SitesBLAST
Comparing WP_013421089.1 NCBI__GCF_000166055.1:WP_013421089.1 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)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
45% identity, 87% coverage: 15:257/278 of query aligns to 3:253/658 of 8wm7C
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
45% identity, 87% coverage: 15:257/278 of query aligns to 3:253/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (= F24), Y20 (≠ F31), S42 (= S53), G43 (= G54), G45 (= G56), K46 (= K57), S47 (= S58), T48 (= T59), Q83 (= Q94), K132 (≠ A141), E136 (≠ Q145), S138 (= S147), G140 (= G149), H195 (= H204)
- binding magnesium ion: S47 (= S58), Q83 (= Q94)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
43% identity, 87% coverage: 15:256/278 of query aligns to 5:253/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
43% identity, 87% coverage: 15:256/278 of query aligns to 3:251/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (≠ F24), H40 (≠ A52), S41 (= S53), G42 (= G54), G44 (= G56), K45 (= K57), S46 (= S58), T47 (= T59), Q82 (= Q94), Q135 (= Q145), S137 (= S147), G139 (= G149), M140 (= M150), H194 (= H204)
- binding magnesium ion: S46 (= S58), Q82 (= Q94)
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)
38% identity, 90% coverage: 12:261/278 of query aligns to 1:240/393 of P9WQI3
- H193 (= H204) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 77% coverage: 15:228/278 of query aligns to 18:228/378 of P69874
- C26 (≠ A23) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F24) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F46) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C55) mutation to T: Loss of ATPase activity and transport.
- L60 (= L61) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I77) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V133) mutation to M: Loss of ATPase activity and transport.
- D172 (= D170) 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.
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 67% coverage: 33:219/278 of query aligns to 18:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S53), C40 (= C55), G41 (= G56), K42 (= K57), S43 (= S58), T44 (= T59), Q82 (= Q94), R129 (≠ A141), Q133 (= Q145), S135 (= S147), G136 (= G148), G137 (= G149), Q159 (≠ E171), H192 (= H204)
- binding magnesium ion: S43 (= S58), Q82 (= Q94)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 67% coverage: 33:219/278 of query aligns to 18:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S53), G39 (= G54), G41 (= G56), K42 (= K57), S43 (= S58), Q82 (= Q94), Q133 (= Q145), G136 (= G148), G137 (= G149), Q138 (≠ M150), H192 (= H204)
- binding magnesium ion: S43 (= S58), Q82 (= Q94)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 67% coverage: 33:219/278 of query aligns to 16:205/384 of 8hplC
Sites not aligning to the query:
1g291 Malk (see paper)
41% identity, 75% coverage: 12:220/278 of query aligns to 1:214/372 of 1g291
- binding magnesium ion: D69 (≠ G84), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (≠ N86)
- binding pyrophosphate 2-: S38 (= S53), G39 (= G54), C40 (= C55), G41 (= G56), K42 (= K57), T43 (≠ S58), T44 (= T59)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 75% coverage: 12:220/278 of query aligns to 4:217/375 of 2d62A
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
42% identity, 78% coverage: 12:229/278 of query aligns to 1:215/369 of P19566
- L86 (= L98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P172) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D177) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 78% coverage: 12:229/278 of query aligns to 1:215/371 of P68187
- A85 (≠ R97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Q129) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D131) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S136) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G149) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D170) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 78% coverage: 13:229/278 of query aligns to 1:214/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
42% identity, 78% coverage: 13:229/278 of query aligns to 1:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F24), S37 (= S53), G38 (= G54), C39 (= C55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), Q81 (= Q94), R128 (≠ A141), A132 (≠ Q145), S134 (= S147), G136 (= G149), Q137 (≠ M150), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 78% coverage: 13:229/278 of query aligns to 1:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F24), G38 (= G54), C39 (= C55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A141), S134 (= S147), Q137 (≠ M150)
- binding beryllium trifluoride ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q94), S134 (= S147), G136 (= G149), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 78% coverage: 13:229/278 of query aligns to 1:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ G28), G38 (= G54), C39 (= C55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A141), A132 (≠ Q145), S134 (= S147), Q137 (≠ M150)
- binding tetrafluoroaluminate ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q94), S134 (= S147), G135 (= G148), G136 (= G149), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 78% coverage: 13:229/278 of query aligns to 1:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F24), V17 (≠ G28), G38 (= G54), C39 (= C55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A141), A132 (≠ Q145), S134 (= S147), Q137 (≠ M150)
- binding magnesium ion: S42 (= S58), Q81 (= Q94)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 77% coverage: 15:229/278 of query aligns to 1:212/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F24), S35 (= S53), G36 (= G54), C37 (= C55), G38 (= G56), K39 (= K57), S40 (= S58), T41 (= T59), R126 (≠ A141), A130 (≠ Q145), S132 (= S147), G134 (= G149), Q135 (≠ M150)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 70% coverage: 35:229/278 of query aligns to 12:184/344 of 2awnC
Sites not aligning to the query:
Query Sequence
>WP_013421089.1 NCBI__GCF_000166055.1:WP_013421089.1
MTALANPVTFRLAALELESVGRAFDVAGTKFDALRDVSLTVCEGEFIAFVGASGCGKSTL
LKAIVGLDRGFEGSIRIDGKPVDGPNLDRSIVFQEHRLLPWLTVEANVGAALRRSGLPSS
ERKQRVAEQLDLVGLSSFAKAYPAQLSGGMAQRVAIARALVTRPRFLLLDEPLGALDALT
RLRLQGELARLIRHEGTTALLVTHDVDEAVTLADRIVVMKPHPGRVARILDVPRHAIRDR
SSPAFLRARDEVLGLLGVPGFVEEPDAPRDRPAELQTA
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