SitesBLAST
Comparing WP_024851725.1 NCBI__GCF_000526715.1:WP_024851725.1 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)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
41% identity, 89% coverage: 5:255/282 of query aligns to 5:250/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
40% identity, 89% coverage: 5:255/282 of query aligns to 3:248/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (≠ F14), H40 (≠ A42), S41 (= S43), G42 (= G44), G44 (= G46), K45 (= K47), S46 (= S48), T47 (= T49), Q82 (= Q84), Q135 (= Q142), S137 (= S144), G139 (= G146), M140 (= M147), H194 (= H201)
- binding magnesium ion: S46 (= S48), Q82 (= Q84)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
43% identity, 83% coverage: 23:256/282 of query aligns to 22:250/658 of 8wm7C
Sites not aligning to the query:
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
42% identity, 83% coverage: 24:256/282 of query aligns to 23:250/256 of 8w9mC
- binding adenosine-5'-triphosphate: S42 (= S43), G43 (= G44), G45 (= G46), K46 (= K47), S47 (= S48), T48 (= T49), Q83 (= Q84), K132 (≠ S138), E136 (≠ Q142), S138 (= S144), G140 (= G146), H195 (= H201)
- binding magnesium ion: S47 (= S48), Q83 (= Q84)
Sites not aligning to the query:
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)
44% identity, 76% coverage: 4:216/282 of query aligns to 3:208/393 of P9WQI3
- H193 (= H201) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 76% coverage: 4:216/282 of query aligns to 2:207/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (= S48), Q82 (= Q84), Q133 (= Q142), G136 (= G145), G137 (= G146), Q138 (≠ M147), H192 (= H201)
- binding magnesium ion: S43 (= S48), Q82 (= Q84)
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 76% coverage: 4:216/282 of query aligns to 2:207/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (= S48), T44 (= T49), Q82 (= Q84), R129 (≠ S138), Q133 (= Q142), S135 (= S144), G136 (= G145), G137 (= G146), Q159 (≠ E168), H192 (= H201)
- binding magnesium ion: S43 (= S48), Q82 (= Q84)
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 72% coverage: 15:216/282 of query aligns to 8:205/384 of 8hplC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 78% coverage: 5:225/282 of query aligns to 18:228/378 of P69874
- C26 (≠ T13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) 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 (≠ V67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ M130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
40% identity, 78% coverage: 7:225/282 of query aligns to 5:213/358 of 8y5iA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 75% coverage: 15:226/282 of query aligns to 8:214/374 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)
43% identity, 75% coverage: 15:226/282 of query aligns to 8:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (vs. gap), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q84), R128 (≠ S138), A132 (≠ Q142), S134 (= S144), G136 (= G146), Q137 (≠ M147), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 75% coverage: 15:226/282 of query aligns to 8:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (vs. gap), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ S138), S134 (= S144), Q137 (≠ M147)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S144), G136 (= G146), H191 (= H201)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 75% coverage: 15:226/282 of query aligns to 8:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (vs. gap), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ S138), A132 (≠ Q142), S134 (= S144), Q137 (≠ M147)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
43% identity, 75% coverage: 15:226/282 of query aligns to 8:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (vs. gap), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ S138), A132 (≠ Q142), S134 (= S144), Q137 (≠ M147)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 75% coverage: 15:226/282 of query aligns to 9:215/371 of P68187
- A85 (≠ S87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ S123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E133) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G146) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D167) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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)
43% identity, 75% coverage: 15:226/282 of query aligns to 6:212/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (vs. gap), S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (= S48), T41 (= T49), R126 (≠ S138), A130 (≠ Q142), S132 (= S144), G134 (= G146), Q135 (≠ M147)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
39% identity, 74% coverage: 19:226/282 of query aligns to 17:224/375 of 2d62A
1g291 Malk (see paper)
40% identity, 74% coverage: 19:228/282 of query aligns to 14:229/372 of 1g291
- binding magnesium ion: D69 (≠ K74), E71 (≠ G76), K72 (= K77), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
42% identity, 75% coverage: 15:226/282 of query aligns to 9:215/369 of P19566