SitesBLAST

Comparing WP_010441963.1 NCBI__GCF_000192475.1:WP_010441963.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

7ahhC Opua inhibited inward-facing, sbd docked (see paper)
49% identity, 78% coverage: 9:280/349 of query aligns to 3:269/382 of 7ahhC

• binding phosphoaminophosphonic acid-adenylate ester: F12 (= F18), T39 (≠ I50), V40 (≠ P51), G41 (≠ A52), G62 (= G73), G64 (= G75), K65 (= K76), D187 (= D198), E188 (= E199)

Sites not aligning to the query:

• binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298

7aheC Opua inhibited inward facing (see paper)
49% identity, 78% coverage: 9:280/349 of query aligns to 3:269/382 of 7aheC

Sites not aligning to the query:

• binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298

7ahdC Opua (e190q) occluded (see paper)
49% identity, 75% coverage: 9:271/349 of query aligns to 3:260/260 of 7ahdC

• binding adenosine-5'-triphosphate: F12 (= F18), T39 (≠ I50), S61 (= S72), G62 (= G73), G64 (= G75), K65 (= K76), S66 (= S77), T67 (= T78), Q111 (= Q122), K161 (≠ R172), Q162 (= Q173), S164 (= S175), G166 (= G177), M167 (≠ Q178), Q188 (≠ E199), H221 (= H232)

2d62A Crystal structure of multiple sugar binding transport atp-binding protein
38% identity, 66% coverage: 45:273/349 of query aligns to 14:242/375 of 2d62A

• binding pyrophosphate 2-: G42 (= G73), C43 (≠ S74), G44 (= G75), K45 (= K76), T46 (≠ S77), T47 (= T78)

4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
41% identity, 66% coverage: 45:273/349 of query aligns to 9:235/240 of 4ymuJ

• binding adenosine-5'-triphosphate: F11 (≠ H47), V16 (≠ A52), S36 (= S72), G37 (= G73), S38 (= S74), G39 (= G75), K40 (= K76), S41 (= S77), T42 (= T78), E162 (= E199), H194 (= H232)
• binding magnesium ion: S41 (= S77), E162 (= E199)

1g291 Malk (see paper)
36% identity, 65% coverage: 47:273/349 of query aligns to 13:239/372 of 1g291

• binding magnesium ion: D69 (≠ G103), E71 (≠ S105), K72 (= K106), K79 (≠ R113), D80 (≠ R114)
• binding pyrophosphate 2-: S38 (= S72), G39 (= G73), C40 (≠ S74), G41 (= G75), K42 (= K76), T43 (≠ S77), T44 (= T78)

Sites not aligning to the query:

• binding magnesium ion: 292, 293, 359

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 61% coverage: 60:273/349 of query aligns to 40:247/378 of P69874

• F45 (≠ L65) mutation to L: Lower ATPase activity and transport efficiency.
• C54 (≠ S74) mutation to T: Loss of ATPase activity and transport.
• L60 (≠ I80) mutation to F: Lower ATPase activity and transport efficiency.
• L76 (≠ V96) mutation to P: Lower ATPase activity and transport efficiency.
• V135 (= V161) mutation to M: Loss of ATPase activity and transport.
• D172 (= D198) mutation to N: 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.
• 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.

8hplC Lpqy-sugabc in state 1 (see paper)
39% identity, 64% coverage: 52:273/349 of query aligns to 16:231/384 of 8hplC

• binding adenosine-5'-triphosphate: G37 (= G73), C38 (≠ S74), G39 (= G75), K40 (= K76), S41 (= S77), T42 (= T78)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 12

8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 64% coverage: 52:273/349 of query aligns to 18:233/363 of 8hprC

• binding adenosine-5'-triphosphate: S38 (= S72), G39 (= G73), G41 (= G75), K42 (= K76), S43 (= S77), Q82 (= Q122), Q133 (= Q173), G136 (= G176), G137 (= G177), Q138 (= Q178), H192 (= H232)
• binding magnesium ion: S43 (= S77), Q82 (= Q122)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 12

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 64% coverage: 50:273/349 of query aligns to 18:240/343 of P30750

