SitesBLAST
Comparing WP_011649609.1 NCBI__GCF_000009265.1:WP_011649609.1 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)
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)
41% identity, 81% coverage: 1:289/356 of query aligns to 1:288/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 97% coverage: 1:346/356 of query aligns to 4:366/375 of 2d62A
1g291 Malk (see paper)
39% identity, 82% coverage: 24:314/356 of query aligns to 18:329/372 of 1g291
- binding magnesium ion: D69 (≠ N75), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q79), D80 (≠ S80), E292 (= E286), D293 (vs. gap)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 81% coverage: 2:288/356 of query aligns to 1:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (≠ T49), T44 (= T50), Q82 (= Q88), R129 (= R135), Q133 (≠ G139), S135 (≠ T141), G136 (≠ A142), G137 (≠ D143), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T49), Q82 (= Q88)
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 81% coverage: 2:288/356 of query aligns to 1:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (≠ T49), Q82 (= Q88), Q133 (≠ G139), G136 (≠ A142), G137 (≠ D143), Q138 (= Q144), H192 (= H199)
- binding magnesium ion: S43 (≠ T49), Q82 (= Q88)
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 81% coverage: 2:288/356 of query aligns to 1:284/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
32% identity, 97% coverage: 1:346/356 of query aligns to 4:344/353 of 1vciA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 91% coverage: 1:325/356 of query aligns to 1:319/369 of P19566
- L86 (≠ I92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ R312) 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)
33% identity, 91% coverage: 1:325/356 of query aligns to 1:321/371 of P68187
- A85 (≠ V91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ D143) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ T235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F248) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ Y269) 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 (≠ E280) 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 (= G306) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ R312) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 91% coverage: 2:325/356 of query aligns to 1:320/374 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)
33% identity, 91% coverage: 2:325/356 of query aligns to 1:320/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), Q81 (= Q88), R128 (= R135), A132 (≠ G139), S134 (≠ T141), G136 (≠ D143), Q137 (= Q144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 91% coverage: 2:325/356 of query aligns to 1:320/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R135), S134 (≠ T141), Q137 (= Q144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G136 (≠ D143), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
33% identity, 91% coverage: 2:325/356 of query aligns to 1:320/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ K18), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R135), A132 (≠ G139), S134 (≠ T141), Q137 (= Q144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G135 (≠ A142), G136 (≠ D143), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
33% identity, 91% coverage: 2:325/356 of query aligns to 1:320/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ K18), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R135), A132 (≠ G139), S134 (≠ T141), Q137 (= Q144)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
34% identity, 84% coverage: 26:325/356 of query aligns to 17:318/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (≠ T49), T41 (= T50), R126 (= R135), A130 (≠ G139), S132 (≠ T141), G134 (≠ D143), Q135 (= Q144)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 62% coverage: 27:246/356 of query aligns to 35:253/378 of P69874
- F45 (≠ A37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I127) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 84% coverage: 26:325/356 of query aligns to 12:290/344 of 2awnC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
37% identity, 62% coverage: 21:242/356 of query aligns to 12:229/348 of 3d31A
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
30% identity, 82% coverage: 1:293/356 of query aligns to 1:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
30% identity, 82% coverage: 1:293/356 of query aligns to 1:286/353 of 1oxvA
Query Sequence
>WP_011649609.1 NCBI__GCF_000009265.1:WP_011649609.1
MARITLDHIRHAYGANPKSDKDYSLKEVDHEWNDGGAYALLGPSGCGKTTLLNIISGLLQ
PSHGRILFDGKDVTNLSTQSRNIAQVFQFPVIYDTMTVYDNLAFPLRNRGVAEADVDRRV
RDILEMIDLASWARRKAQGLTADQKQKISLGRGLVRNDVNAILFDEPLTVIDPHMKWVLR
SQLKRLHKQFGFTMVYVTHDQTEALTFAEKVVVMYDGQIVQIGTPAELFERPSHTFVGYF
IGSPGMNFMPARIEGSTVKVGDETLTLEYAPKTSGTAKTELGIRPEFIRLGREGMPITIS
KVEDIGRQKIVRARFADQPIAIVVPEDADIPADARVTFDPSAISIYADSWRVGREA
Or try a new SitesBLAST search
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