SitesBLAST
Comparing WP_156816733.1 NCBI__GCF_000375485.1:WP_156816733.1 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
34% identity, 93% coverage: 7:478/510 of query aligns to 4:473/501 of P04983
- K43 (= K46) mutation to R: Loss of transport.
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
30% identity, 43% coverage: 12:230/510 of query aligns to 11:233/375 of 2d62A
1g291 Malk (see paper)
32% identity, 43% coverage: 13:230/510 of query aligns to 9:230/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ A77), D80 (= D78)
- binding pyrophosphate 2-: S38 (≠ N42), G39 (= G43), C40 (≠ A44), G41 (= G45), K42 (= K46), T43 (≠ S47), T44 (= T48)
Sites not aligning to the query:
4yerA Crystal structure of an abc transporter atp-binding protein (tm_1403) from thermotoga maritima msb8 at 2.35 a resolution
29% identity, 47% coverage: 7:247/510 of query aligns to 4:236/285 of 4yerA
- binding adenosine-5'-diphosphate: F14 (= F17), F17 (≠ V20), N39 (= N42), G40 (= G43), G42 (= G45), K43 (= K46), T44 (≠ S47), T45 (= T48), T135 (≠ S140), F136 (≠ L141), S137 (= S142)
8k1oB Mycobacterial efflux pump, amppnp bound state (see paper)
35% identity, 42% coverage: 8:221/510 of query aligns to 6:212/215 of 8k1oB
8k1pB Mycobacterial efflux pump, adp+vanadate bound state
35% identity, 42% coverage: 8:221/510 of query aligns to 4:210/213 of 8k1pB
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
32% identity, 44% coverage: 6:230/510 of query aligns to 1:226/241 of 4u00A
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
28% identity, 44% coverage: 7:229/510 of query aligns to 3:231/615 of 5lilA
- binding adenosine-5'-triphosphate: F13 (= F17), V22 (≠ A22), S42 (≠ N42), G43 (= G43), G45 (= G45), K46 (= K46), S47 (= S47), T48 (= T48), Q92 (= Q89), K136 (≠ D133), Q143 (≠ S140), S145 (= S142), G147 (= G144), Q148 (≠ E145)
- binding magnesium ion: S47 (= S47), Q92 (= Q89)
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
28% identity, 44% coverage: 7:229/510 of query aligns to 3:231/592 of 5lj7A
- binding adenosine-5'-triphosphate: V22 (≠ A22), S42 (≠ N42), G43 (= G43), G45 (= G45), K46 (= K46), S47 (= S47), T48 (= T48), Q92 (= Q89), K136 (≠ D133), Q143 (≠ S140), S145 (= S142), G147 (= G144), Q148 (≠ E145)
- binding magnesium ion: S47 (= S47), Q92 (= Q89)
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
30% identity, 44% coverage: 6:228/510 of query aligns to 3:229/648 of P75831
- K47 (= K46) mutation to L: Lack of activity.
- D169 (= D165) mutation to N: Lack of activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 3:220/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 1:218/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F17), S35 (≠ N42), G36 (= G43), C37 (≠ A44), G38 (= G45), K39 (= K46), S40 (= S47), T41 (= T48), R126 (= R136), A130 (≠ S140), S132 (= S142), G134 (= G144), Q135 (≠ E145)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
30% identity, 43% coverage: 8:227/510 of query aligns to 4:221/371 of P68187
- A85 (≠ M92) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ M121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G144) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) 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)
30% identity, 43% coverage: 8:227/510 of query aligns to 3:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F17), S37 (≠ N42), G38 (= G43), C39 (≠ A44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), Q81 (= Q89), R128 (= R136), A132 (≠ S140), S134 (= S142), G136 (= G144), Q137 (≠ E145), E158 (= E166), H191 (= H198)
- binding magnesium ion: S42 (= S47), Q81 (= Q89)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 3:220/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F17), G38 (= G43), C39 (≠ A44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R136), S134 (= S142), Q137 (≠ E145)
- binding beryllium trifluoride ion: S37 (≠ N42), G38 (= G43), K41 (= K46), Q81 (= Q89), S134 (= S142), G136 (= G144), H191 (= H198)
- binding magnesium ion: S42 (= S47), Q81 (= Q89)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 3:220/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F17), V17 (≠ A22), G38 (= G43), C39 (≠ A44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R136), A132 (≠ S140), S134 (= S142), Q137 (≠ E145)
- binding tetrafluoroaluminate ion: S37 (≠ N42), G38 (= G43), K41 (= K46), Q81 (= Q89), S134 (= S142), G135 (≠ M143), G136 (= G144), E158 (= E166), H191 (= H198)
- binding magnesium ion: S42 (= S47), Q81 (= Q89)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 3:220/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F17), V17 (≠ A22), G38 (= G43), C39 (≠ A44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R136), A132 (≠ S140), S134 (= S142), Q137 (≠ E145)
- binding magnesium ion: S42 (= S47), Q81 (= Q89)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 43% coverage: 8:227/510 of query aligns to 4:221/369 of P19566
- L86 (= L93) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ S172) 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.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 48% coverage: 7:250/510 of query aligns to 1:251/343 of P30750
- 40:46 (vs. 42:48, 86% identical) binding ATP
- E166 (= E166) 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
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
26% identity, 47% coverage: 7:244/510 of query aligns to 2:240/240 of 6mjpA
Query Sequence
>WP_156816733.1 NCBI__GCF_000375485.1:WP_156816733.1
MSENAPLLSCRGVTKRFGEVVANRDITFEVRAGQVQALLGENGAGKSTLMSVIAGRFRPD
AGEIRVRGELVQFSRPADAMRMGIGMVYQRFMLVERLTVAENIRLSAHSCGIGSRQADRR
MAELSERYGLGVDPSRTVGSLSMGERQRAEILKLLVQNANILIFDEPTAVLSQPEAEGLF
KIFDRLRQNGCGVVFITHKLEEVMAAADHISILRRGRIIASVAPGEIESKRELARLMVGR
EFVLAVDKPELNPGETVLELKHFAGSGASGRTGFEGVNLSVRRGEILAVIGVAGNGQSAL
AAAVTGNTDAGLAESGSVTFGDETVSAPDWKGHHGIAHVPEDRHNTGSVHDMTLAENYAL
TRLDAAGDGPWFDLSRIAKKTQKAIENYSIRATGAEDMAGSLSGGNLQKLILARELARKP
ELFVAEQPTQGLDIASTEEIWAALIRQRKHSGILLFSGDLKEVLTLADRIAVMFRGRILE
VLDALDADAVARIGLLMAGGETAEGDSQCA
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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