SitesBLAST
Comparing WP_104486353.1 NCBI__GCF_002936955.1:WP_104486353.1 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)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 95% coverage: 2:244/256 of query aligns to 11:255/265 of P07821
- K50 (= K41) mutation to Q: Lack of activity.
- D172 (= D161) mutation to E: Lack of activity.
- E173 (= E162) mutation to A: Lack of activity.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 86% coverage: 1:219/256 of query aligns to 5:211/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 79% coverage: 18:219/256 of query aligns to 22:225/375 of 2d62A
5x40A Structure of a cbio dimer bound with amppcp (see paper)
38% identity, 88% coverage: 3:226/256 of query aligns to 5:229/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (≠ Y12), V18 (≠ L16), A20 (≠ I17), N40 (= N37), G41 (= G38), G43 (= G40), K44 (= K41), S45 (= S42), T46 (= T43), Q88 (≠ P82), H139 (≠ E135), M140 (≠ Q136), L141 (= L137), S142 (= S138), G144 (= G140), Q145 (= Q141), Q166 (≠ E162), H198 (= H195)
- binding magnesium ion: S45 (= S42), Q88 (≠ P82)
3d31A Modbc from methanosarcina acetivorans (see paper)
34% identity, 88% coverage: 3:226/256 of query aligns to 2:217/348 of 3d31A
Sites not aligning to the query:
1g291 Malk (see paper)
33% identity, 79% coverage: 18:219/256 of query aligns to 19:222/372 of 1g291
- binding magnesium ion: D69 (≠ N68), E71 (≠ S70), K72 (≠ R71), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (≠ N37), G39 (= G38), C40 (≠ T39), G41 (= G40), K42 (= K41), T43 (≠ S42), T44 (= T43)
Sites not aligning to the query:
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
29% identity, 91% coverage: 3:234/256 of query aligns to 3:233/240 of 6mjpA
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/238 of 6s8nB
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/238 of 6s8gA
- binding phosphoaminophosphonic acid-adenylate ester: Y12 (= Y12), R15 (≠ G15), N37 (= N37), G40 (= G40), K41 (= K41), T42 (≠ S42), T43 (= T43), Q84 (= Q83), S136 (≠ Q136), S138 (= S138), E141 (≠ Q141)
6b89A E. Coli lptb in complex with adp and novobiocin (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/234 of 6b89A
- binding adenosine-5'-diphosphate: Y12 (= Y12), R15 (≠ G15), V17 (≠ I17), N37 (= N37), G38 (= G38), G40 (= G40), K41 (= K41), T42 (≠ S42), T43 (= T43)
- binding magnesium ion: T42 (≠ S42), Q84 (= Q83)
- binding novobiocin: L71 (vs. gap), H72 (vs. gap), P83 (= P82), A86 (≠ T85), S87 (≠ P86), F89 (≠ G88), R90 (≠ V89), R91 (= R90), L92 (≠ I91), V101 (≠ A100), Q135 (≠ E135), R149 (≠ Q149)
4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/234 of 4p31A
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/235 of 6mhzA
- binding adp orthovanadate: Y12 (= Y12), N37 (= N37), G38 (= G38), G40 (= G40), K41 (= K41), T42 (≠ S42), T43 (= T43), Q84 (= Q83), S136 (≠ Q136), S138 (= S138), G139 (= G139), G140 (= G140), E162 (= E162), G166 (≠ A166), H194 (= H195)
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
30% identity, 91% coverage: 2:234/256 of query aligns to 2:233/233 of 6b8bA
- binding adenosine-5'-diphosphate: Y12 (= Y12), R15 (≠ G15), V17 (≠ I17), G38 (= G38), G40 (= G40), K41 (= K41), T42 (≠ S42), T43 (= T43)
- binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (≠ G88), R90 (≠ V89), R91 (= R90)
O65934 ABC transporter ATP-binding/permease protein Rv1747; EC 7.-.-.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
35% identity, 81% coverage: 17:223/256 of query aligns to 334:539/865 of O65934
- E479 (= E162) mutation to Q: Loss of ATPase activity.
Sites not aligning to the query:
- 33 R→A: Strong decrease in phosphorylation.
- 47 S→A: Strong decrease in phosphorylation. Lack of interaction with PknF. Attenuates growth in macrophages.
- 69 N→A: Strong decrease in phosphorylation.
- 152 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-210.
- 210 modified: Phosphothreonine; T→A: Lack of phosphorylation. Attenuates growth in macrophages and in mice; when associated with A-152.
- 234 R→A: Strong decrease in phosphorylation.
- 248 S→A: Strong decrease in phosphorylation. Decreases interaction with PknF.
- 270 N→A: Strong decrease in phosphorylation.
6mbnA Lptb e163q in complex with atp (see paper)
29% identity, 91% coverage: 2:234/256 of query aligns to 3:234/241 of 6mbnA
4fwiB Crystal structure of the nucleotide-binding domain of a dipeptide abc transporter (see paper)
32% identity, 91% coverage: 13:246/256 of query aligns to 16:263/310 of 4fwiB
- binding adenosine-5'-triphosphate: S42 (≠ N37), A43 (≠ G38), S44 (≠ T39), G45 (= G40), K46 (= K41), S47 (= S42), T48 (= T43), N60 (≠ Q55), Q96 (= Q83)
- binding magnesium ion: S47 (= S42), Q96 (= Q83)
- binding iron/sulfur cluster: H247 (≠ I230), P248 (≠ Q231)
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)
31% identity, 79% coverage: 17:219/256 of query aligns to 32:230/378 of P69874
- F45 (≠ L30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ T39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 85% coverage: 2:219/256 of query aligns to 3:216/371 of P68187
- A85 (≠ P86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A127) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
32% identity, 85% coverage: 2:219/256 of query aligns to 2:215/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y12), S37 (≠ N37), G38 (= G38), C39 (≠ T39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), Q81 (= Q83), R128 (= R132), A132 (≠ Q136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (= S42), Q81 (= Q83)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
32% identity, 85% coverage: 2:219/256 of query aligns to 2:215/371 of 3puxA