SitesBLAST
Comparing WP_061945612.1 NCBI__GCF_001584185.1:WP_061945612.1 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)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
48% identity, 68% coverage: 1:246/362 of query aligns to 4:245/375 of 2d62A
1g291 Malk (see paper)
50% identity, 62% coverage: 23:246/362 of query aligns to 19:242/372 of 1g291
- binding magnesium ion: D69 (= D73), E71 (≠ Q75), K72 (≠ R76), K79 (≠ E83), D80 (≠ E84)
- binding pyrophosphate 2-: S38 (= S42), G39 (= G43), C40 (≠ S44), G41 (= G45), K42 (= K46), T43 (= T47), T44 (= T48)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 76% coverage: 22:296/362 of query aligns to 32:305/378 of P69874
- F45 (≠ V35) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S44) mutation to T: Loss of ATPase activity and transport.
- L60 (= L50) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F72) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L131) mutation to M: Loss of ATPase activity and transport.
- D172 (= D168) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ V271) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (vs. gap) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
44% identity, 76% coverage: 22:296/362 of query aligns to 17:290/358 of 8y5iA
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)
45% identity, 70% coverage: 1:254/362 of query aligns to 1:247/393 of P9WQI3
- H193 (= H202) 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)
39% identity, 82% coverage: 1:298/362 of query aligns to 1:284/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 82% coverage: 1:298/362 of query aligns to 1:284/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 82% coverage: 1:298/362 of query aligns to 1:284/353 of 1oxuA
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
39% identity, 82% coverage: 1:298/362 of query aligns to 1:284/353 of Q97UY8
- S142 (= S145) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G147) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E169) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 19:245/374 of 2awnB
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 19:245/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S42), G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), Q81 (= Q92), R128 (= R139), A132 (≠ Q143), S134 (= S145), G136 (= G147), Q137 (= Q148), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q92)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 19:245/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R139), S134 (= S145), Q137 (= Q148)
- binding beryllium trifluoride ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q92), S134 (= S145), G136 (= G147), H191 (= H202)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q92)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 19:245/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R139), A132 (≠ Q143), S134 (= S145), Q137 (= Q148)
- binding tetrafluoroaluminate ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q92), S134 (= S145), G135 (= G146), G136 (= G147), E158 (= E169), H191 (= H202)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q92)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 19:245/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G43), C39 (≠ S44), G40 (= G45), K41 (= K46), S42 (≠ T47), T43 (= T48), R128 (= R139), A132 (≠ Q143), S134 (= S145), Q137 (= Q148)
- binding magnesium ion: S42 (≠ T47), Q81 (= Q92)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
49% identity, 64% coverage: 24:254/362 of query aligns to 20:246/371 of P68187
- A85 (= A95) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V127) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G129) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G134) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G147) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D168) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L238) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ R249) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
49% identity, 64% coverage: 24:254/362 of query aligns to 17:243/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S42), G36 (= G43), C37 (≠ S44), G38 (= G45), K39 (= K46), S40 (≠ T47), T41 (= T48), R126 (= R139), A130 (≠ Q143), S132 (= S145), G134 (= G147), Q135 (= Q148)
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)
48% identity, 64% coverage: 24:254/362 of query aligns to 20:246/369 of P19566
- L86 (= L96) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P170) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D175) 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.
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 67% coverage: 11:252/362 of query aligns to 5:242/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 64% coverage: 23:252/362 of query aligns to 19:244/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S42), C40 (≠ S44), G41 (= G45), K42 (= K46), S43 (≠ T47), T44 (= T48), Q82 (= Q92), R129 (= R139), Q133 (= Q143), S135 (= S145), G136 (= G146), G137 (= G147), Q159 (≠ E169), H192 (= H202)
- binding magnesium ion: S43 (≠ T47), Q82 (= Q92)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
47% identity, 64% coverage: 23:252/362 of query aligns to 19:244/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S42), G39 (= G43), G41 (= G45), K42 (= K46), S43 (≠ T47), Q82 (= Q92), Q133 (= Q143), G136 (= G146), G137 (= G147), Q138 (= Q148), H192 (= H202)
- binding magnesium ion: S43 (≠ T47), Q82 (= Q92)
Sites not aligning to the query:
Query Sequence
>WP_061945612.1 NCBI__GCF_001584185.1:WP_061945612.1
MSELSVNNLHLDYGSGASANPILKGVSMELQRGEVVALLGPSGSGKTTLLRAVAGLESPK
SGSIQIGERIMFDGQRKLEIPAEERNLGLVFQSYALWPHKTVSDNVGYGLKLRKMSSSDI
ATRVKTVLGQLGLGHLGDRFPHQLSGGQQQRVAIARALVYNPPVILLDEPLSNLDAKLRE
EARAFLRELIVRLGLSALMVTHDQAEAMAISDRILLLNNGKIEQQGTPQSMYETPDTLFT
AEFMGSNNRLPAKLLQRDGARVLLQVEGGNVTATLRGAAGNDAKDAIAIIRVEQVNISDV
PVENSIKLPLATCMYLGDRWECVFRNSTESGADSSVLRAYARQRLAPGEYWLQLPQDALW
AF
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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