SitesBLAST
Comparing WP_200806763.1 NCBI__GCF_900167125.1:WP_200806763.1 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
47% identity, 81% coverage: 43:370/406 of query aligns to 16:336/378 of P69874
- C26 (≠ R53) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F54) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L72) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C81) mutation to T: Loss of ATPase activity and transport.
- L60 (= L87) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I103) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V162) mutation to M: Loss of ATPase activity and transport.
- D172 (= D199) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ F304) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ Q325) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
46% identity, 81% coverage: 43:370/406 of query aligns to 1:321/358 of 8y5iA
1g291 Malk (see paper)
49% identity, 63% coverage: 44:298/406 of query aligns to 3:267/372 of 1g291
- binding magnesium ion: D69 (= D110), E71 (vs. gap), K72 (vs. gap), K79 (≠ H114), D80 (≠ K115)
- binding pyrophosphate 2-: S38 (= S79), G39 (= G80), C40 (= C81), G41 (= G82), K42 (= K83), T43 (= T84), T44 (= T85)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
48% identity, 63% coverage: 45:300/406 of query aligns to 7:272/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 63% coverage: 44:298/406 of query aligns to 2:257/374 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)
46% identity, 63% coverage: 44:298/406 of query aligns to 2:257/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F54), S37 (= S79), G38 (= G80), C39 (= C81), G40 (= G82), K41 (= K83), S42 (≠ T84), T43 (= T85), Q81 (= Q123), R128 (= R170), A132 (≠ Q174), S134 (= S176), G136 (= G178), Q137 (= Q179), E158 (= E200), H191 (= H233)
- binding magnesium ion: S42 (≠ T84), Q81 (= Q123)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
46% identity, 63% coverage: 44:298/406 of query aligns to 2:257/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F54), G38 (= G80), C39 (= C81), G40 (= G82), K41 (= K83), S42 (≠ T84), T43 (= T85), R128 (= R170), S134 (= S176), Q137 (= Q179)
- binding beryllium trifluoride ion: S37 (= S79), G38 (= G80), K41 (= K83), Q81 (= Q123), S134 (= S176), G136 (= G178), H191 (= H233)
- binding magnesium ion: S42 (≠ T84), Q81 (= Q123)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
46% identity, 63% coverage: 44:298/406 of query aligns to 2:257/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F54), V17 (≠ A59), G38 (= G80), C39 (= C81), G40 (= G82), K41 (= K83), S42 (≠ T84), T43 (= T85), R128 (= R170), A132 (≠ Q174), S134 (= S176), Q137 (= Q179)
- binding tetrafluoroaluminate ion: S37 (= S79), G38 (= G80), K41 (= K83), Q81 (= Q123), S134 (= S176), G135 (= G177), G136 (= G178), E158 (= E200), H191 (= H233)
- binding magnesium ion: S42 (≠ T84), Q81 (= Q123)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
46% identity, 63% coverage: 44:298/406 of query aligns to 2:257/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F54), V17 (≠ A59), G38 (= G80), C39 (= C81), G40 (= G82), K41 (= K83), S42 (≠ T84), T43 (= T85), R128 (= R170), A132 (≠ Q174), S134 (= S176), Q137 (= Q179)
- binding magnesium ion: S42 (≠ T84), Q81 (= Q123)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
46% identity, 63% coverage: 44:298/406 of query aligns to 3:258/371 of P68187
- A85 (= A126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S147) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V155) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A158) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E160) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ P165) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G178) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D199) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ Y269) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F280) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 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)
46% identity, 63% coverage: 45:298/406 of query aligns to 1:255/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F54), S35 (= S79), G36 (= G80), C37 (= C81), G38 (= G82), K39 (= K83), S40 (≠ T84), T41 (= T85), R126 (= R170), A130 (≠ Q174), S132 (= S176), G134 (= G178), Q135 (= Q179)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 66% coverage: 45:311/406 of query aligns to 7:267/353 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)
47% identity, 60% coverage: 44:285/406 of query aligns to 3:246/369 of P19566
- L86 (= L127) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P201) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D206) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
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)
48% identity, 57% coverage: 59:288/406 of query aligns to 19:250/393 of P9WQI3
- H193 (= H233) 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)
48% identity, 55% coverage: 59:283/406 of query aligns to 16:242/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 55% coverage: 59:283/406 of query aligns to 18:244/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S79), G39 (= G80), G41 (= G82), K42 (= K83), S43 (≠ T84), Q82 (= Q123), Q133 (= Q174), G136 (= G177), G137 (= G178), Q138 (= Q179), H192 (= H233)
- binding magnesium ion: S43 (≠ T84), Q82 (= Q123)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 55% coverage: 59:283/406 of query aligns to 18:244/362 of 8hprD