SitesBLAST
Comparing WP_057508273.1 NCBI__GCF_001431535.1:WP_057508273.1 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)
8dmmA Structure of the vanadate-trapped msba bound to kdl (see paper)
41% identity, 99% coverage: 4:577/582 of query aligns to 1:576/576 of 8dmmA
- binding adp orthovanadate: Y347 (= Y350), R350 (≠ D353), S374 (= S377), G375 (= G378), S376 (= S379), G377 (= G380), K378 (= K381), S379 (≠ T382), T380 (≠ S383), Q420 (= Q423), L476 (= L477), S478 (= S479), G479 (= G480), G480 (= G481), H533 (= H534)
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid: V25 (≠ A28), Y79 (≠ L82), Y83 (= Y86), R184 (= R187), R234 (≠ L237), K239 (= K242), I246 (≠ F249), I250 (≠ T253)
P60752 ATP-dependent lipid A-core flippase; Lipid A export ATP-binding/permease protein MsbA; Lipid flippase; EC 7.5.2.6 from Escherichia coli (strain K12) (see 7 papers)
41% identity, 99% coverage: 2:577/582 of query aligns to 3:580/582 of P60752
- C88 (≠ T87) mutation to S: Does not affect ATPase activity.
- E208 (= E207) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates. Inhibits formation of outward-facing conformation.; mutation to C: Exhibits ATPase activity. Forms intermolecular cross-links.; mutation to Q: Improves basal ATPase activity and increases transport activity.
- K212 (≠ S211) mutation to A: Does not reduce substrate binding or nucleotide binding, but decreases ATP-dependent extrusion of substrates.
- A270 (= A269) mutation to T: Temperature-sensitive. Loss of lipid export to the outer membrane. Significantly decreases ATPase activity at 42 degrees Celsius but not at 30 degrees Celsius.
- C315 (≠ A314) mutation to S: Does not affect ATPase activity.
- E506 (= E503) mutation to Q: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
- L511 (= L508) mutation to P: Loss of ATPase activity; ATP is still bound.
- D512 (= D509) mutation to G: Loss of ATPase activity; ATP is still bound.
- H537 (= H534) mutation to A: Lacks cell viability and does not support growth. Can still bind ATP and slowly hydrolyze ATP, but becomes locked into a closed dimer conformation.
6bppA E. Coli msba in complex with lps and inhibitor g092 (see paper)
41% identity, 98% coverage: 4:576/582 of query aligns to 2:576/576 of 6bppA
- binding (2E)-3-{6-[(1S)-1-(3-amino-2,6-dichlorophenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: L168 (≠ M170), A172 (≠ V174), V175 (≠ I177), S176 (≠ G178), I179 (≠ V181), A256 (= A258), M288 (= M290), L291 (≠ I293), M292 (≠ I294), K296 (≠ R298)
6bplA E. Coli msba in complex with lps and inhibitor g907 (see paper)
41% identity, 98% coverage: 4:576/582 of query aligns to 2:576/576 of 6bplA
- binding (2E)-3-{6-[(1S)-1-(2-chloro-6-cyclopropylphenyl)ethoxy]-4-cyclopropylquinolin-3-yl}prop-2-enoic acid: F154 (≠ L156), L168 (≠ M170), V175 (≠ I177), S176 (≠ G178), I179 (≠ V181), A256 (= A258), M288 (= M290), L291 (≠ I293), M292 (≠ I294), L295 (= L297), K296 (≠ R298)
7ph3A Amp-pnp bound nanodisc reconstituted msba with nanobodies, spin- labeled at position a60c (see paper)
41% identity, 99% coverage: 2:576/582 of query aligns to 1:577/577 of 7ph3A
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y350), S376 (= S377), G377 (= G378), G379 (= G380), K380 (= K381), S381 (≠ T382), T382 (≠ S383), Q422 (= Q423), L478 (= L477), S480 (= S479), G482 (= G481), Q483 (= Q482), H535 (= H534)
- binding magnesium ion: S381 (≠ T382), Q422 (= Q423)
7mewA E. Coli msba in complex with g247 (see paper)
41% identity, 98% coverage: 9:576/582 of query aligns to 3:572/572 of 7mewA
7bcwA Structure of msba in salipro with adp vanadate (see paper)
41% identity, 98% coverage: 9:576/582 of query aligns to 5:574/574 of 7bcwA
- binding adenosine-5'-diphosphate: Y346 (= Y350), G374 (= G378), S375 (= S379), K377 (= K381), S378 (≠ T382), T379 (≠ S383), L475 (= L477), S477 (= S479), Q480 (= Q482)
- binding magnesium ion: S378 (≠ T382), Q419 (= Q423)
- binding vanadate ion: S373 (= S377), K377 (= K381), S477 (= S479), A505 (= A507), H532 (= H534)
7ph2A Nanodisc reconstituted msba in complex with nanobodies, spin-labeled at position a60c (see paper)
41% identity, 97% coverage: 12:577/582 of query aligns to 2:569/569 of 7ph2A
