SitesBLAST
Comparing WP_106717340.1 NCBI__GCF_003010935.1:WP_106717340.1 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
32% identity, 95% coverage: 14:256/257 of query aligns to 4:239/501 of P04983
- K43 (= K53) mutation to R: Loss of transport.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
29% identity, 89% coverage: 14:242/257 of query aligns to 1:220/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F24), V16 (≠ A29), S36 (≠ N49), G37 (= G50), S38 (≠ A51), G39 (= G52), K40 (= K53), S41 (= S54), T42 (= T55), E162 (= E184), H194 (= H216)
- binding magnesium ion: S41 (= S54), E162 (= E184)
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
30% identity, 89% coverage: 13:242/257 of query aligns to 1:220/241 of 4u00A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 87% coverage: 13:235/257 of query aligns to 16:225/378 of P69874
- C26 (≠ R23) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F24) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I42) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A51) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I57) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I73) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ R132) mutation to M: Loss of ATPase activity and transport.
- D172 (= D183) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 88% coverage: 14:239/257 of query aligns to 4:231/254 of 1g6hA
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 3:210/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F24), S37 (≠ N49), G38 (= G50), C39 (≠ A51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), Q81 (= Q96), R128 (≠ A154), A132 (≠ L158), S134 (= S160), G136 (= G162), Q137 (= Q163), E158 (= E184), H191 (= H216)
- binding magnesium ion: S42 (= S54), Q81 (= Q96)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 3:210/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F24), G38 (= G50), C39 (≠ A51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ A154), S134 (= S160), Q137 (= Q163)
- binding beryllium trifluoride ion: S37 (≠ N49), G38 (= G50), K41 (= K53), Q81 (= Q96), S134 (= S160), G136 (= G162), H191 (= H216)
- binding magnesium ion: S42 (= S54), Q81 (= Q96)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 3:210/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ A29), G38 (= G50), C39 (≠ A51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ A154), A132 (≠ L158), S134 (= S160), Q137 (= Q163)
- binding tetrafluoroaluminate ion: S37 (≠ N49), G38 (= G50), K41 (= K53), Q81 (= Q96), S134 (= S160), G135 (= G161), G136 (= G162), E158 (= E184), H191 (= H216)
- binding magnesium ion: S42 (= S54), Q81 (= Q96)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 3:210/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ A29), G38 (= G50), C39 (≠ A51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ A154), A132 (≠ L158), S134 (= S160), Q137 (= Q163)
- binding magnesium ion: S42 (= S54), Q81 (= Q96)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 86% coverage: 15:235/257 of query aligns to 4:211/371 of P68187
- A85 (= A99) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ T138) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L141) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q143) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ P150) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G162) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D183) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 1:208/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F24), S35 (≠ N49), G36 (= G50), C37 (≠ A51), G38 (= G52), K39 (= K53), S40 (= S54), T41 (= T55), R126 (≠ A154), A130 (≠ L158), S132 (= S160), G134 (= G162), Q135 (= Q163)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
31% identity, 86% coverage: 15:235/257 of query aligns to 3:210/374 of 2awnB
7mdyC Lolcde nucleotide-bound
33% identity, 88% coverage: 14:240/257 of query aligns to 2:224/226 of 7mdyC
- binding adp orthovanadate: Y12 (≠ F24), G42 (= G50), S43 (≠ A51), G44 (= G52), K45 (= K53), S46 (= S54), T47 (= T55), Q91 (= Q96), H138 (≠ A154), E142 (≠ L158), S144 (= S160), G145 (= G161), G146 (= G162), E168 (= E184), N172 (≠ A188), H201 (= H216)
- binding magnesium ion: S46 (= S54), Q91 (= Q96)
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
33% identity, 88% coverage: 14:240/257 of query aligns to 5:227/233 of P75957
- G42 (= G47) mutation to D: Loss of lipoprotein release when overexpressed.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 84% coverage: 21:235/257 of query aligns to 10:211/369 of P19566
- L86 (= L100) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P185) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ G190) 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.
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 88% coverage: 14:239/257 of query aligns to 4:231/253 of 1g9xB
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
32% identity, 88% coverage: 14:240/257 of query aligns to 4:226/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: V23 (vs. gap), S43 (≠ N49), G44 (= G50), G46 (= G52), K47 (= K53), S48 (= S54), T49 (= T55), Q93 (= Q96), R137 (vs. gap), H140 (≠ A154), E144 (≠ L158), S146 (= S160), G148 (= G162), E149 (≠ Q163), H203 (= H216)
- binding magnesium ion: S48 (= S54), Q93 (= Q96)
3c4jA Abc protein artp in complex with atp-gamma-s
27% identity, 89% coverage: 14:242/257 of query aligns to 3:222/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
27% identity, 89% coverage: 14:242/257 of query aligns to 3:222/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
27% identity, 89% coverage: 14:242/257 of query aligns to 3:222/242 of 2olkA