SitesBLAST
Comparing WP_092347428.1 NCBI__GCF_900107645.1:WP_092347428.1 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)
37% identity, 97% coverage: 3:353/362 of query aligns to 4:356/372 of 1g291
- binding magnesium ion: D69 (≠ S72), E71 (≠ D74), K72 (= K75), K79 (≠ E82), D80 (≠ N83), E292 (= E291), D293 (vs. gap)
- binding pyrophosphate 2-: S38 (= S41), G39 (= G42), C40 (= C43), G41 (= G44), K42 (= K45), T43 (= T46), T44 (= T47)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 93% coverage: 19:353/362 of query aligns to 19:359/375 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, 78% coverage: 15:295/362 of query aligns to 28:301/378 of P69874
- F45 (≠ I34) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C43) mutation to T: Loss of ATPase activity and transport.
- L60 (= L49) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I65) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L271) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E291) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 99% coverage: 1:358/362 of query aligns to 5:344/353 of 1vciA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 86% coverage: 1:310/362 of query aligns to 2:298/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 86% coverage: 1:310/362 of query aligns to 2:298/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 86% coverage: 1:310/362 of query aligns to 2:298/353 of 1oxuA
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)
37% identity, 86% coverage: 1:310/362 of query aligns to 2:298/353 of Q97UY8
- S142 (= S144) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G146) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E168) 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+).
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 99% coverage: 3:360/362 of query aligns to 4:353/369 of P19566
- L86 (≠ I95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P169) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D174) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E319) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 3:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
35% identity, 99% coverage: 3:360/362 of query aligns to 4:355/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D133) 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.
- R228 (≠ K237) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L248) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ I270) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G281) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ M285) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ C287) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G309) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I315) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ T330) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G345) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ S351) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (≠ L360) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y12), S35 (= S41), G36 (= G42), C37 (= C43), G38 (= G44), K39 (= K45), S40 (≠ T46), T41 (= T47), R126 (= R138), A130 (≠ K142), S132 (= S144), G134 (= G146), Q135 (= Q147)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 3:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y12), S37 (= S41), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (≠ T46), T43 (= T47), Q81 (= Q91), R128 (= R138), A132 (≠ K142), S134 (= S144), G136 (= G146), Q137 (= Q147), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (≠ T46), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 3:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (≠ T46), T43 (= T47), R128 (= R138), S134 (= S144), Q137 (= Q147)
- binding beryllium trifluoride ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q91), S134 (= S144), G136 (= G146), H191 (= H201)
- binding magnesium ion: S42 (≠ T46), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 3:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (≠ K20), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (≠ T46), T43 (= T47), R128 (= R138), A132 (≠ K142), S134 (= S144), Q137 (= Q147)
- binding tetrafluoroaluminate ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q91), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (≠ T46), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
35% identity, 99% coverage: 3:360/362 of query aligns to 3:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (≠ K20), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (≠ T46), T43 (= T47), R128 (= R138), A132 (≠ K142), S134 (= S144), Q137 (= Q147)
- binding magnesium ion: S42 (≠ T46), Q81 (= Q91)
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 67% coverage: 2:244/362 of query aligns to 2:233/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 67% coverage: 2:244/362 of query aligns to 2:235/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S41), C40 (= C43), G41 (= G44), K42 (= K45), S43 (≠ T46), T44 (= T47), Q82 (= Q91), R129 (= R138), Q133 (≠ K142), S135 (= S144), G136 (= G145), G137 (= G146), Q159 (≠ E168), H192 (= H201)
- binding magnesium ion: S43 (≠ T46), Q82 (= Q91)
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 67% coverage: 2:244/362 of query aligns to 2:235/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S41), G39 (= G42), G41 (= G44), K42 (= K45), S43 (≠ T46), Q82 (= Q91), Q133 (≠ K142), G136 (= G145), G137 (= G146), Q138 (= Q147), H192 (= H201)
- binding magnesium ion: S43 (≠ T46), Q82 (= Q91)
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)
38% identity, 80% coverage: 5:294/362 of query aligns to 5:288/393 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.
Query Sequence
>WP_092347428.1 NCBI__GCF_900107645.1:WP_092347428.1
MEIRIKDLTRTYYSEGKQIKALDHVDLTIPANKIFTLLGPSGCGKTTLLRCIVGLETPDD
GDIYIGDDLVFSKDKGLFIPPENRGLGMVFQTYAIWPHMNVFDNVAYPLQTNRTPKDKIR
QQVVKALKFVQLDGFENRPATKLSGGQQQRVALARALVAEPKVILFDEPLSNLDAKLREE
TRKELRSFLTELKITAIYVTHDRIEALALSDLIAVMRAGKIIEIGDPKKIYFNSDDKFVA
DFIGRANLIKGKIEKQEGEHAIIASEIGSILALNSQGISVGQSAMLCVRPEFIRLAPEQG
KQGQNIFSGQMESLIFIGEAYEGEIRIGDTLLTTTIEPTANIVEGDKISISFDPDHCFLL
SA
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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