SitesBLAST
Comparing 15634 FitnessBrowser__Keio:15634 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)
39% identity, 97% coverage: 11:506/511 of query aligns to 4:497/501 of P04983
- K43 (= K50) mutation to R: Loss of transport.
7z18I E. Coli c-p lyase bound to a phnk abc dimer and atp (see paper)
33% identity, 44% coverage: 267:489/511 of query aligns to 2:230/250 of 7z18I
- binding adenosine-5'-triphosphate: Y13 (vs. gap), S38 (≠ V298), G39 (= G299), S40 (≠ A300), G41 (= G301), K42 (≠ R302), T43 (= T303), T44 (≠ E304), Q88 (≠ D346), R136 (≠ Q396), T143 (= T403), S145 (= S405), G147 (= G407), M148 (≠ N408), H202 (≠ S461)
- binding magnesium ion: T43 (= T303), Q88 (≠ D346)
7z15I E. Coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi (see paper)
33% identity, 44% coverage: 267:489/511 of query aligns to 2:230/253 of 7z15I
- binding adenosine-5'-diphosphate: Y13 (vs. gap), K17 (≠ E277), G18 (= G278), S38 (≠ V298), G39 (= G299), G41 (= G301), K42 (≠ R302), T43 (= T303), T44 (≠ E304), R136 (≠ Q396), T143 (= T403), S145 (= S405), M148 (≠ N408)
- binding magnesium ion: T43 (= T303), Q88 (≠ D346)
7z16I E. Coli c-p lyase bound to phnk/phnl dual abc dimer with amppnp and phnk e171q mutation (see paper)
33% identity, 44% coverage: 267:489/511 of query aligns to 2:230/250 of 7z16I
- binding phosphoaminophosphonic acid-adenylate ester: Y13 (vs. gap), K17 (≠ E277), S38 (≠ V298), G39 (= G299), S40 (≠ A300), G41 (= G301), K42 (≠ R302), T43 (= T303), T44 (≠ E304), R136 (≠ Q396), T143 (= T403), S145 (= S405), G147 (= G407), M148 (≠ N408), H202 (≠ S461)
1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
30% identity, 44% coverage: 11:234/511 of query aligns to 6:233/240 of 1ji0A
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 42% coverage: 15:227/511 of query aligns to 7:221/369 of P19566
- L86 (= L97) 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 (≠ T172) 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.
6b8bA E. Coli lptb in complex with adp and a novobiocin derivative (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/233 of 6b8bA
- binding adenosine-5'-diphosphate: Y12 (= Y21), R15 (≠ V24), V17 (= V26), G38 (= G47), G40 (= G49), K41 (= K50), T42 (≠ S51), T43 (= T52)
- binding (3s,5s,7s)-N-{7-[(3-O-carbamoyl-6-deoxy-5-methyl-4-O-methyl-beta-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}tricyclo[3.3.1.1~3,7~]decane-1-carboxamide: F89 (= F98), R90 (≠ P99), R91 (≠ S100)
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/238 of 6s8nB
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/238 of 6s8gA
- binding phosphoaminophosphonic acid-adenylate ester: Y12 (= Y21), R15 (≠ V24), N37 (= N46), G40 (= G49), K41 (= K50), T42 (≠ S51), T43 (= T52), Q84 (= Q93), S136 (= S140), S138 (≠ D142), E141 (≠ D145)
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/235 of 6mhzA
- binding adp orthovanadate: Y12 (= Y21), N37 (= N46), G38 (= G47), G40 (= G49), K41 (= K50), T42 (≠ S51), T43 (= T52), Q84 (= Q93), S136 (= S140), S138 (≠ D142), G139 (≠ V143), G140 (≠ A144), E162 (= E166), G166 (≠ S170), H194 (= H198)
6b89A E. Coli lptb in complex with adp and novobiocin (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/234 of 6b89A
- binding adenosine-5'-diphosphate: Y12 (= Y21), R15 (≠ V24), V17 (= V26), N37 (= N46), G38 (= G47), G40 (= G49), K41 (= K50), T42 (≠ S51), T43 (= T52)
- binding magnesium ion: T42 (≠ S51), Q84 (= Q93)
- binding novobiocin: L71 (≠ V81), H72 (= H82), P83 (= P92), A86 (≠ P95), S87 (≠ L96), F89 (= F98), R90 (≠ P99), R91 (≠ S100), L92 (= L101), V101 (≠ G110), Q135 (≠ G139), R149 (= R153)
4p31A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 3:232/234 of 4p31A
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 43% coverage: 8:226/511 of query aligns to 1:236/254 of 1g6hA
6mbnA Lptb e163q in complex with atp (see paper)
29% identity, 44% coverage: 12:236/511 of query aligns to 4:233/241 of 6mbnA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 43% coverage: 8:226/511 of query aligns to 1:236/253 of 1g9xB
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
30% identity, 43% coverage: 10:227/511 of query aligns to 16:235/378 of P69874
- C26 (≠ Q20) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y21) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V39) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A48) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M54) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
33% identity, 42% coverage: 15:227/511 of query aligns to 6:220/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 42% coverage: 15:227/511 of query aligns to 7:221/371 of P68187
- A85 (≠ L96) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K113) 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 (≠ A126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ A144) 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)
33% identity, 42% coverage: 15:227/511 of query aligns to 6:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y21), S37 (≠ N46), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), Q81 (= Q93), R128 (≠ S136), A132 (≠ S140), S134 (≠ D142), G136 (≠ A144), Q137 (≠ D145), E158 (= E166), H191 (= H198)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 42% coverage: 15:227/511 of query aligns to 6:220/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ S136), S134 (≠ D142), Q137 (≠ D145)
- binding beryllium trifluoride ion: S37 (≠ N46), G38 (= G47), K41 (= K50), Q81 (= Q93), S134 (≠ D142), G136 (≠ A144), H191 (= H198)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
Query Sequence
>15634 FitnessBrowser__Keio:15634
MQTSDTRALPLLCARSVYKQYSGVNVLKGIDFTLHQGEVHALLGGNGAGKSTLMKIIAGI
TPADSGTLEIEGNNYVRLTPVHAHQLGIYLVPQEPLLFPSLSIKENILFGLAKKQLSMQK
MKNLLAALGCQFDLHSLAGSLDVADRQMVEILRGLMRDSRILILDEPTASLTPAETERLF
SRLQELLATGVGIVFISHKLPEIRQIADRISVMRDGTIALSGKTSELSTDDIIQAITPAV
REKSLSASQKLWLELPGNRPQHAAGTPVLTLENLTGEGFRNVSLTLNAGEILGLAGLVGA
GRTELAETLYGLRTLRGGRIMLNGKEINKLSTGERLLRGLVYLPEDRQSSGLNLDASLAW
NVCALTHNLRGFWAKTAKDNATLERYRRALNIKFNQPEQAARTLSGGNQQKILIAKCLEA
SPQVLIVDEPTRGVDVSARNDIYQLLRSIAAQNVAVLLISSDLEEIELMADRVYVMHQGE
ITHSALTERDINVETIMRVAFGDSQRQEASC
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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