SitesBLAST
Comparing WP_011813608.1 NCBI__GCF_000015585.1:WP_011813608.1 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)
42% identity, 81% coverage: 5:308/375 of query aligns to 13:324/378 of P69874
- C26 (= C18) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y19) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ D286) 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
36% identity, 93% coverage: 10:356/375 of query aligns to 7:371/375 of 2d62A
1g291 Malk (see paper)
46% identity, 63% coverage: 10:247/375 of query aligns to 4:245/372 of 1g291
- binding magnesium ion: D69 (≠ V75), E71 (vs. gap), K72 (vs. gap), K79 (≠ E83), D80 (≠ K84)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50)
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
40% identity, 86% coverage: 10:332/375 of query aligns to 4:331/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y19), Q14 (≠ G20), T16 (= T22), V18 (≠ A24), S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50), R133 (= R137), E137 (= E141), S139 (= S143), G141 (= G145), Q142 (= Q146)
- binding calcium ion: T43 (= T49), Q86 (= Q92)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 75% coverage: 12:292/375 of query aligns to 6:285/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 75% coverage: 12:292/375 of query aligns to 6:285/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 75% coverage: 12:292/375 of query aligns to 6:285/353 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)
36% identity, 75% coverage: 12:292/375 of query aligns to 6:285/353 of Q97UY8
- S142 (= S143) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G145) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E167) 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+).
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 75% coverage: 10:291/375 of query aligns to 3:277/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 75% coverage: 10:291/375 of query aligns to 4:278/371 of P68187
- A85 (= A95) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R236) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (vs. gap) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ D280) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G291) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
36% identity, 75% coverage: 10:291/375 of query aligns to 3:277/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y19), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), Q81 (= Q92), R128 (= R137), A132 (≠ E141), S134 (= S143), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q92)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 75% coverage: 10:291/375 of query aligns to 3:277/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R137), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q92), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q92)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 75% coverage: 10:291/375 of query aligns to 3:277/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R137), A132 (≠ E141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q92), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q92)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 75% coverage: 10:291/375 of query aligns to 3:277/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R137), A132 (≠ E141), S134 (= S143), Q137 (= Q146)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q92)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 75% coverage: 10:291/375 of query aligns to 1:275/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y19), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (≠ T49), T41 (= T50), R126 (= R137), A130 (≠ E141), S132 (= S143), G134 (= G145), Q135 (= Q146)
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, 67% coverage: 10:262/375 of query aligns to 4:258/369 of P19566
- L86 (= L96) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) 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.
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)
35% identity, 92% coverage: 12:355/375 of query aligns to 6:383/393 of P9WQI3
- H193 (= H200) 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)
33% identity, 93% coverage: 10:356/375 of query aligns to 7:349/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 60% coverage: 24:247/375 of query aligns to 16:237/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 60% coverage: 24:247/375 of query aligns to 18:239/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (≠ T49), Q82 (= Q92), Q133 (≠ E141), G136 (= G144), G137 (= G145), Q138 (= Q146), H192 (= H200)
- binding magnesium ion: S43 (≠ T49), Q82 (= Q92)
Sites not aligning to the query:
Query Sequence
>WP_011813608.1 NCBI__GCF_000015585.1:WP_011813608.1
MVDYTASPLLELSNVHCCYGGTTAVYQLSLRVMPGQIACLLGPSGCGKTTTLRAIAGFEP
LCNGEIRVRGEPLSVPGYVMPPEKRRMGMVFQDYALFPHLNIYDNITFGLRKLSRRDRRR
RADELLELVDLQGYGERFPHELSGGQQQRVSLARAVAPQPQLVLLDEPFSNLDVELRERL
SREFHDIFRDQQITAILVTHDQHEAFAMADEIGLMRDGRIVQWDTPFNLYHEPADRFAAE
FIGQGSMISGTLIDGERIQTSLGTLRGSHGFPWPAGTRVDVLLRPDDVRMGEAPSGLYGR
VVKKAFKGAETLYTLRTPDGVELLALAPSHSDYDVGDDVGLTMDTEHLVAFPADGEVQAA
VEQPTRFPVRAVNVG
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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