SitesBLAST
Comparing WP_028490400.1 NCBI__GCF_000621325.1:WP_028490400.1 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)
39% identity, 87% coverage: 13:318/350 of query aligns to 27:341/378 of P69874
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V123) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ D280) 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
38% identity, 90% coverage: 13:327/350 of query aligns to 12:335/358 of 8y5iA
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
46% identity, 68% coverage: 1:237/350 of query aligns to 4:244/375 of 2d62A
1g291 Malk (see paper)
45% identity, 68% coverage: 1:237/350 of query aligns to 1:241/372 of 1g291
- binding magnesium ion: D69 (= D69), E71 (vs. gap), K72 (≠ H70), K79 (≠ E77), D80 (≠ K78)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)
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)
41% identity, 78% coverage: 1:274/350 of query aligns to 1:269/369 of P19566
- L86 (= L90) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 75% coverage: 1:264/350 of query aligns to 1:259/371 of P68187
- A85 (= A89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V123) 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 (≠ A230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ V246) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
41% identity, 75% coverage: 2:264/350 of query aligns to 1:258/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q86), R128 (= R131), A132 (≠ E135), S134 (= S137), G136 (= G139), Q137 (= Q140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q86)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 75% coverage: 2:264/350 of query aligns to 1:258/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R131), S134 (= S137), Q137 (= Q140)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q86), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q86)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 75% coverage: 2:264/350 of query aligns to 1:258/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R131), A132 (≠ E135), S134 (= S137), Q137 (= Q140)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q86), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q86)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 75% coverage: 2:264/350 of query aligns to 1:258/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R131), A132 (≠ E135), S134 (= S137), Q137 (= Q140)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q86)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 75% coverage: 2:264/350 of query aligns to 1:258/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 75% coverage: 4:264/350 of query aligns to 1:256/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (= R131), A130 (≠ E135), S132 (= S137), G134 (= G139), Q135 (= Q140)
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
41% identity, 81% coverage: 13:296/350 of query aligns to 13:293/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y13), Q14 (≠ S14), T16 (≠ N16), V18 (= V18), S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44), R133 (= R131), E137 (= E135), S139 (= S137), G141 (= G139), Q142 (= Q140)
- binding calcium ion: T43 (= T43), Q86 (= Q86)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 82% coverage: 1:287/350 of query aligns to 1:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 82% coverage: 1:287/350 of query aligns to 1:286/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 82% coverage: 1:287/350 of query aligns to 1:286/353 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)
38% identity, 82% coverage: 1:287/350 of query aligns to 1:286/353 of Q97UY8
- S142 (= S137) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G139) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E161) 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+).
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)
40% identity, 68% coverage: 1:237/350 of query aligns to 1:236/393 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 68% coverage: 1:237/350 of query aligns to 4:230/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 67% coverage: 2:237/350 of query aligns to 1:235/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (≠ T43), Q82 (= Q86), Q133 (≠ E135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q86)
Query Sequence
>WP_028490400.1 NCBI__GCF_000621325.1:WP_028490400.1
MSKLTLQNIHIRYSNNAVVHAVSLTVEDGQIGCLLGPSGCGKTTLLRAIAGFESVTQGSI
TLNGQLISDHNTHLPPEKRTIGMVFQDYALFPHLNIADNITFGIRKQSSQDKARRVAELL
ELVNLPGYAKRYPHELSGGQQQRIALARALAPRPRLLLLDEPFGSQDVELREMLAREVRD
ILKREGMTAILVTHDQHEAFAMADEIGVLQQGRLQQWDTGYNLYHKPANAFVAGFIGQGV
LLPGIVLNHNTVATALGNVHGDVPESCQPECPVSVLIRPDDLRLVADSPHPATVISRGFR
GAEYLYGLALNDGSQLLALTPSHQAHPIGASVCIELDLQHLVILPTLTSY
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