SitesBLAST
Comparing WP_057507764.1 NCBI__GCF_001431535.1:WP_057507764.1 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 93% coverage: 26:376/378 of query aligns to 23:372/378 of P69874
- C26 (≠ E29) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F30) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I48) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S57) mutation to T: Loss of ATPase activity and transport.
- L60 (= L63) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L79) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V138) mutation to M: Loss of ATPase activity and transport.
- D172 (= D175) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ A278) 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
42% identity, 93% coverage: 26:376/378 of query aligns to 8:357/358 of 8y5iA
1g291 Malk (see paper)
43% identity, 87% coverage: 25:352/378 of query aligns to 8:344/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ Y90), D80 (≠ K91), E292 (= E301), D293 (≠ K302)
- binding pyrophosphate 2-: S38 (= S55), G39 (= G56), C40 (≠ S57), G41 (= G58), K42 (= K59), T43 (≠ S60), T44 (= T61)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
41% identity, 90% coverage: 28:368/378 of query aligns to 14:358/375 of 2d62A
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 90% coverage: 21:361/378 of query aligns to 4:342/369 of P19566
- L86 (= L103) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P177) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D182) 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)
36% identity, 90% coverage: 21:361/378 of query aligns to 3:343/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 90% coverage: 21:361/378 of query aligns to 1:341/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F30), S35 (= S55), G36 (= G56), C37 (≠ S57), G38 (= G58), K39 (= K59), S40 (= S60), T41 (= T61), R126 (= R146), A130 (≠ Q150), S132 (= S152), G134 (= G154), Q135 (= Q155)
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, 90% coverage: 21:361/378 of query aligns to 3:343/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F30), S37 (= S55), G38 (= G56), C39 (≠ S57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), Q81 (= Q99), R128 (= R146), A132 (≠ Q150), S134 (= S152), G136 (= G154), Q137 (= Q155), E158 (= E176), H191 (= H209)
- binding magnesium ion: S42 (= S60), Q81 (= Q99)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 90% coverage: 21:361/378 of query aligns to 3:343/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F30), G38 (= G56), C39 (≠ S57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (= R146), S134 (= S152), Q137 (= Q155)
- binding beryllium trifluoride ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q99), S134 (= S152), G136 (= G154), H191 (= H209)
- binding magnesium ion: S42 (= S60), Q81 (= Q99)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 90% coverage: 21:361/378 of query aligns to 3:343/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F30), V17 (≠ A35), G38 (= G56), C39 (≠ S57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (= R146), A132 (≠ Q150), S134 (= S152), Q137 (= Q155)
- binding tetrafluoroaluminate ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q99), S134 (= S152), G135 (= G153), G136 (= G154), E158 (= E176), H191 (= H209)
- binding magnesium ion: S42 (= S60), Q81 (= Q99)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 90% coverage: 21:361/378 of query aligns to 3:343/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F30), V17 (≠ A35), G38 (= G56), C39 (≠ S57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (= R146), A132 (≠ Q150), S134 (= S152), Q137 (= Q155)
- binding magnesium ion: S42 (= S60), Q81 (= Q99)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 90% coverage: 21:361/378 of query aligns to 4:344/371 of P68187
- A85 (= A102) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V131) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M134) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E136) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T141) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G154) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D175) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R245) 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 (≠ R272) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G283) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T287) 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.
- S322 (= S339) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G357) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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.
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)
48% identity, 59% coverage: 31:253/378 of query aligns to 15:237/393 of P9WQI3
- H193 (= H209) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 72% coverage: 35:306/378 of query aligns to 18:280/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S55), G39 (= G56), G41 (= G58), K42 (= K59), S43 (= S60), Q82 (= Q99), Q133 (= Q150), G136 (= G153), G137 (= G154), Q138 (= Q155), H192 (= H209)
- binding magnesium ion: S43 (= S60), Q82 (= Q99)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 72% coverage: 35:306/378 of query aligns to 16:278/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 72% coverage: 35:306/378 of query aligns to 18:280/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S55), C40 (≠ S57), G41 (= G58), K42 (= K59), S43 (= S60), T44 (= T61), Q82 (= Q99), R129 (= R146), Q133 (= Q150), S135 (= S152), G136 (= G153), G137 (= G154), Q159 (≠ E176), H192 (= H209)
- binding magnesium ion: S43 (= S60), Q82 (= Q99)
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)
39% identity, 84% coverage: 21:337/378 of query aligns to 7:311/353 of 1vciA
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 86% coverage: 38:361/378 of query aligns to 13:313/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 73% coverage: 34:308/378 of query aligns to 19:286/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 73% coverage: 34:308/378 of query aligns to 19:286/353 of 1oxvA
Sites not aligning to the query:
Query Sequence
>WP_057507764.1 NCBI__GCF_001431535.1:WP_057507764.1
MPAEALPEAAVIDTHGEPGYLSIRDLRKEFDGFVAVDDVNLDVRKGEIFALLGGSGSGKS
TLLRCLGGFETPTRGSIVLDGQPLVALPPYKRPVNMMFQSYALFPHMSVEQNIAFGLKQD
GLAGDAIRRRVGEMLELVHMTSLAKRRPHQLSGGQQQRVALARSLAKGPKLLLLDEPMGA
LDKKLRSQMQLELVNIIETSGVTCVMVTHDQEEAMTMATRIAVMDAGWIQQVGKPDEVYE
QPANRFVAGFIGSVNSFEGVIDEDLPEYVTVRSPAFPAPIYIGHGITCYEGQPVAFAVRP
EKIIIGKDEPEGHTNKAQGVIEDIAYFGSHSVYHVRLPSGAKVMANFANSQRWASDGLTW
GDEVWVHWRDNDGVVLTS
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