SitesBLAST
Comparing WP_012590119.1 NCBI__GCF_000021745.1:WP_012590119.1 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)
48% identity, 67% coverage: 8:251/363 of query aligns to 23:260/378 of P69874
- C26 (≠ S11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ G41) mutation to T: Loss of ATPase activity and transport.
- L60 (= L47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) 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)
46% identity, 72% coverage: 3:263/363 of query aligns to 4:267/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (= E70), K72 (= K71), K79 (≠ Q74), D80 (≠ E75)
- binding pyrophosphate 2-: S38 (= S39), G39 (= G40), C40 (≠ G41), G41 (= G42), K42 (= K43), T43 (= T44), T44 (= T45)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 78% coverage: 8:289/363 of query aligns to 8:278/384 of 8hplC
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 66% coverage: 2:240/363 of query aligns to 6:244/375 of 2d62A
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 8:289/363 of query aligns to 8:280/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F12), S38 (= S39), C40 (≠ G41), G41 (= G42), K42 (= K43), S43 (≠ T44), T44 (= T45), Q82 (= Q83), R129 (= R134), Q133 (= Q138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (≠ T44), Q82 (= Q83)
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 8:289/363 of query aligns to 8:280/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F12), S38 (= S39), G39 (= G40), G41 (= G42), K42 (= K43), S43 (≠ T44), Q82 (= Q83), Q133 (= Q138), G136 (= G141), G137 (= G142), Q138 (= Q143), H192 (= H197)
- binding magnesium ion: S43 (≠ T44), Q82 (= Q83)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 87% coverage: 3:317/363 of query aligns to 4:321/371 of P68187
- A85 (= A86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P233) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ S246) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ S272) 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 (vs. gap) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ F280) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A298) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ R304) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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)
38% identity, 87% coverage: 3:317/363 of query aligns to 3:320/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F12), S37 (= S39), G38 (= G40), C39 (≠ G41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), Q81 (= Q83), R128 (= R134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 87% coverage: 3:317/363 of query aligns to 3:320/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F12), G38 (= G40), C39 (≠ G41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R134), S134 (= S140), Q137 (= Q143)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 87% coverage: 3:317/363 of query aligns to 3:320/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F12), V17 (≠ R17), G38 (= G40), C39 (≠ G41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding tetrafluoroaluminate ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q83), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 87% coverage: 3:317/363 of query aligns to 3:320/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F12), V17 (≠ R17), G38 (= G40), C39 (≠ G41), G40 (= G42), K41 (= K43), S42 (≠ T44), T43 (= T45), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding magnesium ion: S42 (≠ T44), Q81 (= Q83)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 87% coverage: 3:317/363 of query aligns to 3:320/374 of 2awnB
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, 81% coverage: 23:317/363 of query aligns to 22:319/369 of P19566
- L86 (= L87) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ R304) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 87% coverage: 3:317/363 of query aligns to 1:318/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F12), S35 (= S39), G36 (= G40), C37 (≠ G41), G38 (= G42), K39 (= K43), S40 (≠ T44), T41 (= T45), R126 (= R134), A130 (≠ Q138), S132 (= S140), G134 (= G142), Q135 (= Q143)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 79% coverage: 1:288/363 of query aligns to 5:280/353 of 1vciA
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)
43% identity, 71% coverage: 2:257/363 of query aligns to 3:262/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 80% coverage: 1:291/363 of query aligns to 2:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 80% coverage: 1:291/363 of query aligns to 2:286/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 80% coverage: 1:291/363 of query aligns to 2:286/353 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)
37% identity, 80% coverage: 1:291/363 of query aligns to 2:286/353 of Q97UY8
- S142 (= S140) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G142) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E164) 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+).
Query Sequence
>WP_012590119.1 NCBI__GCF_000021745.1:WP_012590119.1
MQIRAQDIVKSFPGARRSALEGVSLNVGSGELVALLGPSGGGKTTLLRIIAGLDLPDSGK
VFFGDEDASEKSVQERRVGFVFQNYALFKHLTVEDNIGFGLDVRDRAQRPPKAEIRRRAL
ELLDLVQLKGLEKRRPSQLSGGQRQRVALARALAVEPRVLLLDEPFGALDAKVRRELRSW
LREFHARTGHTTIFVTHDQDEALELADRVAVLNGGHIEQIGTPDEIYDHPATPFVNGFIG
ESTAISAHLREGQVFLGDHRLELPKANRLATSSDGEGQLFVRPQDILIGEEGPGALQAEV
LSVRRSGPTRRAEIALPYEQSSIEVDTPASVTFQPGERVPVRFLRGTFFLKADAAGAAAH
ARS
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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