• 40:46 (vs. 72:78, 86% identical) binding ATP
• E166 (= E199) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

• 278:283 binding L-methionine
• 295 N→A: Reduces the binding of L-methionine to undetectable levels.
• 295:296 binding L-methionine

8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 64% coverage: 52:273/349 of query aligns to 18:233/362 of 8hprD

• binding adenosine-5'-triphosphate: S38 (= S72), C40 (≠ S74), G41 (= G75), K42 (= K76), S43 (= S77), T44 (= T78), Q82 (= Q122), R129 (≠ S169), Q133 (= Q173), S135 (= S175), G136 (= G176), G137 (= G177), Q159 (≠ E199), H192 (= H232)
• binding magnesium ion: S43 (= S77), Q82 (= Q122)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 12

8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
40% identity, 62% coverage: 60:277/349 of query aligns to 25:236/358 of 8y5iA

• binding adenosine-5'-triphosphate: G38 (= G73), K41 (= K76), T42 (≠ S77), T43 (= T78), R128 (≠ S169), Q132 (= Q173), S134 (= S175)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 12, 15

2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 65% coverage: 48:273/349 of query aligns to 13:232/374 of 2awnB

• binding adenosine-5'-diphosphate: V17 (≠ A52), S37 (= S72), G38 (= G73), G40 (= G75), K41 (= K76), S42 (= S77), T43 (= T78)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 65% coverage: 48:273/349 of query aligns to 13:232/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: S37 (= S72), G38 (= G73), C39 (≠ S74), G40 (= G75), K41 (= K76), S42 (= S77), T43 (= T78), Q81 (= Q122), R128 (≠ S169), A132 (≠ Q173), S134 (= S175), G136 (= G177), Q137 (= Q178), E158 (= E199), H191 (= H232)
• binding magnesium ion: S42 (= S77), Q81 (= Q122)

Sites not aligning to the query:

• binding phosphoaminophosphonic acid-adenylate ester: 12

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 65% coverage: 48:273/349 of query aligns to 13:232/371 of 3puxA

• binding adenosine-5'-diphosphate: G38 (= G73), C39 (≠ S74), G40 (= G75), K41 (= K76), S42 (= S77), T43 (= T78), R128 (≠ S169), S134 (= S175), Q137 (= Q178)
• binding beryllium trifluoride ion: S37 (= S72), G38 (= G73), K41 (= K76), Q81 (= Q122), S134 (= S175), G136 (= G177), H191 (= H232)
• binding magnesium ion: S42 (= S77), Q81 (= Q122)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 65% coverage: 48:273/349 of query aligns to 13:232/371 of 3puwA

• binding adenosine-5'-diphosphate: V17 (≠ A52), G38 (= G73), C39 (≠ S74), G40 (= G75), K41 (= K76), S42 (= S77), T43 (= T78), R128 (≠ S169), A132 (≠ Q173), S134 (= S175), Q137 (= Q178)
• binding tetrafluoroaluminate ion: S37 (= S72), G38 (= G73), K41 (= K76), Q81 (= Q122), S134 (= S175), G135 (= G176), G136 (= G177), E158 (= E199), H191 (= H232)
• binding magnesium ion: S42 (= S77), Q81 (= Q122)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12

3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 65% coverage: 48:273/349 of query aligns to 13:232/371 of 3puvA

• binding adenosine-5'-diphosphate: V17 (≠ A52), G38 (= G73), C39 (≠ S74), G40 (= G75), K41 (= K76), S42 (= S77), T43 (= T78), R128 (≠ S169), A132 (≠ Q173), S134 (= S175), Q137 (= Q178)
• binding magnesium ion: S42 (= S77), Q81 (= Q122)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 65% coverage: 48:273/349 of query aligns to 14:233/371 of P68187

• A85 (≠ G125) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (≠ S146) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (≠ A154) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (= V157) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (≠ S159) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (≠ E164) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G137 (= G177) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
• D158 (= D198) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
• R228 (≠ D268) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.

Sites not aligning to the query:

• 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• 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)
38% identity, 65% coverage: 48:273/349 of query aligns to 11:230/367 of 1q12A