SitesBLAST
Comparing WP_011020381.1 NCBI__GCF_000007345.1:WP_011020381.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 99% coverage: 3:353/353 of query aligns to 1:348/348 of 3d31A
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
33% identity, 95% coverage: 18:353/353 of query aligns to 22:367/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 94% coverage: 14:344/353 of query aligns to 17:336/353 of 1vciA
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)
36% identity, 74% coverage: 21:280/353 of query aligns to 36:299/378 of P69874
- F45 (≠ Y30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E278) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
36% identity, 74% coverage: 21:280/353 of query aligns to 21:284/358 of 8y5iA
Sites not aligning to the query:
1g291 Malk (see paper)
36% identity, 62% coverage: 18:235/353 of query aligns to 19:242/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ D72), D80 (≠ K73)
- binding pyrophosphate 2-: S38 (= S37), G39 (= G38), C40 (≠ S39), G41 (= G40), K42 (= K41), T43 (≠ S42), T44 (≠ L43)
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 78% coverage: 18:291/353 of query aligns to 21:292/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 78% coverage: 18:291/353 of query aligns to 21:292/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 78% coverage: 18:291/353 of query aligns to 21:292/353 of 1oxuA
Sites not aligning to the query:
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
36% identity, 78% coverage: 18:291/353 of query aligns to 21:292/353 of Q97UY8
- S142 (= S134) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G136) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E158) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 75% coverage: 19:281/353 of query aligns to 17:288/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S37), G36 (= G38), C37 (≠ S39), G38 (= G40), K39 (= K41), S40 (= S42), T41 (≠ L43), R126 (= R128), A130 (≠ T132), S132 (= S134), G134 (= G136), Q135 (≠ E137)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 75% coverage: 19:281/353 of query aligns to 20:291/371 of P68187
- A85 (≠ M84) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ R123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D227) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ V237) 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 (= G268) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T272) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ S274) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 75% coverage: 19:281/353 of query aligns to 19:290/374 of 2awnB
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 75% coverage: 19:281/353 of query aligns to 19:290/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S37), G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (≠ L43), Q81 (= Q81), R128 (= R128), A132 (≠ T132), S134 (= S134), G136 (= G136), Q137 (≠ E137), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (= S42), Q81 (= Q81)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 75% coverage: 19:281/353 of query aligns to 19:290/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (≠ L43), R128 (= R128), S134 (= S134), Q137 (≠ E137)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q81), S134 (= S134), G136 (= G136), H191 (= H191)
- binding magnesium ion: S42 (= S42), Q81 (= Q81)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 75% coverage: 19:281/353 of query aligns to 19:290/371 of 3puwA