SitesBLAST
Comparing WP_011938227.1 NCBI__GCF_000016745.1:WP_011938227.1 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)
1g291 Malk (see paper)
51% identity, 69% coverage: 10:254/353 of query aligns to 8:254/372 of 1g291
- binding magnesium ion: D69 (≠ E71), E71 (≠ A73), K72 (= K74), K79 (≠ E81), D80 (≠ K82)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (≠ S42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
50% identity, 69% coverage: 15:257/353 of query aligns to 16:259/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 80% coverage: 20:301/353 of query aligns to 32:308/378 of P69874
- F45 (≠ I33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L269) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E290) 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)
43% identity, 80% coverage: 19:301/353 of query aligns to 16:293/358 of 8y5iA
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
48% identity, 67% coverage: 21:255/353 of query aligns to 17:247/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 67% coverage: 21:255/353 of query aligns to 19:249/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S40), C40 (≠ S42), G41 (= G43), K42 (= K44), S43 (≠ T45), T44 (= T46), Q82 (= Q90), R129 (= R137), Q133 (= Q141), S135 (= S143), G136 (= G144), G137 (= G145), Q159 (≠ E167), H192 (= H200)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q90)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 67% coverage: 21:255/353 of query aligns to 19:249/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (≠ T45), Q82 (= Q90), Q133 (= Q141), G136 (= G144), G137 (= G145), Q138 (= Q146), H192 (= H200)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q90)
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
41% identity, 80% coverage: 16:296/353 of query aligns to 16:285/353 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)
41% identity, 80% coverage: 16:296/353 of query aligns to 16:285/353 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)
41% identity, 80% coverage: 16:296/353 of query aligns to 16:285/353 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)
41% identity, 80% coverage: 16:296/353 of query aligns to 16:285/353 of Q97UY8
- S142 (= S143) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G145) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E167) 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+).
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, 63% coverage: 21:244/353 of query aligns to 20:237/393 of P9WQI3
- H193 (= H200) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 75% coverage: 1:263/353 of query aligns to 1:257/371 of P68187
- A85 (= A93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L236) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ T247) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 70% coverage: 16:263/353 of query aligns to 13:256/374 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)
46% identity, 70% coverage: 16:263/353 of query aligns to 13:256/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S40), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), Q81 (= Q90), R128 (= R137), A132 (≠ Q141), S134 (= S143), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q90)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
46% identity, 70% coverage: 16:263/353 of query aligns to 13:256/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R137), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q90), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q90)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
46% identity, 70% coverage: 16:263/353 of query aligns to 13:256/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ I20), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (= R137), A132 (≠ Q141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q90)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
46% identity, 70% coverage: 16:263/353 of query aligns to 13:256/371 of 3puvA