SitesBLAST
Comparing WP_011187451.1 NCBI__GCF_000025945.1:WP_011187451.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
46% identity, 94% coverage: 3:397/421 of query aligns to 2:380/382 of 7ahhC
- 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: L275 (≠ V286), S297 (≠ E308), S298 (≠ Y309)
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F13), T39 (= T40), V40 (= V41), G41 (= G42), G62 (= G63), G64 (= G65), K65 (= K66), D187 (= D188), E188 (= E189)
7aheC Opua inhibited inward facing (see paper)
46% identity, 94% coverage: 3:397/421 of query aligns to 2:380/382 of 7aheC
- 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: L275 (≠ V286), S297 (≠ E308), S298 (≠ Y309)
7ahdC Opua (e190q) occluded (see paper)
59% identity, 62% coverage: 3:261/421 of query aligns to 2:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F13), T39 (= T40), S61 (= S62), G62 (= G63), G64 (= G65), K65 (= K66), S66 (= S67), T67 (= T68), Q111 (= Q112), K161 (= K162), Q162 (≠ E163), S164 (= S165), G166 (= G167), M167 (= M168), Q188 (≠ E189), H221 (= H222)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 58% coverage: 32:275/421 of query aligns to 11:253/375 of 2d62A
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
39% identity, 56% coverage: 32:267/421 of query aligns to 6:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ T37), V16 (≠ G42), S36 (= S62), G37 (= G63), S38 (= S64), G39 (= G65), K40 (= K66), S41 (= S67), T42 (= T68), E162 (= E189), H194 (= H222)
- binding magnesium ion: S41 (= S67), E162 (= E189)
1g291 Malk (see paper)
37% identity, 59% coverage: 27:275/421 of query aligns to 3:250/372 of 1g291
- binding magnesium ion: D69 (≠ K93), E71 (≠ D95), K72 (= K96), K79 (≠ R103), D80 (≠ R104)
- binding pyrophosphate 2-: S38 (= S62), G39 (= G63), C40 (≠ S64), G41 (= G65), K42 (= K66), T43 (≠ S67), T44 (= T68)
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)
42% identity, 52% coverage: 48:264/421 of query aligns to 38:248/378 of P69874
- F45 (≠ I55) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S64) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ V70) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V86) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V151) mutation to M: Loss of ATPase activity and transport.
- D172 (= D188) 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.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 55% coverage: 34:266/421 of query aligns to 12:243/343 of P30750
- 40:46 (vs. 62:68, 86% identical) binding ATP
- E166 (= E189) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
37% identity, 55% coverage: 34:266/421 of query aligns to 13:244/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: Q14 (≠ E35), I19 (≠ T40), S41 (= S62), G42 (= G63), A43 (≠ S64), G44 (= G65), K45 (= K66), S46 (= S67), T47 (= T68), N141 (≠ E163), S143 (= S165), Q146 (≠ M168), H200 (= H222)
Sites not aligning to the query:
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
39% identity, 63% coverage: 4:267/421 of query aligns to 3:239/241 of 4u00A
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
37% identity, 55% coverage: 34:266/421 of query aligns to 13:244/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
37% identity, 55% coverage: 34:266/421 of query aligns to 13:244/344 of 3tuiC
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 56% coverage: 31:264/421 of query aligns to 6:233/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 56% coverage: 31:264/421 of query aligns to 7:234/371 of P68187
- A85 (= A115) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E136) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A144) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A147) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N149) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ N154) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G167) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D188) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D258) 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)
38% identity, 56% coverage: 31:264/421 of query aligns to 4:231/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ T37), S35 (= S62), G36 (= G63), C37 (≠ S64), G38 (= G65), K39 (= K66), S40 (= S67), T41 (= T68), R126 (≠ S159), A130 (≠ E163), S132 (= S165), G134 (= G167), Q135 (≠ M168)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 56% coverage: 31:264/421 of query aligns to 6:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ T37), S37 (= S62), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (= T68), Q81 (= Q112), R128 (≠ S159), A132 (≠ E163), S134 (= S165), G136 (= G167), Q137 (≠ M168), E158 (= E189), H191 (= H222)
- binding magnesium ion: S42 (= S67), Q81 (= Q112)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 56% coverage: 31:264/421 of query aligns to 6:233/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ T37), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (= T68), R128 (≠ S159), S134 (= S165), Q137 (≠ M168)
- binding beryllium trifluoride ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q112), S134 (= S165), G136 (= G167), H191 (= H222)
- binding magnesium ion: S42 (= S67), Q81 (= Q112)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 56% coverage: 31:264/421 of query aligns to 6:233/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ T37), V17 (≠ G42), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (= T68), R128 (≠ S159), A132 (≠ E163), S134 (= S165), Q137 (≠ M168)
- binding tetrafluoroaluminate ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q112), S134 (= S165), G135 (= G166), G136 (= G167), E158 (= E189), H191 (= H222)
- binding magnesium ion: S42 (= S67), Q81 (= Q112)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 56% coverage: 31:264/421 of query aligns to 6:233/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ T37), V17 (≠ G42), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (= T68), R128 (≠ S159), A132 (≠ E163), S134 (= S165), Q137 (≠ M168)
- binding magnesium ion: S42 (= S67), Q81 (= Q112)
6z5uK Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp (see paper)
40% identity, 53% coverage: 45:266/421 of query aligns to 20:240/253 of 6z5uK
Sites not aligning to the query:
Query Sequence
>WP_011187451.1 NCBI__GCF_000025945.1:WP_011187451.1
MKKIEVRNLYKIFGPDPDKGMKLLAQGMDKQDIHEKTGMTVGVQDASFTINQGEIFVIMG
LSGSGKSTLVRTLNRLIEPTSGEILVDGENILKMDKAELVTFRRAKTGMVFQSFALMPQL
TVIENVAFGLDLDGMEKEQRLERAQDALNQVGLNGWENSYPKELSGGMQQRVGLARGLAV
DPDILLMDEAFSALDPLIRTEMQDELLKLQDQQERTIVFISHDLDEALRIGDRIAIMEGG
RVVQVGTPEEILQNPADDYVRAFFRGVDPTGVISAGDIVRDTQPTVIWHTPAGSLRATLE
LLNNRDREYAYVIGSKRTFFGVVSTDSLCDTIEADGQGKNKPKIEDAFIPEAKAVQDDES
LQDILKKVASHPWPIPVVDEDGKYRGVVSKNSFLRTLYRAENGSHFGNNPTDGTHEGEDK
C
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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