SitesBLAST
Comparing WP_011384270.1 NCBI__GCF_000009985.1:WP_011384270.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
43% identity, 70% coverage: 33:215/262 of query aligns to 44:236/382 of 7ahhC
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
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
43% identity, 70% coverage: 33:215/262 of query aligns to 44:236/382 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)
42% identity, 70% coverage: 33:215/262 of query aligns to 44:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S50), G62 (= G51), G64 (= G53), K65 (= K54), S66 (= S55), T67 (= T56), Q111 (= Q90), K161 (≠ H140), Q162 (≠ H141), S164 (= S143), G166 (= G145), M167 (≠ Q146), Q188 (≠ E167), H221 (= H200)
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)
38% identity, 79% coverage: 10:215/262 of query aligns to 16:221/378 of P69874
- C26 (≠ G20) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y21) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
40% identity, 71% coverage: 31:216/262 of query aligns to 22:217/375 of 2d62A
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
37% identity, 78% coverage: 11:215/262 of query aligns to 1:218/232 of 1f3oA
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
37% identity, 78% coverage: 11:215/262 of query aligns to 1:218/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (= Y21), S40 (= S50), G41 (= G51), S42 (≠ A52), G43 (= G53), K44 (= K54), S45 (= S55), T46 (= T56), F138 (= F134), Q145 (≠ H141), S147 (= S143), G149 (= G145), Q150 (= Q146), H204 (= H200)
1g291 Malk (see paper)
40% identity, 71% coverage: 31:216/262 of query aligns to 19:214/372 of 1g291
- binding magnesium ion: D69 (≠ E75), E71 (≠ P77), K72 (= K78), K79 (≠ D81), D80 (≠ S82)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (≠ A52), G41 (= G53), K42 (= K54), T43 (≠ S55), T44 (= T56)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 76% coverage: 29:228/262 of query aligns to 16:220/374 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)
37% identity, 76% coverage: 29:228/262 of query aligns to 16:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S50), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), Q81 (= Q90), R128 (= R137), A132 (≠ H141), S134 (= S143), G136 (= G145), Q137 (= Q146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S55), Q81 (= Q90)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 76% coverage: 29:228/262 of query aligns to 16:220/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (= R137), S134 (= S143), Q137 (= Q146)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q90), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (= S55), Q81 (= Q90)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 76% coverage: 29:228/262 of query aligns to 16:220/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (= R137), A132 (≠ H141), S134 (= S143), Q137 (= Q146)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S55), Q81 (= Q90)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 76% coverage: 29:228/262 of query aligns to 16:220/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (= T56), R128 (= R137), A132 (≠ H141), S134 (= S143), Q137 (= Q146)
- binding magnesium ion: S42 (= S55), Q81 (= Q90)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 76% coverage: 29:228/262 of query aligns to 14:218/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S50), G36 (= G51), C37 (≠ A52), G38 (= G53), K39 (= K54), S40 (= S55), T41 (= T56), R126 (= R137), A130 (≠ H141), S132 (= S143), G134 (= G145), Q135 (= Q146)
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)
37% identity, 76% coverage: 29:228/262 of query aligns to 17:221/371 of P68187
- A85 (≠ R93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) 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.
Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
37% identity, 78% coverage: 11:215/262 of query aligns to 1:210/276 of Q5M243
- Q90 (≠ L94) mutation to A: No effect on ATPase, 10-fold decrease in riboflavin uptake; when associated with A-97 in EcfA2.
- E163 (= E167) mutation to Q: 10-fold decrease in ATPase and riboflavin uptake; when associated with Q-171 in EcfA2.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 76% coverage: 29:228/262 of query aligns to 17:221/369 of P19566
- L86 (= L94) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) 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.
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
38% identity, 79% coverage: 11:217/262 of query aligns to 3:218/226 of 5xu1B
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)
36% identity, 80% coverage: 12:221/262 of query aligns to 4:214/393 of P9WQI3
- H193 (= H200) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 71% coverage: 31:217/262 of query aligns to 21:216/343 of P30750
- 40:46 (vs. 50:56, 100% identical) binding
- E166 (= E167) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
Query Sequence
>WP_011384270.1 NCBI__GCF_000009985.1:WP_011384270.1
MDALAPVSPPVIRLEGLAFGYPGDRSHAIVLQDLDLEVRHGDFIALVGQSGAGKSTLLRV
IAGLVPAVLGQVYVEPPKEPDSRQIGMVFQDARLLPWRRVLANVEYGLEGLVKSRHERRR
RALAALDLVGLTEFADRWPHHLSGGQRQRVGLARALAVRPALLLMDEPFGALDPATRHGL
QDQLLSIWQATGTSIIFVTHDIDEATYLADRVIVLGGSPARILRQLDVEAPRPRCRNDLA
DDPTATALRSQLYETFFYKDGI
Or try a new SitesBLAST search
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