SitesBLAST
Comparing WP_086509734.1 NCBI__GCF_002151265.1:WP_086509734.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
43% identity, 74% coverage: 6:236/313 of query aligns to 31:263/382 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)
43% identity, 74% coverage: 6:236/313 of query aligns to 31:263/382 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)
44% identity, 73% coverage: 6:233/313 of query aligns to 31:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ E14), S61 (= S36), G62 (= G37), G64 (= G39), K65 (= K40), S66 (= S41), T67 (= T42), Q111 (= Q82), K161 (≠ R134), Q162 (= Q135), S164 (= S137), G166 (= G139), M167 (≠ Q140), Q188 (≠ E161), H221 (= H194)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 82% coverage: 2:258/313 of query aligns to 7:270/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 77% coverage: 1:240/313 of query aligns to 17:252/378 of P69874
- C26 (≠ R10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C38) mutation to T: Loss of ATPase activity and transport.
- L60 (= L44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L60) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) 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.
1g291 Malk (see paper)
41% identity, 83% coverage: 2:260/313 of query aligns to 4:269/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ V65), K72 (≠ R66), K79 (≠ L73), D80 (≠ R74)
- binding pyrophosphate 2-: S38 (= S36), G39 (= G37), C40 (= C38), G41 (= G39), K42 (= K40), T43 (≠ S41), T44 (= T42)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
44% identity, 74% coverage: 7:238/313 of query aligns to 8:236/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S36), C40 (= C38), G41 (= G39), K42 (= K40), S43 (= S41), T44 (= T42), Q82 (= Q82), R129 (≠ K131), Q133 (= Q135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (= S41), Q82 (= Q82)
8hprC Lpqy-sugabc in state 4 (see paper)
44% identity, 74% coverage: 7:238/313 of query aligns to 8:236/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S36), G39 (= G37), G41 (= G39), K42 (= K40), S43 (= S41), Q82 (= Q82), Q133 (= Q135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (= S41), Q82 (= Q82)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
40% identity, 79% coverage: 2:248/313 of query aligns to 7:241/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 74% coverage: 7:237/313 of query aligns to 8:233/384 of 8hplC
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 75% coverage: 2:237/313 of query aligns to 3:234/374 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)
39% identity, 75% coverage: 2:237/313 of query aligns to 3:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F11), S37 (= S36), G38 (= G37), C39 (= C38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), Q81 (= Q82), R128 (≠ K131), A132 (≠ Q135), S134 (= S137), G136 (= G139), Q137 (= Q140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (= S41), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 75% coverage: 2:237/313 of query aligns to 3:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F11), G38 (= G37), C39 (= C38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), R128 (≠ K131), S134 (= S137), Q137 (= Q140)
- binding beryllium trifluoride ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (= S41), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 75% coverage: 2:237/313 of query aligns to 3:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ A16), G38 (= G37), C39 (= C38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), R128 (≠ K131), A132 (≠ Q135), S134 (= S137), Q137 (= Q140)
- binding tetrafluoroaluminate ion: S37 (= S36), G38 (= G37), K41 (= K40), Q81 (= Q82), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (= S41), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 75% coverage: 2:237/313 of query aligns to 3:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ A16), G38 (= G37), C39 (= C38), G40 (= G39), K41 (= K40), S42 (= S41), T43 (= T42), R128 (≠ K131), A132 (≠ Q135), S134 (= S137), Q137 (= Q140)
- binding magnesium ion: S42 (= S41), Q81 (= Q82)
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, 85% coverage: 2:266/313 of query aligns to 4:264/393 of P9WQI3
- H193 (= H194) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 75% coverage: 2:237/313 of query aligns to 4:235/371 of P68187
- A85 (≠ G85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A126) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G139) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D160) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
39% identity, 75% coverage: 2:237/313 of query aligns to 1:232/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F11), S35 (= S36), G36 (= G37), C37 (= C38), G38 (= G39), K39 (= K40), S40 (= S41), T41 (= T42), R126 (≠ K131), A130 (≠ Q135), S132 (= S137), G134 (= G139), Q135 (= Q140)
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
43% identity, 75% coverage: 1:236/313 of query aligns to 2:236/241 of 4u00A
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, 75% coverage: 2:237/313 of query aligns to 4:235/369 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 (= P162) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D167) 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.
Query Sequence
>WP_086509734.1 NCBI__GCF_002151265.1:WP_086509734.1
MIELFDVTKRFGDETAVDGISLRVEKGELCALVGTSGCGKSTTLRMINRLIEHDGGEIHL
DGQPVRSFDEVALRRRIGYVIQSTGLFPHWTVARNIGLVPRLLKWPKGKVRDRVEELMQL
LGLPVAEFADKYPRQLSGGQAQRVGVARALAADPDILLMDEPFGALDPITRATLQDELRV
LQARLHKTVVFVTHDMDEALALADRLVVMHQGRIVQQGSPVELLREPANPFVESLLGGMD
RGLKEAALIQVSEHMLPLGPRLLASERIPYGASLSQALSVMLWHRVDRLTVVDEEDIPIG
ELSLRRLLGAKVP
Or try a new SitesBLAST search
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