SitesBLAST
Comparing WP_011385004.1 NCBI__GCF_000009985.1:WP_011385004.1 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)
47% identity, 85% coverage: 21:344/379 of query aligns to 16:339/378 of P69874
- C26 (≠ R31) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F32) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F50) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C59) mutation to T: Loss of ATPase activity and transport.
- L60 (= L65) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I81) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V140) mutation to M: Loss of ATPase activity and transport.
- D172 (= D177) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ H279) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E302) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 87% coverage: 23:350/379 of query aligns to 4:330/369 of P19566
- L86 (= L105) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P179) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D184) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ A326) 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)
40% identity, 87% coverage: 23:350/379 of query aligns to 3:331/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 87% coverage: 23:350/379 of query aligns to 4:332/371 of P68187
- A85 (= A104) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A125) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V133) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A136) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E138) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G143) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G156) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D177) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R247) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ Q260) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ L281) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G292) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T296) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ M298) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G320) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A326) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S340) 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)
40% identity, 87% coverage: 23:350/379 of query aligns to 3:331/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F32), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), Q81 (= Q101), R128 (= R148), A132 (≠ Q152), S134 (= S154), G136 (= G156), Q137 (= Q157), E158 (= E178), H191 (= H211)
- binding magnesium ion: S42 (≠ T62), Q81 (= Q101)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 87% coverage: 23:350/379 of query aligns to 3:331/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F32), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), R128 (= R148), S134 (= S154), Q137 (= Q157)
- binding beryllium trifluoride ion: S37 (= S57), G38 (= G58), K41 (= K61), Q81 (= Q101), S134 (= S154), G136 (= G156), H191 (= H211)
- binding magnesium ion: S42 (≠ T62), Q81 (= Q101)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 87% coverage: 23:350/379 of query aligns to 3:331/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (≠ A37), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), R128 (= R148), A132 (≠ Q152), S134 (= S154), Q137 (= Q157)
- binding tetrafluoroaluminate ion: S37 (= S57), G38 (= G58), K41 (= K61), Q81 (= Q101), S134 (= S154), G135 (= G155), G136 (= G156), E158 (= E178), H191 (= H211)
- binding magnesium ion: S42 (≠ T62), Q81 (= Q101)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 87% coverage: 23:350/379 of query aligns to 3:331/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (≠ A37), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), R128 (= R148), A132 (≠ Q152), S134 (= S154), Q137 (= Q157)
- binding magnesium ion: S42 (≠ T62), Q81 (= Q101)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 87% coverage: 23:350/379 of query aligns to 1:329/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F32), S35 (= S57), G36 (= G58), C37 (= C59), G38 (= G60), K39 (= K61), S40 (≠ T62), T41 (= T63), R126 (= R148), A130 (≠ Q152), S132 (= S154), G134 (= G156), Q135 (= Q157)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
45% identity, 83% coverage: 23:337/379 of query aligns to 7:332/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
51% identity, 65% coverage: 23:270/379 of query aligns to 7:246/353 of 1vciA
1g291 Malk (see paper)
42% identity, 87% coverage: 23:350/379 of query aligns to 4:342/372 of 1g291
- binding magnesium ion: D69 (≠ E88), E71 (vs. gap), K72 (vs. gap), K79 (≠ Y92), D80 (≠ E93), E292 (= E302), D293 (≠ K303)
- binding pyrophosphate 2-: S38 (= S57), G39 (= G58), C40 (= C59), G41 (= G60), K42 (= K61), T43 (= T62), T44 (= T63)
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)
44% identity, 74% coverage: 23:304/379 of query aligns to 4:287/393 of P9WQI3
- H193 (= H211) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 85% coverage: 29:350/379 of query aligns to 2:301/344 of 2awnC
8hprD Lpqy-sugabc in state 4 (see paper)
46% identity, 62% coverage: 23:258/379 of query aligns to 3:239/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F32), S38 (= S57), C40 (= C59), G41 (= G60), K42 (= K61), S43 (≠ T62), T44 (= T63), Q82 (= Q101), R129 (= R148), Q133 (= Q152), S135 (= S154), G136 (= G155), G137 (= G156), Q159 (≠ E178), H192 (= H211)
- binding magnesium ion: S43 (≠ T62), Q82 (= Q101)
8hprC Lpqy-sugabc in state 4 (see paper)
46% identity, 62% coverage: 23:258/379 of query aligns to 3:239/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F32), S38 (= S57), G39 (= G58), G41 (= G60), K42 (= K61), S43 (≠ T62), Q82 (= Q101), Q133 (= Q152), G136 (= G155), G137 (= G156), Q138 (= Q157), H192 (= H211)
- binding magnesium ion: S43 (≠ T62), Q82 (= Q101)
8hplC Lpqy-sugabc in state 1 (see paper)
48% identity, 59% coverage: 37:258/379 of query aligns to 16:237/384 of 8hplC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 89% coverage: 22:360/379 of query aligns to 1:330/348 of 3d31A
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 23:329/379 of query aligns to 4:308/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 23:329/379 of query aligns to 4:308/353 of 1oxvA
Query Sequence
>WP_011385004.1 NCBI__GCF_000009985.1:WP_011385004.1
MAQAAVKREVTAPWNDPQAVPLIRFEGISKRFGDFTAVEHVDLAIHKGEFFSLLGASGCG
KTTLLRMLAGFEIPTTGRILIDGQDVTEVPPYERPVNMMFQSYALFPHMSVADNIAFGLK
QDGLAKPVIKDKVAAALELVQMGRFSGRKPHQLSGGQRQRVALARCLAKEPKVVLLDEPL
AALDKKLREATQLELVNIQDRVGITFVMVTHDQGEAMTMSSRIGVMNAGCIEQVGSPVDI
YEYPGTRFVADFIGAANMFQGSVRGGEGALAIACPELEHDLSVTEAGAVAAGTPVTVMVR
PEKVMIARDKPASGLNWAEGVVSDIAYLGDVSIYHVRLASGRKIQALRTNLHHGEESRLT
WEDPVFLAWHPADSLVLTK
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