SitesBLAST
Comparing WP_041456731.1 NCBI__GCF_000204075.1:WP_041456731.1 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
44% identity, 99% coverage: 1:430/433 of query aligns to 4:375/375 of 2d62A
1g291 Malk (see paper)
48% identity, 91% coverage: 37:430/433 of query aligns to 14:372/372 of 1g291
- binding magnesium ion: D69 (= D92), E71 (vs. gap), K72 (vs. gap), K79 (= K96), D80 (≠ E97), E292 (= E347), D293 (≠ H348), K359 (= K417)
- binding pyrophosphate 2-: S38 (= S61), G39 (= G62), C40 (= C63), G41 (= G64), K42 (= K65), T43 (≠ S66), T44 (= T67)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
47% identity, 91% coverage: 37:429/433 of query aligns to 17:352/353 of 1vciA
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 98% coverage: 2:427/433 of query aligns to 1:357/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S61), C40 (= C63), G41 (= G64), K42 (= K65), S43 (= S66), T44 (= T67), Q82 (= Q105), R129 (= R192), Q133 (= Q196), S135 (= S198), G136 (= G199), G137 (= G200), Q159 (≠ E222), H192 (= H255)
- binding magnesium ion: S43 (= S66), Q82 (= Q105)
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 98% coverage: 2:427/433 of query aligns to 1:358/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S61), G39 (= G62), G41 (= G64), K42 (= K65), S43 (= S66), Q82 (= Q105), Q133 (= Q196), G136 (= G199), G137 (= G200), Q138 (= Q201), H192 (= H255)
- binding magnesium ion: S43 (= S66), Q82 (= Q105)
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 98% coverage: 2:427/433 of query aligns to 1:379/384 of 8hplC
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)
41% identity, 98% coverage: 1:425/433 of query aligns to 1:383/393 of P9WQI3
- H193 (= H255) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 79% coverage: 37:377/433 of query aligns to 13:317/374 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)
46% identity, 79% coverage: 37:377/433 of query aligns to 13:317/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S61), G38 (= G62), C39 (= C63), G40 (= G64), K41 (= K65), S42 (= S66), T43 (= T67), Q81 (= Q105), R128 (= R192), A132 (≠ Q196), S134 (= S198), G136 (= G200), Q137 (= Q201), E158 (= E222), H191 (= H255)
- binding magnesium ion: S42 (= S66), Q81 (= Q105)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
46% identity, 79% coverage: 37:377/433 of query aligns to 13:317/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G62), C39 (= C63), G40 (= G64), K41 (= K65), S42 (= S66), T43 (= T67), R128 (= R192), S134 (= S198), Q137 (= Q201)
- binding beryllium trifluoride ion: S37 (= S61), G38 (= G62), K41 (= K65), Q81 (= Q105), S134 (= S198), G136 (= G200), H191 (= H255)
- binding magnesium ion: S42 (= S66), Q81 (= Q105)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
46% identity, 79% coverage: 37:377/433 of query aligns to 13:317/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V41), G38 (= G62), C39 (= C63), G40 (= G64), K41 (= K65), S42 (= S66), T43 (= T67), R128 (= R192), A132 (≠ Q196), S134 (= S198), Q137 (= Q201)
- binding tetrafluoroaluminate ion: S37 (= S61), G38 (= G62), K41 (= K65), Q81 (= Q105), S134 (= S198), G135 (= G199), G136 (= G200), E158 (= E222), H191 (= H255)
- binding magnesium ion: S42 (= S66), Q81 (= Q105)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
46% identity, 79% coverage: 37:377/433 of query aligns to 13:317/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V41), G38 (= G62), C39 (= C63), G40 (= G64), K41 (= K65), S42 (= S66), T43 (= T67), R128 (= R192), A132 (≠ Q196), S134 (= S198), Q137 (= Q201)
- binding magnesium ion: S42 (= S66), Q81 (= Q105)
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)
46% identity, 79% coverage: 37:377/433 of query aligns to 14:318/371 of P68187
- A85 (= A108) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ T156) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V177) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V180) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ H182) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E187) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G200) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D221) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R291) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F304) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W328) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G337) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ I341) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G343) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V361) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E367) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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)
46% identity, 79% coverage: 37:377/433 of query aligns to 11:315/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S61), G36 (= G62), C37 (= C63), G38 (= G64), K39 (= K65), S40 (= S66), T41 (= T67), R126 (= R192), A130 (≠ Q196), S132 (= S198), G134 (= G200), Q135 (= Q201)
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)
46% identity, 79% coverage: 37:377/433 of query aligns to 14:316/369 of P19566
- L86 (= L109) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P223) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D228) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E367) mutation to 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)
43% identity, 78% coverage: 39:377/433 of query aligns to 8:287/344 of 2awnC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 61% coverage: 41:302/433 of query aligns to 32:253/378 of P69874
- F45 (= F54) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C63) mutation to T: Loss of ATPase activity and transport.
- L60 (= L69) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V85) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L184) mutation to M: Loss of ATPase activity and transport.
- D172 (= D221) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 90% coverage: 37:424/433 of query aligns to 16:353/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 90% coverage: 37:424/433 of query aligns to 16:353/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 90% coverage: 37:424/433 of query aligns to 16:353/353 of 1oxuA
Sites not aligning to the query:
Query Sequence
>WP_041456731.1 NCBI__GCF_000204075.1:WP_041456731.1
MAQVVLENVYKSFPPRRGENVSSQTPSAKKTDAEPAGTVNVLRRINLTIPDGEFMVLVGP
SGCGKSTLLRLIAGLEVMTGGNIWVGDRLVNDLPPKERDIAMVFQNYALYPHMTVYDNIA
FGLRRRSSSEQHRDNSHPSSQTQFPTWAENLLVGATRKLPKGLRYISDQEREVDEQVRSV
AHLLQMETLLNRLPKQLSGGQRQRVALGRAIARNPQVFLMDEPLSNLDAKLRAETRAQIV
KLQRQLGTTTIYVTHDQTEAMTMGDRIAIMNQGQIQQVASPLELYNHPANRFVAEFIGTP
PMNFIPVEFHAPLLITHSQFRLTLPEIWASALQKYDGQTLILGIRPEHLTVSVPATKNLP
VQVDLVENLGNDSFINVVLTEAESRFAHTIKPLQVRVPSDRIINVGEQIWLSLTLDKIHF
FDPDTDLAIFPKN
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