SitesBLAST
Comparing WP_011911319.1 NCBI__GCF_000013785.1:WP_011911319.1 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, 78% coverage: 10:308/383 of query aligns to 5:301/378 of P69874
- C26 (≠ K31) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F32) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I50) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S59) mutation to T: Loss of ATPase activity and transport.
- L60 (= L65) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L81) 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 (≠ N280) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E304) 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)
48% identity, 75% coverage: 22:308/383 of query aligns to 2:286/358 of 8y5iA
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
39% identity, 91% coverage: 23:372/383 of query aligns to 7:358/375 of 2d62A
1g291 Malk (see paper)
41% identity, 87% coverage: 28:361/383 of query aligns to 9:346/372 of 1g291
- binding magnesium ion: D69 (= D88), E71 (vs. gap), K72 (vs. gap), K79 (≠ Y92), D80 (≠ E93), E292 (= E304), D293 (≠ K305)
- binding pyrophosphate 2-: S38 (= S57), G39 (= G58), C40 (≠ S59), G41 (= G60), K42 (= K61), T43 (≠ S62), T44 (= T63)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 84% coverage: 23:345/383 of query aligns to 3:321/374 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)
39% identity, 84% coverage: 23:345/383 of query aligns to 3:321/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F32), S37 (= S57), G38 (= G58), C39 (≠ S59), G40 (= G60), K41 (= K61), S42 (= S62), T43 (= T63), Q81 (= Q101), R128 (= R148), A132 (≠ Q152), S134 (= S154), G136 (= G156), Q137 (= Q157), E158 (= E178), H191 (= H211)
- binding magnesium ion: S42 (= S62), Q81 (= Q101)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 84% coverage: 23:345/383 of query aligns to 3:321/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F32), G38 (= G58), C39 (≠ S59), G40 (= G60), K41 (= K61), S42 (= S62), 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 (= S62), Q81 (= Q101)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 84% coverage: 23:345/383 of query aligns to 3:321/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (≠ A37), G38 (= G58), C39 (≠ S59), G40 (= G60), K41 (= K61), S42 (= S62), 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 (= S62), Q81 (= Q101)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 84% coverage: 23:345/383 of query aligns to 3:321/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (≠ A37), G38 (= G58), C39 (≠ S59), G40 (= G60), K41 (= K61), S42 (= S62), T43 (= T63), R128 (= R148), A132 (≠ Q152), S134 (= S154), Q137 (= Q157)
- binding magnesium ion: S42 (= S62), Q81 (= Q101)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 84% coverage: 23:345/383 of query aligns to 4:322/371 of P68187
- A85 (= A104) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P125) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V133) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M136) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G138) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T143) 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 (≠ L258) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ G285) 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 (≠ T298) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ A300) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G325) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A331) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S345) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 84% coverage: 23:345/383 of query aligns to 1:319/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F32), S35 (= S57), G36 (= G58), C37 (≠ S59), G38 (= G60), K39 (= K61), S40 (= S62), T41 (= T63), R126 (= R148), A130 (≠ Q152), S132 (= S154), G134 (= G156), Q135 (= Q157)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
46% identity, 61% coverage: 23:255/383 of query aligns to 4:236/369 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.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
8hprC Lpqy-sugabc in state 4 (see paper)
47% identity, 61% coverage: 25:259/383 of query aligns to 5:242/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F32), S38 (= S57), G39 (= G58), G41 (= G60), K42 (= K61), S43 (= S62), Q82 (= Q101), Q133 (= Q152), G136 (= G155), G137 (= G156), Q138 (= Q157), H192 (= H211)
- binding magnesium ion: S43 (= S62), Q82 (= Q101)
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 61% coverage: 25:259/383 of query aligns to 5:242/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F32), S38 (= S57), C40 (≠ S59), G41 (= G60), K42 (= K61), S43 (= S62), T44 (= T63), Q82 (= Q101), R129 (= R148), Q133 (= Q152), S135 (= S154), G136 (= G155), G137 (= G156), Q159 (≠ E178), H192 (= H211)
- binding magnesium ion: S43 (= S62), Q82 (= Q101)
8hplC Lpqy-sugabc in state 1 (see paper)
47% identity, 61% coverage: 25:259/383 of query aligns to 5:240/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 63% coverage: 19:260/383 of query aligns to 3:238/353 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)
46% identity, 62% coverage: 25:263/383 of query aligns to 6:247/393 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 82% coverage: 21:335/383 of query aligns to 5:309/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 82% coverage: 21:335/383 of query aligns to 5:309/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 82% coverage: 21:335/383 of query aligns to 5:309/353 of 1oxuA
Query Sequence
>WP_011911319.1 NCBI__GCF_000013785.1:WP_011911319.1
MAVASSAYKKALSGESKNKQVLLKIDRVTKKFDETVAVDDVSLSIHQGEIFALLGGSGSG
KSTLLRMLAGFERPTEGRIFLDGQDITDMPPYERPINMMFQSYALFPHMTVEQNIAFGLK
QDGLPKAEIEERVKEMLGLVQMTQYAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM
GALDKKLRSQMQLELVQIIERVGVTCVMVTHDQEEAMTMAERIAIMHQGWIAQVGSPMDI
YETPASRLVCEFIGNVNLFEGELVEDMGDHAIIASPGLDNPIYVGHGISTRAQDKHITYA
LRPEKLLIGTELPELERPGYNWAKGVVHDIAYLGGHSVYYIKLPSGGVLQAFMANAERHV
KLPTWEEEVYVYWWDDSGVVLQA
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