SitesBLAST
Comparing WP_083509566.1 NCBI__GCF_001541235.1:WP_083509566.1 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)
38% identity, 80% coverage: 36:350/392 of query aligns to 8:336/378 of P69874
- C26 (≠ N54) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F55) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V73) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C82) mutation to T: Loss of ATPase activity and transport.
- L60 (= L88) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I104) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V165) mutation to M: Loss of ATPase activity and transport.
- D172 (= D202) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ D295) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ R320) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
46% identity, 58% coverage: 50:275/392 of query aligns to 11:240/375 of 2d62A
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
39% identity, 77% coverage: 51:350/392 of query aligns to 8:321/358 of 8y5iA
1g291 Malk (see paper)
44% identity, 63% coverage: 50:295/392 of query aligns to 8:259/372 of 1g291
- binding magnesium ion: D69 (≠ G111), E71 (≠ S113), K72 (≠ S114), K79 (≠ E119), D80 (≠ K120)
- binding pyrophosphate 2-: S38 (= S80), G39 (= G81), C40 (= C82), G41 (= G83), K42 (= K84), T43 (= T85), T44 (= T86)
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 69% coverage: 56:327/392 of query aligns to 16:286/353 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)
40% identity, 69% coverage: 56:327/392 of query aligns to 16:286/353 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)
40% identity, 69% coverage: 56:327/392 of query aligns to 16:286/353 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)
40% identity, 69% coverage: 56:327/392 of query aligns to 16:286/353 of Q97UY8
- S142 (= S179) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G181) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E203) 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+).
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 63% coverage: 48:295/392 of query aligns to 9:247/353 of 1vciA
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 88% coverage: 44:386/392 of query aligns to 1:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F55), S37 (= S80), G38 (= G81), C39 (= C82), G40 (= G83), K41 (= K84), S42 (≠ T85), T43 (= T86), Q81 (= Q128), R128 (≠ E173), A132 (≠ V177), S134 (= S179), G136 (= G181), Q137 (= Q182), E158 (= E203), H191 (= H236)
- binding magnesium ion: S42 (≠ T85), Q81 (= Q128)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 88% coverage: 44:386/392 of query aligns to 1:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F55), G38 (= G81), C39 (= C82), G40 (= G83), K41 (= K84), S42 (≠ T85), T43 (= T86), R128 (≠ E173), S134 (= S179), Q137 (= Q182)
- binding beryllium trifluoride ion: S37 (= S80), G38 (= G81), K41 (= K84), Q81 (= Q128), S134 (= S179), G136 (= G181), H191 (= H236)
- binding magnesium ion: S42 (≠ T85), Q81 (= Q128)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 88% coverage: 44:386/392 of query aligns to 1:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F55), V17 (≠ A60), G38 (= G81), C39 (= C82), G40 (= G83), K41 (= K84), S42 (≠ T85), T43 (= T86), R128 (≠ E173), A132 (≠ V177), S134 (= S179), Q137 (= Q182)
- binding tetrafluoroaluminate ion: S37 (= S80), G38 (= G81), K41 (= K84), Q81 (= Q128), S134 (= S179), G135 (= G180), G136 (= G181), E158 (= E203), H191 (= H236)
- binding magnesium ion: S42 (≠ T85), Q81 (= Q128)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 88% coverage: 44:386/392 of query aligns to 1:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F55), V17 (≠ A60), G38 (= G81), C39 (= C82), G40 (= G83), K41 (= K84), S42 (≠ T85), T43 (= T86), R128 (≠ E173), A132 (≠ V177), S134 (= S179), Q137 (= Q182)
- binding magnesium ion: S42 (≠ T85), Q81 (= Q128)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 88% coverage: 44:386/392 of query aligns to 1:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 88% coverage: 44:386/392 of query aligns to 2:355/371 of P68187
- A85 (= A131) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K155) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V165) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (vs. gap) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E168) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G181) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D202) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L272) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ E283) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ H310) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (vs. gap) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T314) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G316) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G333) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ K339) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ G353) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G371) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ Q377) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F386) 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)
36% identity, 87% coverage: 46:386/392 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F55), S35 (= S80), G36 (= G81), C37 (= C82), G38 (= G83), K39 (= K84), S40 (≠ T85), T41 (= T86), R126 (≠ E173), A130 (≠ V177), S132 (= S179), G134 (= G181), Q135 (= Q182)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 88% coverage: 44:386/392 of query aligns to 2:353/369 of P19566
- L86 (= L132) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P204) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D209) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ K339) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
39% identity, 72% coverage: 43:324/392 of query aligns to 1:284/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F55), Q14 (≠ G56), T16 (= T58), V18 (≠ A60), S38 (= S80), G39 (= G81), C40 (= C82), G41 (= G83), K42 (= K84), T43 (= T85), T44 (= T86), R133 (≠ E173), E137 (≠ V177), S139 (= S179), G141 (= G181), Q142 (= Q182)
- binding calcium ion: T43 (= T85), Q86 (= Q128)
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
39% identity, 59% coverage: 50:281/392 of query aligns to 6:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F55), V16 (≠ A60), S36 (= S80), G37 (= G81), S38 (≠ C82), G39 (= G83), K40 (= K84), S41 (≠ T85), T42 (= T86), E162 (= E203), H194 (= H236)
- binding magnesium ion: S41 (≠ T85), E162 (= E203)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 60% coverage: 50:283/392 of query aligns to 31:268/382 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
Query Sequence
>WP_083509566.1 NCBI__GCF_001541235.1:WP_083509566.1
MSSSQTASHSDAPSVDVPDVARRSAAGAAAGDAGKGRAAAAFSACLTFEDVRRNFGTTQA
LAGVSLEIDRGEVVCLLGPSGCGKTTLLRIAAGIERPTGGRVLINGHEVAGPSSFVVPEK
RSVGLMFQDFALFPHLTIAGNVAFGLKSLPRAEAKREALAALKRVGLEHMADEYPHVLSG
GQQQRVALARALVPRPAVMLMDEPFSGLDVQLRDAMQEETLSLLRETGATAMVVTHNPEE
AMRIGDRIVVMRAGGLIQQGQAEALYHQPADLFVARLFSEINEVAYRVGADGKIDTPIGK
LSPPAGLQAHDAVTIGVRERDIRLSDNGEGLSGRVLDAKFLGDVVRLEVGIEGFDQPLKV
RVRESAGFRQGHDVRAQIDPERALVFAAELQK
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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