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3,5-bis(oxidanyl)oxan-2-yl]oxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-4-[(3~{R})-3-nonanoyloxytetradecanoyl]oxy-5-[[(3~{R})-3-octanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{S},5~{S},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanylnonanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-oxan-2-yl]methoxy]-5-oxidanyl-oxane-2-carboxylic acid: D30 (≠ G40), L37 (≠ M47), F277 (≠ M287), A282 (= A292), R285 (≠ P295)
7selA E. Coli msba in complex with lps and inhibitor g7090 (compound 3) (see paper)
41% identity, 98% coverage: 4:576/582 of query aligns to 2:575/575 of 7selA
- binding (2E)-3-{7-[(1S)-1-(2,6-dichloro-3-fluorophenyl)ethoxy]-1-methylnaphthalen-2-yl}prop-2-enoic acid: L168 (≠ M170), A172 (≠ V174), S176 (≠ G178), I179 (≠ V181), I252 (≠ V254), A256 (= A258), M288 (= M290), L291 (≠ I293), L295 (= L297), K296 (≠ R298)
- binding (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid: R75 (= R77), R293 (≠ P295)
8gk7A Msba bound to cerastecin c
39% identity, 97% coverage: 11:573/582 of query aligns to 2:563/564 of 8gk7A
- binding phosphoaminophosphonic acid-adenylate ester: Y339 (= Y350), T343 (≠ G355), S365 (= S377), G366 (= G378), G368 (= G380), K369 (= K381), T370 (= T382), N467 (≠ L477), L468 (= L478), S469 (= S479), G470 (= G480), G471 (= G481)
- binding 2-[(4-butylbenzene-1-sulfonyl)amino]-5-[(3-{4-[(4-butylbenzene-1-sulfonyl)amino]-3-carboxyanilino}-3-oxopropyl)carbamoyl]benzoic acid: V34 (≠ F43), I60 (= I70), R67 (= R77), M248 (≠ A258), M252 (≠ L262), I277 (≠ M287), T278 (= T288), A280 (≠ M290), G281 (≠ M291), S284 (≠ I294)
7metA A. Baumannii msba in complex with tbt1 decoupler (see paper)
39% identity, 97% coverage: 11:573/582 of query aligns to 1:562/564 of 7metA
2onjA Structure of the multidrug abc transporter sav1866 from s. Aureus in complex with amp-pnp (see paper)
31% identity, 97% coverage: 13:576/582 of query aligns to 3:576/578 of 2onjA
- binding phosphoaminophosphonic acid-adenylate ester: Y349 (= Y350), I356 (≠ A357), S376 (= S377), G377 (= G378), G378 (≠ S379), G379 (= G380), K380 (= K381), S381 (≠ T382), T382 (≠ S383), Q422 (= Q423), K477 (≠ L477), S479 (= S479), G480 (= G480), E503 (= E503), H534 (= H534)
2hydA Multidrug abc transporter sav1866 (see paper)
31% identity, 97% coverage: 13:576/582 of query aligns to 3:576/578 of 2hydA
Q9NP78 ABC-type oligopeptide transporter ABCB9; ATP-binding cassette sub-family B member 9; ATP-binding cassette transporter 9; ABC transporter 9 protein; hABCB9; TAP-like protein; TAPL; EC 7.4.2.6 from Homo sapiens (Human) (see 4 papers)
33% identity, 97% coverage: 13:576/582 of query aligns to 175:741/766 of Q9NP78
- K545 (= K381) mutation to A: Loss of peptide transport activity; whena ssociated with A-699.
- H699 (= H534) mutation to A: Loss of peptide transport activity; whena ssociated with A-545.
Sites not aligning to the query:
- 17 Intramolecular salt bridge with Arg-57. Essential for the release from the ER; D→N: Loss of lysosomal localization. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect dimerization. Does not affect peptide transport activity. Decreases interaction with YIF1B.; D→R: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-100.
- 45 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-49. Loss of lysosomal localization; when assosiated with K-49 and D-100. Does not affect peptide transport activity; when assosiated with K-49 and D-100.; D→N: Decreases lysosomal localization; when associated with N-49.
- 49 Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments; D→K: Loss of lysosomal localization; when assosiated with K-45. Loss of lysosomal localization; when assosiated with K-45 and D-100. Does not affect peptide transport activity; when assosiated with K-45 and D-100.; D→N: Decreases lysosomal localization; when associated with N-45.
- 57 Intramolecular salt bridge with Asp-17. Essential for the release from the ER; R→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-100.; R→D: Loss of lysosomal localization. Does not affect lysosomal localization; when associated with R-17. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
- 100 K→A: Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-57.; K→D: Decreases lysosomal localization. Loss of lysosomal localization; when assosiated with R-17. Loss of lysosomal localization; when assosiated with K-45 and K-49. Does not affect peptide transport activity; when assosiated with K-45 and K-49. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.
