SitesBLAST
Comparing SMc01631 FitnessBrowser__Smeli:SMc01631 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)
47% identity, 92% coverage: 9:338/359 of query aligns to 18:352/378 of P69874
- C26 (≠ R17) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y18) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V128) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ K268) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E286) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
49% identity, 65% coverage: 8:242/359 of query aligns to 6:244/375 of 2d62A
1g291 Malk (see paper)
52% identity, 64% coverage: 13:242/359 of query aligns to 8:241/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ M72), K72 (≠ N73), K79 (≠ Y78), D80 (≠ R79)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49)
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)
39% identity, 97% coverage: 8:357/359 of query aligns to 6:344/353 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)
37% identity, 97% coverage: 9:357/359 of query aligns to 4:353/369 of P19566
- L86 (= L91) 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 (≠ I306) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 97% coverage: 9:357/359 of query aligns to 3:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 97% coverage: 9:357/359 of query aligns to 4:355/371 of P68187
- A85 (= A90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G144) 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 (≠ L235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ R246) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ G265) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ A276) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ M280) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ A282) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G300) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I306) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ G320) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G342) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ S348) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F357) 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)
37% identity, 97% coverage: 9:357/359 of query aligns to 3:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y18), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q87), R128 (= R136), A132 (≠ E140), S134 (= S142), G136 (= G144), Q137 (= Q145), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 97% coverage: 9:357/359 of query aligns to 3:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), S134 (= S142), Q137 (= Q145)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S142), G136 (= G144), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 97% coverage: 9:357/359 of query aligns to 3:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), A132 (≠ E140), S134 (= S142), Q137 (= Q145)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S142), G135 (= G143), G136 (= G144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 97% coverage: 9:357/359 of query aligns to 3:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), A132 (≠ E140), S134 (= S142), Q137 (= Q145)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 97% coverage: 9:357/359 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y18), S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (≠ T48), T41 (= T49), R126 (= R136), A130 (≠ E140), S132 (= S142), G134 (= G144), Q135 (= Q145)
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 98% coverage: 8:359/359 of query aligns to 2:353/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y18), S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (≠ T48), T44 (= T49), Q82 (= Q87), R129 (= R136), Q133 (≠ E140), S135 (= S142), G136 (= G143), G137 (= G144), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 98% coverage: 8:359/359 of query aligns to 2:354/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y18), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (≠ T48), Q82 (= Q87), Q133 (≠ E140), G136 (= G143), G137 (= G144), Q138 (= Q145), H192 (= H199)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
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, 78% coverage: 8:288/359 of query aligns to 3:287/393 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.
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 82% coverage: 8:300/359 of query aligns to 2:298/384 of 8hplC
3d31A Modbc from methanosarcina acetivorans (see paper)
32% identity, 97% coverage: 9:357/359 of query aligns to 2:347/348 of 3d31A
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 94% coverage: 20:357/359 of query aligns to 7:324/344 of 2awnC
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 79% coverage: 12:293/359 of query aligns to 7:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 79% coverage: 12:293/359 of query aligns to 7:286/353 of 1oxvA
Query Sequence
>SMc01631 FitnessBrowser__Smeli:SMc01631
MTSASTNDIEFRSVAKRYGSVTAVSDINLTVPKGAFVALLGPSGCGKTTCLRMIGGFEQP
SEGMVYIGGQPMNGVPAYRRPVNMVFQQYALFPHLDVEQNVAYGLKQTRPRIPAAEITRR
AQEALEMVRLGGFGKRRIHEMSGGQQQRVALARAIVNKPKVLLLDEPLAALDKKLRTAMQ
IELQSLQRELGITFVLVTHDQEEALSMSDFVCVMSTGRIVQIGPPQEIYDRPASLFVADF
VGKTNRIAGTIEPGAGAVLLANGVGLAKPARANGTAGPVMVALRPEAISLVRDGSAALRG
TVTHRIFLGSSVEYSVEVEGLGDFLVTADRRSLNDSDLAEPGERIGLSFDPNAMHVFPA
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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