SitesBLAST
Comparing WP_012170620.1 NCBI__GCF_000010525.1:WP_012170620.1 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 83% coverage: 22:319/359 of query aligns to 36:338/378 of P69874
- F45 (≠ L31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: Loss of ATPase activity and transport.
- C276 (= C259) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E277) 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.
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 87% coverage: 3:315/359 of query aligns to 2:312/348 of 3d31A
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
42% identity, 77% coverage: 2:279/359 of query aligns to 6:297/375 of 2d62A
1g291 Malk (see paper)
40% identity, 88% coverage: 14:329/359 of query aligns to 14:349/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ H73), D80 (≠ E74), E292 (= E277), D293 (≠ H278)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (≠ S40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)
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)
41% identity, 77% coverage: 2:279/359 of query aligns to 3:287/393 of P9WQI3
- H193 (= H192) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
43% identity, 78% coverage: 1:279/359 of query aligns to 5:278/353 of 1vciA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 78% coverage: 2:281/359 of query aligns to 3:290/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) 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.
8hprC Lpqy-sugabc in state 4 (see paper)
44% identity, 64% coverage: 5:235/359 of query aligns to 5:235/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (= S43), Q82 (= Q82), Q133 (≠ S133), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
8hprD Lpqy-sugabc in state 4 (see paper)
44% identity, 64% coverage: 5:235/359 of query aligns to 5:235/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y12), S38 (= S38), C40 (≠ S40), G41 (= G41), K42 (= K42), S43 (= S43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (≠ S133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (= S43), Q82 (= Q82)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 78% coverage: 2:281/359 of query aligns to 2:291/374 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)
40% identity, 78% coverage: 2:281/359 of query aligns to 2:291/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y12), S37 (= S38), G38 (= G39), C39 (≠ S40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ S133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 78% coverage: 2:281/359 of query aligns to 2:291/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), G38 (= G39), C39 (≠ S40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 78% coverage: 2:281/359 of query aligns to 2:291/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (≠ G18), G38 (= G39), C39 (≠ S40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ S133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 78% coverage: 2:281/359 of query aligns to 2:291/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y12), V17 (≠ G18), G38 (= G39), C39 (≠ S40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (= R129), A132 (≠ S133), S134 (= S135), Q137 (= Q138)
- binding magnesium ion: S42 (= S43), Q81 (= Q82)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 78% coverage: 2:281/359 of query aligns to 3:292/371 of P68187
- A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L239) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ E256) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G267) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ I271) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ L273) 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.
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 64% coverage: 5:235/359 of query aligns to 5:233/384 of 8hplC
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 78% coverage: 3:281/359 of query aligns to 1:289/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y12), S35 (= S38), G36 (= G39), C37 (≠ S40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (= R129), A130 (≠ S133), S132 (= S135), G134 (= G137), Q135 (= Q138)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
42% identity, 64% coverage: 6:234/359 of query aligns to 29:263/382 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)
42% identity, 64% coverage: 6:234/359 of query aligns to 29:263/382 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
7ahdC Opua (e190q) occluded (see paper)
41% identity, 63% coverage: 6:230/359 of query aligns to 29:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (= T16), S61 (= S38), G62 (= G39), G64 (= G41), K65 (= K42), S66 (= S43), T67 (= T44), Q111 (= Q82), K161 (≠ T132), Q162 (≠ S133), S164 (= S135), G166 (= G137), M167 (≠ Q138), Q188 (≠ E159), H221 (= H192)
Sites not aligning to the query:
Query Sequence
>WP_012170620.1 NCBI__GCF_000010525.1:WP_012170620.1
MSVRFENVSFRYPGTTTGVFDIDLEIATGELLAVIGPSGSGKSTLLKLLSGFAVPDTGRI
LVDGKDVTHLPPHERALGVVFQSYALFPHMSLWRNVAYPLKVRGIPKTERQERARDALAR
VGLGDFAERAPTSLSGGQQQRVALARALVFSPRALLLDEPLSALDAALRHGMRDEIMRVQ
RKAGIATLHVTHDQEEALSMGDRVAVMSAGRLEQVAMPRDLYDRPASRRVAAFVGHANLW
EGMVVAPGLVSTRLGELVCDTAGFATGADVIALVRPEHVVPLLELPSGPRPNVFFGHMAE
DRFLGAVRRCDLEVGGGTVRIETSIRAAIAAVAVPPDAIRLLPPESPSPTRPAHTGNPS
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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