SitesBLAST
Comparing SMc02869 FitnessBrowser__Smeli:SMc02869 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
55% identity, 82% coverage: 17:306/352 of query aligns to 1:317/369 of P19566
- L86 (= L102) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D181) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E295) 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)
54% identity, 83% coverage: 18:310/352 of query aligns to 1:322/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
54% identity, 84% coverage: 17:310/352 of query aligns to 1:323/371 of P68187
- A85 (= A101) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V130) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A133) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E140) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D174) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L244) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F257) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G266) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T270) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G272) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G289) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E295) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ T309) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
54% identity, 83% coverage: 18:310/352 of query aligns to 1:322/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F29), S37 (= S54), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), Q81 (= Q98), R128 (= R145), A132 (≠ E149), S134 (= S151), G136 (= G153), Q137 (= Q154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S59), Q81 (= Q98)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
54% identity, 83% coverage: 18:310/352 of query aligns to 1:322/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F29), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (= R145), S134 (= S151), Q137 (= Q154)
- binding beryllium trifluoride ion: S37 (= S54), G38 (= G55), K41 (= K58), Q81 (= Q98), S134 (= S151), G136 (= G153), H191 (= H208)
- binding magnesium ion: S42 (= S59), Q81 (= Q98)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
54% identity, 83% coverage: 18:310/352 of query aligns to 1:322/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F29), V17 (= V34), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (= R145), A132 (≠ E149), S134 (= S151), Q137 (= Q154)
- binding tetrafluoroaluminate ion: S37 (= S54), G38 (= G55), K41 (= K58), Q81 (= Q98), S134 (= S151), G135 (= G152), G136 (= G153), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S59), Q81 (= Q98)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
54% identity, 83% coverage: 18:310/352 of query aligns to 1:322/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F29), V17 (= V34), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (= R145), A132 (≠ E149), S134 (= S151), Q137 (= Q154)
- binding magnesium ion: S42 (= S59), Q81 (= Q98)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
54% identity, 83% coverage: 20:310/352 of query aligns to 1:320/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F29), S35 (= S54), G36 (= G55), C37 (= C56), G38 (= G57), K39 (= K58), S40 (= S59), T41 (= T60), R126 (= R145), A130 (≠ E149), S132 (= S151), G134 (= G153), Q135 (= Q154)
8hplC Lpqy-sugabc in state 1 (see paper)
51% identity, 80% coverage: 35:317/352 of query aligns to 17:331/384 of 8hplC
Sites not aligning to the query:
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)
50% identity, 81% coverage: 32:317/352 of query aligns to 17:334/393 of P9WQI3
- H193 (= H208) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
45% identity, 93% coverage: 17:344/352 of query aligns to 4:369/375 of 2d62A
8hprC Lpqy-sugabc in state 4 (see paper)
52% identity, 78% coverage: 35:307/352 of query aligns to 19:323/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S54), G39 (= G55), G41 (= G57), K42 (= K58), S43 (= S59), Q82 (= Q98), Q133 (≠ E149), G136 (= G152), G137 (= G153), Q138 (= Q154), H192 (= H208)
- binding magnesium ion: S43 (= S59), Q82 (= Q98)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
52% identity, 77% coverage: 35:305/352 of query aligns to 19:321/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S54), C40 (= C56), G41 (= G57), K42 (= K58), S43 (= S59), T44 (= T60), Q82 (= Q98), R129 (= R145), Q133 (≠ E149), S135 (= S151), G136 (= G152), G137 (= G153), Q159 (≠ E175), H192 (= H208)
- binding magnesium ion: S43 (= S59), Q82 (= Q98)
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
50% identity, 83% coverage: 18:310/352 of query aligns to 1:292/344 of 2awnC
1g291 Malk (see paper)
57% identity, 70% coverage: 20:266/352 of query aligns to 4:256/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ A89), D80 (≠ K90)
- binding pyrophosphate 2-: S38 (= S54), G39 (= G55), C40 (= C56), G41 (= G57), K42 (= K58), T43 (≠ S59), T44 (= T60)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
46% identity, 82% coverage: 19:306/352 of query aligns to 6:310/353 of 1vciA
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
51% identity, 67% coverage: 20:255/352 of query aligns to 18:253/378 of P69874
- C26 (≠ A28) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F29) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F47) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C56) mutation to T: Loss of ATPase activity and transport.
- L60 (= L62) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I78) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L137) mutation to M: Loss of ATPase activity and transport.
- D172 (= D174) 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.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 83% coverage: 18:310/352 of query aligns to 1:280/330 of 2awnA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 22:291/352 of query aligns to 6:301/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 22:291/352 of query aligns to 6:301/353 of 1oxvA
Query Sequence
>SMc02869 FitnessBrowser__Smeli:SMc02869
MCAPASRSSFNPRGRHVGSLQLKTIRKAFGSHEVLKGIDLDVKDGEFVIFVGPSGCGKST
LLRTIAGLEDATSGSVQIDGVEVGHVAPAKRGIAMVFQSYALYPHLTVKDNMGLGLKQAG
VPKAEIEEKVAKAAGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPKLFLFDEPLSNL
DAALRVNTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVLNAGRIEQVGSPMELYNR
PANLFVAGFIGSPQMNFIEAAKLGDGEAKTIGIRPEHIGLSRESGDWKGKVIHVEHLGAD
TIIYIESETVGLLTVRLFGEHRYATDDIVHATPVIGSMHRFDADGRVIKSGQ
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