- 121 V → M: in dbSNP:rs3803002
- 136:137 LL→AA: No effect on lysosomal localization.
7vfiA Cryo-em structure of the mouse tapl (9mer-peptide bound) (see paper)
33% identity, 97% coverage: 13:576/582 of query aligns to 3:569/570 of 7vfiA
7v5cA Cryo-em structure of the mouse abcb9 (adp.Bef3-bound) (see paper)
33% identity, 97% coverage: 13:576/582 of query aligns to 4:570/572 of 7v5cA
- binding adenosine-5'-diphosphate: Y342 (= Y350), T344 (≠ E352), S372 (= S379), K374 (= K381), S375 (≠ T382), S376 (= S383), S473 (= S479), Q476 (= Q482)
- binding beryllium trifluoride ion: S370 (= S377), K374 (= K381), Q416 (= Q423), H528 (= H534)
- binding magnesium ion: S375 (≠ T382), Q416 (= Q423)
O06967 Multidrug resistance ABC transporter ATP-binding/permease protein BmrA; EC 7.6.2.- from Bacillus subtilis (strain 168) (see 2 papers)
36% identity, 87% coverage: 73:578/582 of query aligns to 73:579/589 of O06967
- K380 (= K381) mutation to A: Complete loss of ATPase activity.; mutation to R: Retains 2% ATPase activity; unable to transport Hoechst 33342. Traps ADP in a beryllium fluoride-dependent manner, confirming ATPase activity. Probably unable to undergo NBD dimerization.
- E504 (= E503) mutation E->A,C,D,Q,S: Complete loss of ATPase activity; mutant proteins trap ATP in a vanadate-independent manner whereas the wild-type protein traps ADP.
7ow8A Cryoem structure of the abc transporter bmra e504a mutant in complex with atp-mg (see paper)
35% identity, 87% coverage: 73:578/582 of query aligns to 64:570/577 of 7ow8A
- binding adenosine-5'-triphosphate: D107 (= D116), Y341 (= Y350), S367 (= S377), G368 (= G378), G370 (= G380), K371 (= K381), T372 (= T382), T373 (≠ S383), Q413 (= Q423), I468 (≠ A476), S471 (= S479), G473 (= G481), H526 (= H534)
- binding magnesium ion: T372 (= T382), Q413 (= Q423)
7bg4A Multidrug resistance transporter bmra mutant e504a bound with atp, mg, and rhodamine 6g solved by cryo-em (see paper)
36% identity, 87% coverage: 73:578/582 of query aligns to 65:562/572 of 7bg4A
- binding adenosine-5'-triphosphate: Y333 (= Y350), S359 (= S377), G360 (= G378), G361 (≠ S379), K363 (= K381), T364 (= T382), T365 (≠ S383), Q405 (= Q423), I460 (≠ A476), M461 (≠ L477), S463 (= S479), G464 (= G480), G465 (= G481)
- binding magnesium ion: T364 (= T382), Q405 (= Q423)
- binding rhodamine 6g: L250 (≠ W267), I277 (= I294)
7metB A. Baumannii msba in complex with tbt1 decoupler (see paper)
51% identity, 51% coverage: 280:573/582 of query aligns to 160:453/455 of 7metB
Sites not aligning to the query:
Query Sequence
>WP_057508273.1 NCBI__GCF_001431535.1:WP_057508273.1
MSSKHAPVWPIYKRLLGYTRAYWVFMVAAVVAMAVEALAGYAFTRLMEPLVNRGFVNPEP
RMAVILPLTILGLFLMRSLATLVSDYTLARTGRSVVRDLREQVLEKYLHLPSSHFDTEAT
PVMVSRLNFDTEQVTQASADALKTLVADTLTIIAMLVVMLQMSVKVTMAMLVVVPMIGLI
VSYVGKRYRRISRGIQDGMGTMAATAEQSLSAQQEVKVHGTQRHEIDRYSRLANRMLGLN
MKVETTRAFASSTVQFLAALALAVIVWVATREALVGKLNAGQFMGLMTSMMAIIPSLRRL
TSVQTSISRGVAAAERLFSILDMPVERDQGSKRIERARGELAFEHVMLRYREDAGTALDD
ISFVARPGTVTAVVGRSGSGKTSLIRLVPRFYEPSGGRITLDGVALDDYPLADLRRQVAM
VGQKVMLFDDTIGSNIAYGMQASQEQIRAAAEAANAWEFIARLPQQLDTPVGENGALLSG
GQRQRLAIARAILRDAPILILDEATAALDNESERLVQDALQRLMPERTTLVIAHRLSTIE
HADQVLVMDQGRIVERGTHAELLQMGGLYEHLYNMQFRERQA
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