SitesBLAST
Comparing WP_011384263.1 AMB_RS09395 ABC transporter ATP-binding protein 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)
44% identity, 81% coverage: 26:245/273 of query aligns to 27:240/378 of P69874
- F27 (= F26) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F44) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C53) mutation to T: Loss of ATPase activity and transport.
- L60 (= L59) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V75) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V131) mutation to M: Loss of ATPase activity and transport.
- D172 (= D168) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
42% identity, 71% coverage: 26:218/273 of query aligns to 16:217/375 of 2d62A
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
41% identity, 70% coverage: 27:218/273 of query aligns to 37:237/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
41% identity, 70% coverage: 27:218/273 of query aligns to 37:237/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
1g291 Malk (see paper)
43% identity, 71% coverage: 26:218/273 of query aligns to 13:214/372 of 1g291
- binding magnesium ion: D69 (≠ G82), E71 (= E86), K72 (≠ R87), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S51), G39 (= G52), C40 (= C53), G41 (= G54), K42 (= K55), T43 (≠ S56), T44 (= T57)
Sites not aligning to the query:
7ahdC Opua (e190q) occluded (see paper)
41% identity, 70% coverage: 27:218/273 of query aligns to 37:237/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ H29), S61 (= S51), G62 (= G52), G64 (= G54), K65 (= K55), S66 (= S56), T67 (= T57), Q111 (= Q92), K161 (≠ A142), Q162 (≠ A143), S164 (= S145), G166 (= G147), M167 (= M148), Q188 (≠ E169), H221 (= H202)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 75% coverage: 15:219/273 of query aligns to 1:209/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F26), S38 (= S51), G39 (= G52), G41 (= G54), K42 (= K55), S43 (= S56), Q82 (= Q92), Q133 (≠ A143), G136 (= G146), G137 (= G147), Q138 (≠ M148), H192 (= H202)
- binding magnesium ion: S43 (= S56), Q82 (= Q92)
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 75% coverage: 15:219/273 of query aligns to 1:209/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F26), S38 (= S51), C40 (= C53), G41 (= G54), K42 (= K55), S43 (= S56), T44 (= T57), Q82 (= Q92), R129 (= R139), Q133 (≠ A143), S135 (= S145), G136 (= G146), G137 (= G147), Q159 (≠ E169), H192 (= H202)
- binding magnesium ion: S43 (= S56), Q82 (= Q92)
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 75% coverage: 15:219/273 of query aligns to 1:207/384 of 8hplC
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)
42% identity, 69% coverage: 29:217/273 of query aligns to 17:208/393 of P9WQI3
- H193 (= H202) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 1:209/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F26), S35 (= S51), G36 (= G52), C37 (= C53), G38 (= G54), K39 (= K55), S40 (= S56), T41 (= T57), R126 (= R139), A130 (= A143), S132 (= S145), G134 (= G147), Q135 (≠ M148)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 3:211/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F26), S37 (= S51), G38 (= G52), C39 (= C53), G40 (= G54), K41 (= K55), S42 (= S56), T43 (= T57), Q81 (= Q92), R128 (= R139), A132 (= A143), S134 (= S145), G136 (= G147), Q137 (≠ M148), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (= S56), Q81 (= Q92)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 3:211/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F26), G38 (= G52), C39 (= C53), G40 (= G54), K41 (= K55), S42 (= S56), T43 (= T57), R128 (= R139), S134 (= S145), Q137 (≠ M148)
- binding beryllium trifluoride ion: S37 (= S51), G38 (= G52), K41 (= K55), Q81 (= Q92), S134 (= S145), G136 (= G147), H191 (= H202)
- binding magnesium ion: S42 (= S56), Q81 (= Q92)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 3:211/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F26), V17 (≠ A31), G38 (= G52), C39 (= C53), G40 (= G54), K41 (= K55), S42 (= S56), T43 (= T57), R128 (= R139), A132 (= A143), S134 (= S145), Q137 (≠ M148)
- binding tetrafluoroaluminate ion: S37 (= S51), G38 (= G52), K41 (= K55), Q81 (= Q92), S134 (= S145), G135 (= G146), G136 (= G147), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (= S56), Q81 (= Q92)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 3:211/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F26), V17 (≠ A31), G38 (= G52), C39 (= C53), G40 (= G54), K41 (= K55), S42 (= S56), T43 (= T57), R128 (= R139), A132 (= A143), S134 (= S145), Q137 (≠ M148)
- binding magnesium ion: S42 (= S56), Q81 (= Q92)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 76% coverage: 17:224/273 of query aligns to 4:212/371 of P68187
- A85 (≠ S95) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ T116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Y127) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D129) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G134) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G147) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D168) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 76% coverage: 17:224/273 of query aligns to 3:211/374 of 2awnB
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 84% coverage: 17:244/273 of query aligns to 2:219/348 of 3d31A
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)
39% identity, 76% coverage: 17:224/273 of query aligns to 4:212/369 of P19566
- L86 (= L96) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P170) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D175) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
40% identity, 74% coverage: 17:218/273 of query aligns to 7:203/353 of 1vciA
Query Sequence
>WP_011384263.1 AMB_RS09395 ABC transporter ATP-binding protein
MNALPNRRSLTVTRGRIGIQRLSVSFGAHAAVEDFSLEIEPGEFVCLLGPSGCGKSTALN
AVAGFLRPARGRVAVDGVEVTGPGPERGMVFQQHSLFPWKTVLENVAFGPRMQGKTRAEA
RDLAREYLDLVGLGGSAQRYPAALSGGMAQRVGIARALVNHPSVLLMDEPFGALDAQTRS
IMQESLLRLWGQIGNTVLFVTHDIDEALFLADRVVVMSAAPGRVLLDLRLDLPRPRPEDV
FATPQFAEHKRQCLRLIRQESRRAFDFIDGAGI
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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