SitesBLAST
Comparing WP_012970350.1 NCBI__GCF_000025485.1:WP_012970350.1 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)
43% identity, 95% coverage: 19:378/378 of query aligns to 15:374/378 of P69874
- C26 (≠ Q30) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F49) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C58) mutation to T: Loss of ATPase activity and transport.
- L60 (= L64) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I80) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L139) mutation to M: Loss of ATPase activity and transport.
- D172 (= D176) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ I270) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E301) 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
45% identity, 84% coverage: 22:338/378 of query aligns to 7:334/375 of 2d62A
1g291 Malk (see paper)
45% identity, 85% coverage: 22:343/378 of query aligns to 4:336/372 of 1g291
- binding magnesium ion: D69 (= D87), E71 (vs. gap), K72 (vs. gap), K79 (≠ Y91), D80 (≠ S92), E292 (= E301), D293 (≠ K302)
- binding pyrophosphate 2-: S38 (= S56), G39 (= G57), C40 (= C58), G41 (= G59), K42 (= K60), T43 (≠ S61), T44 (= T62)
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)
43% identity, 81% coverage: 22:328/378 of query aligns to 4:309/369 of P19566
- L86 (= L104) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P178) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D183) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ A325) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 81% coverage: 22:329/378 of query aligns to 3:311/374 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)
42% identity, 81% coverage: 22:329/378 of query aligns to 3:311/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F31), S37 (= S56), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (= S61), T43 (= T62), Q81 (= Q100), R128 (= R147), A132 (≠ Q151), S134 (= S153), G136 (= G155), Q137 (= Q156), E158 (= E177), H191 (= H210)
- binding magnesium ion: S42 (= S61), Q81 (= Q100)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 81% coverage: 22:329/378 of query aligns to 3:311/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F31), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (= S61), T43 (= T62), R128 (= R147), S134 (= S153), Q137 (= Q156)
- binding beryllium trifluoride ion: S37 (= S56), G38 (= G57), K41 (= K60), Q81 (= Q100), S134 (= S153), G136 (= G155), H191 (= H210)
- binding magnesium ion: S42 (= S61), Q81 (= Q100)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 81% coverage: 22:329/378 of query aligns to 3:311/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F31), V17 (≠ A36), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (= S61), T43 (= T62), R128 (= R147), A132 (≠ Q151), S134 (= S153), Q137 (= Q156)
- binding tetrafluoroaluminate ion: S37 (= S56), G38 (= G57), K41 (= K60), Q81 (= Q100), S134 (= S153), G135 (= G154), G136 (= G155), E158 (= E177), H191 (= H210)
- binding magnesium ion: S42 (= S61), Q81 (= Q100)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 81% coverage: 22:329/378 of query aligns to 3:311/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F31), V17 (≠ A36), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (= S61), T43 (= T62), R128 (= R147), A132 (≠ Q151), S134 (= S153), Q137 (= Q156)
- binding magnesium ion: S42 (= S61), Q81 (= Q100)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 81% coverage: 22:329/378 of query aligns to 1:309/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F31), S35 (= S56), G36 (= G57), C37 (= C58), G38 (= G59), K39 (= K60), S40 (= S61), T41 (= T62), R126 (= R147), A130 (≠ Q151), S132 (= S153), G134 (= G155), Q135 (= Q156)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 81% coverage: 22:329/378 of query aligns to 4:312/371 of P68187
- A85 (= A103) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V132) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M135) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D137) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T142) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G155) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D176) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R246) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L257) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ G277) 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.
- S282 (≠ V295) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ A297) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G319) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A325) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 84% coverage: 22:338/378 of query aligns to 7:312/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
45% identity, 74% coverage: 24:303/378 of query aligns to 5:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F31), S38 (= S56), G39 (= G57), G41 (= G59), K42 (= K60), S43 (= S61), Q82 (= Q100), Q133 (= Q151), G136 (= G154), G137 (= G155), Q138 (= Q156), H192 (= H210)
- binding magnesium ion: S43 (= S61), Q82 (= Q100)
8hprD Lpqy-sugabc in state 4 (see paper)
45% identity, 74% coverage: 24:303/378 of query aligns to 5:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F31), S38 (= S56), C40 (= C58), G41 (= G59), K42 (= K60), S43 (= S61), T44 (= T62), Q82 (= Q100), R129 (= R147), Q133 (= Q151), S135 (= S153), G136 (= G154), G137 (= G155), Q159 (≠ E177), H192 (= H210)
- binding magnesium ion: S43 (= S61), Q82 (= Q100)
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)
44% identity, 75% coverage: 22:304/378 of query aligns to 4:288/393 of P9WQI3
- H193 (= H210) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 74% coverage: 24:303/378 of query aligns to 5:284/384 of 8hplC
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 94% coverage: 22:376/378 of query aligns to 2:347/348 of 3d31A
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 79% coverage: 30:329/378 of query aligns to 4:281/344 of 2awnC
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 81% coverage: 24:328/378 of query aligns to 6:308/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 81% coverage: 24:328/378 of query aligns to 6:308/353 of 1oxvA
Query Sequence
>WP_012970350.1 NCBI__GCF_000025485.1:WP_012970350.1
MPSPSDRRPLEPWQDPKAAPYVRIDRVTKQFGDVYAVDDVSLNIFQGEFFSLLGSSGCGK
STLLRLLAGLEYPTSGRIYIDGVDVTDVPPYSRPVNMMFQSYALFPHMTVEQNIEFGLKQ
DRLPRRERAERVNEMLDLLKITPLRKRRPDQLSGGQRQRVALARSLAKHPKLLLLDEPLG
ALDKRLRENTQFELVNLQERLGITFVTVTHDQEEAMTMSSRIAVMDAGQIMQIDTPTAIY
EFPNSRFVAEFIGSVNLFEGKIVEIQGDDILIEAQFGGLMRMRSLQPHPIGTPAVVAIRP
EKLRLCQTPSDDGVNRLQGVVEDIAYLGDVSIYRLRTGGGTLVEMTLTNIQPRTEQALTW
EQEVWVEWSPTSGVVLTD
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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