query aligns to 4:318/369 of P19566
- L86 (≠ I88) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D168) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E303) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
44% identity, 78% coverage: 6:282/355 of query aligns to 7:295/375 of 2d62A
1g291 Malk (see paper)
44% identity, 79% coverage: 6:284/355 of query aligns to 4:294/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ N75), D80 (≠ K76), E292 (= E282), D293 (≠ G283)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46)
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)
37% identity, 98% coverage: 6:353/355 of query aligns to 7:344/353 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)
42% identity, 79% coverage: 6:284/355 of query aligns to 4:278/393 of P9WQI3
- H193 (= H195) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 83% coverage: 22:315/355 of query aligns to 12:289/344 of 2awnC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 6:282/355 of query aligns to 3:284/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S40), C40 (= C42), G41 (= G43), K42 (= K44), S43 (≠ T45), T44 (= T46), Q82 (= Q84), R129 (= R132), Q133 (≠ A136), S135 (= S138), G136 (= G139), G137 (= G140), Q159 (≠ E162), H192 (= H195)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q84)
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 6:282/355 of query aligns to 3:284/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (≠ T45), Q82 (= Q84), Q133 (≠ A136), G136 (= G139), G137 (= G140), Q138 (= Q141), H192 (= H195)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q84)
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 78% coverage: 6:282/355 of query aligns to 3:282/384 of 8hplC
3d31A Modbc from methanosarcina acetivorans (see paper)
36% identity, 81% coverage: 5:291/355 of query aligns to 1:283/348 of 3d31A
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
40% identity, 79% coverage: 6:286/355 of query aligns to 4:284/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y15), Q14 (≠ G16), T16 (≠ Y18), V18 (≠ A20), S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46), R133 (= R132), E137 (≠ A136), S139 (= S138), G141 (= G140), Q142 (= Q141)
- binding calcium ion: T43 (= T45), Q86 (= Q84)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 80% coverage: 6:289/355 of query aligns to 4:286/353 of 1oxvD
Query Sequence
>3608192 Dshi_1597 ABC transporter related (RefSeq)
MTAPLIRIQNVQKYYGSYHALRDVSVDIGAGEFFSLLGPSGCGKTTLLRTIAGFEEFESG
TLTLGGVDMVGVPANKRPTNMVFQSYAIFPHLSVGDNVGFGLRRRTDLTGEARASLVADA
LHMVGLKGYGARAAHALSGGQRQRVALARALVLKPKVLLLDEPLSALDKKMREQMQTELR
RLQRHVGITFILVTHDQEEALTMSDRIAVMFEGRIAQLAPPQTLYAQPASRAVAEFIGTM
SFLPAEISGDRADVAGLGTVPVTADQCAEGATGTCVAGVRPEGMALDFDETGQGTPGEVV
EREYFGDMTSYHVRLDGTDRLVEIAMKNGPGIPVLDPGARTRVQWSPEALRYFAA
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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