SitesBLAST
Comparing WP_011842041.1 NCBI__GCF_000015985.1:WP_011842041.1 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
48% identity, 85% coverage: 24:338/372 of query aligns to 20:340/378 of P69874
- C26 (≠ T30) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ M49) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C58) mutation to T: Loss of ATPase activity and transport.
- L60 (= L64) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V80) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V139) mutation to M: Loss of ATPase activity and transport.
- D172 (= D176) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ V275) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ H293) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
53% identity, 62% coverage: 24:253/372 of query aligns to 6:241/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ H91), D80 (= D92)
- binding pyrophosphate 2-: S38 (= S56), G39 (= G57), C40 (= C58), G41 (= G59), K42 (= K60), T43 (= T61), T44 (= T62)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
50% identity, 66% coverage: 24:268/372 of query aligns to 9:261/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
53% identity, 62% coverage: 24:253/372 of query aligns to 9:230/353 of 1vciA
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)
54% identity, 58% coverage: 39:253/372 of query aligns to 22:236/393 of P9WQI3
- H193 (= H210) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
52% identity, 62% coverage: 24:253/372 of query aligns to 5:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F31), S37 (= S56), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (≠ T61), T43 (= T62), Q81 (= Q100), R128 (= R147), A132 (= A151), S134 (= S153), G136 (= G155), Q137 (= Q156), E158 (= E177), H191 (= H210)
- binding magnesium ion: S42 (≠ T61), Q81 (= Q100)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
52% identity, 62% coverage: 24:253/372 of query aligns to 5:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F31), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (≠ T61), T43 (= T62), R128 (= R147), S134 (= S153), Q137 (= Q156)
- binding beryllium trifluoride ion: S37 (= S56), G38 (= G57), K41 (= K60), Q81 (= Q100), S134 (= S153), G136 (= G155), H191 (= H210)
- binding magnesium ion: S42 (≠ T61), Q81 (= Q100)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
52% identity, 62% coverage: 24:253/372 of query aligns to 5:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F31), V17 (= V36), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (≠ T61), T43 (= T62), R128 (= R147), A132 (= A151), S134 (= S153), Q137 (= Q156)
- binding tetrafluoroaluminate ion: S37 (= S56), G38 (= G57), K41 (= K60), Q81 (= Q100), S134 (= S153), G135 (= G154), G136 (= G155), E158 (= E177), H191 (= H210)
- binding magnesium ion: S42 (≠ T61), Q81 (= Q100)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
52% identity, 62% coverage: 24:253/372 of query aligns to 5:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F31), V17 (= V36), G38 (= G57), C39 (= C58), G40 (= G59), K41 (= K60), S42 (≠ T61), T43 (= T62), R128 (= R147), A132 (= A151), S134 (= S153), Q137 (= Q156)
- binding magnesium ion: S42 (≠ T61), Q81 (= Q100)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
52% identity, 62% coverage: 24:253/372 of query aligns to 5:234/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
52% identity, 62% coverage: 24:253/372 of query aligns to 6:235/371 of P68187
- A85 (= A103) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V132) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A135) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A137) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G142) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G155) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D176) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P246) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
52% identity, 62% coverage: 24:253/372 of query aligns to 3:232/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F31), S35 (= S56), G36 (= G57), C37 (= C58), G38 (= G59), K39 (= K60), S40 (≠ T61), T41 (= T62), R126 (= R147), A130 (= A151), S132 (= S153), G134 (= G155), Q135 (= Q156)
8hplC Lpqy-sugabc in state 1 (see paper)
53% identity, 58% coverage: 37:253/372 of query aligns to 17:233/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
53% identity, 58% coverage: 37:253/372 of query aligns to 19:235/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S56), G39 (= G57), G41 (= G59), K42 (= K60), S43 (≠ T61), Q82 (= Q100), Q133 (≠ A151), G136 (= G154), G137 (= G155), Q138 (= Q156), H192 (= H210)
- binding magnesium ion: S43 (≠ T61), Q82 (= Q100)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
53% identity, 58% coverage: 37:253/372 of query aligns to 19:235/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S56), C40 (= C58), G41 (= G59), K42 (= K60), S43 (≠ T61), T44 (= T62), Q82 (= Q100), R129 (= R147), Q133 (≠ A151), S135 (= S153), G136 (= G154), G137 (= G155), Q159 (≠ E177), H192 (= H210)
- binding magnesium ion: S43 (≠ T61), Q82 (= Q100)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
51% identity, 62% coverage: 24:253/372 of query aligns to 6:235/369 of P19566
- L86 (= L104) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P178) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D183) 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
50% identity, 59% coverage: 33:253/372 of query aligns to 7:204/344 of 2awnC
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 89% coverage: 37:366/372 of query aligns to 16:346/348 of 3d31A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
41% identity, 66% coverage: 22:266/372 of query aligns to 4:255/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
41% identity, 66% coverage: 22:266/372 of query aligns to 4:255/353 of 1oxvA
Query Sequence
>WP_011842041.1 NCBI__GCF_000015985.1:WP_011842041.1
MMVERAMTPEAALGTPEGPDHLVLSEVGMTFGTLDVIPSLSLSVRRGEMVAFLGPSGCGK
TTTLRMIAGLLDPTRGRISVGGREITHLPVHDRDMGMVFQSYALFPHMTVAQNVAFGLEM
RRMAKAEIRSRVERALAMVQLGHLAGRKPKALSGGQQQRVALARALVVEPSILLLDEPLS
NLDAKLRDEMRVQIRSLQQQSGITAVFVTHDQVEALSMCDRIVVMRGGHVEQFGTPNEIY
ERPATPFVASFVGRTNRLSGRVDPSGRLLIEGRPVAAEGQLPQGAVEVLVRPHRMSLRAA
AEDQPAGLNSLPGVLTGATFVGDLIQATVRIGGGEITVEQLTRRRSGLPEPGSAVTVAWE
AGDTMVYPEGRA
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