SitesBLAST
Comparing WP_010442691.1 NCBI__GCF_000192475.1:WP_010442691.1 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)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
49% identity, 96% coverage: 7:354/362 of query aligns to 2:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
49% identity, 96% coverage: 7:354/362 of query aligns to 3:355/371 of P68187
- A85 (= A89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A110) 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 (= E123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E128) 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 (≠ I232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ M245) 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 (= G277) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ A280) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G282) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V303) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E309) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S323) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G339) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G345) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F354) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
49% identity, 96% coverage: 7:354/362 of query aligns to 2:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F17), S37 (= S42), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), Q81 (= Q86), R128 (= R133), A132 (= A137), S134 (= S139), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S47), Q81 (= Q86)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
49% identity, 96% coverage: 7:354/362 of query aligns to 2:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F17), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), 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 (= S47), Q81 (= Q86)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
49% identity, 96% coverage: 7:354/362 of query aligns to 2:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F17), V17 (= V22), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R133), A132 (= A137), 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 (= S47), Q81 (= Q86)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
49% identity, 96% coverage: 7:354/362 of query aligns to 2:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F17), V17 (= V22), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R133), A132 (= A137), S134 (= S139), Q137 (= Q142)
- binding magnesium ion: S42 (= S47), Q81 (= Q86)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
49% identity, 96% coverage: 8:354/362 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F17), S35 (= S42), G36 (= G43), C37 (= C44), G38 (= G45), K39 (= K46), S40 (= S47), T41 (= T48), R126 (= R133), A130 (= A137), S132 (= S139), G134 (= G141), Q135 (= Q142)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
48% identity, 96% coverage: 7:354/362 of query aligns to 3:353/369 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.
- E306 (= E309) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 93% coverage: 23:358/362 of query aligns to 19:355/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S42), C40 (= C44), G41 (= G45), K42 (= K46), S43 (= S47), T44 (= T48), Q82 (= Q86), R129 (= R133), Q133 (≠ A137), S135 (= S139), G136 (= G140), G137 (= G141), Q159 (≠ E163), H192 (= H196)
- binding magnesium ion: S43 (= S47), Q82 (= Q86)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 93% coverage: 23:358/362 of query aligns to 19:356/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S42), G39 (= G43), G41 (= G45), K42 (= K46), S43 (= S47), Q82 (= Q86), Q133 (≠ A137), G136 (= G140), G137 (= G141), Q138 (= Q142), H192 (= H196)
- binding magnesium ion: S43 (= S47), Q82 (= Q86)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
48% identity, 95% coverage: 16:359/362 of query aligns to 15:371/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 93% coverage: 23:358/362 of query aligns to 17:377/384 of 8hplC
Sites not aligning to the query:
1g291 Malk (see paper)
48% identity, 94% coverage: 17:358/362 of query aligns to 13:367/372 of 1g291
- binding magnesium ion: D69 (≠ W73), E71 (= E75), K72 (vs. gap), K79 (≠ S77), D80 (= D78), E292 (= E286), D293 (= D292), K359 (≠ R350)
- binding pyrophosphate 2-: S38 (= S42), G39 (= G43), C40 (= C44), G41 (= G45), K42 (= K46), T43 (≠ S47), T44 (= T48)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
46% identity, 99% coverage: 3:359/362 of query aligns to 2:349/353 of 1vciA
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
48% identity, 93% coverage: 20:354/362 of query aligns to 8:324/344 of 2awnC
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, 92% coverage: 23:356/362 of query aligns to 20:381/393 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.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 96% coverage: 7:354/362 of query aligns to 2:312/330 of 2awnA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
47% identity, 65% coverage: 17:250/362 of query aligns to 27:258/378 of P69874
- F27 (= F17) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F35) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C44) mutation to T: Loss of ATPase activity and transport.
- L60 (= L50) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I66) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L125) mutation to M: Loss of ATPase activity and transport.
- D172 (= D162) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
47% identity, 65% coverage: 17:250/362 of query aligns to 12:243/358 of 8y5iA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 77% coverage: 18:295/362 of query aligns to 16:289/353 of 1oxvD
Sites not aligning to the query:
Query Sequence
>WP_010442691.1 NCBI__GCF_000192475.1:WP_010442691.1
MNINSHSVEVRDLDLHFGEVKVLQELNIDIHEGEFLVLLGSSGCGKSTLLNCIAGLLDVT
DGQIFIKGQNVTWKEPSDRGIGMVFQSYALYPQMTVEGNLSFGLKNARVARDEIAKRVAR
AAEILQIEPLLKRKPGALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRTDLRVEL
KRLHQQLKNTMIYVTHDQVEAMTLADRIAIMKGGKIMQLGSPDEIYNRPQNIYVAGFIGS
PAMNMIEGRIDNGHFAGHDLSLPLDGYEFERTDHHAGPVAIGIRPEHVLTGDAVETAAAQ
AEVEVQIVEKLGSDTLVHSTLGSLNLRFRMDGLSRVTEGDRLRIGFDTSRASLFDAVTET
RL
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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