SitesBLAST
Comparing WP_035702077.1 NCBI__GCF_000691145.1:WP_035702077.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 6 papers)
43% identity, 99% coverage: 5:509/510 of query aligns to 56:571/595 of P54582
- W101 (= W46) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
- E135 (= E80) mutation to A: Strongly decreased betaine transport.
- G149 (= G94) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M95) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G96) mutation to A: Nearly abolishes betaine transport.
- I152 (= I97) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 97:98) binding glycine betaine
- G153 (= G98) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
- F156 (= F101) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W137) mutation to C: Mildly decreased betaine transport.
- W194 (= W142) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y145) mutation to L: Nearly abolishes betaine transport.
- R210 (= R158) mutation to A: Nearly abolishes betaine transport.
- S253 (= S200) binding glycine betaine
- G301 (= G247) mutation to L: Strongly decreased betaine transport.
- N309 (= N255) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ L297) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
- W362 (= W307) mutation to C: Strongly decreased betaine transport.
- W366 (= W311) mutation to C: No effect on betaine transport.
- F369 (= F314) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W316) mutation to L: No effect on betaine transport.
- W373 (= W318) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 318:322) binding glycine betaine
- W374 (= W319) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
- W377 (= W322) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F325) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F329) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R332) mutation to A: Mildly decreased betaine transport.
- R392 (= R337) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
43% identity, 98% coverage: 12:509/510 of query aligns to 11:512/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M95), G95 (= G96), D97 (≠ G98), W314 (= W318), W315 (= W319), W318 (= W322)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (≠ K494), R499 (≠ K498)
- binding sodium ion: A91 (≠ S92), M94 (= M95), G95 (= G96), F405 (= F409), T408 (= T412), S409 (= S413)
3p03C Crystal structure of betp-g153d with choline bound (see paper)
43% identity, 98% coverage: 12:509/510 of query aligns to 11:508/508 of 3p03C
8ybqA Choline transporter bett - cht bound (see paper)
40% identity, 90% coverage: 37:493/510 of query aligns to 39:501/502 of 8ybqA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
30% identity, 95% coverage: 27:509/510 of query aligns to 34:511/514 of B4EY22
- E111 (= E106) mutation to A: Abolishes transport activity.
- R262 (≠ N255) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W311) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V326) mutation to V: 10-fold decrease in Vmax.
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
30% identity, 91% coverage: 27:491/510 of query aligns to 34:503/504 of P31553
- Y114 (≠ H110) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W137) binding (R)-carnitine
- D288 (= D281) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
- M295 (≠ S288) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ Q292) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
- T304 (≠ L297) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (= GW 310:311) binding 4-(trimethylamino)butanoate
- W316 (= W311) mutation to L: Decrease in transport activity.
- W323 (= W318) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 318:319) binding (R)-carnitine
- W324 (= W319) mutation to L: Abolishes transport activity.
- Y327 (≠ W322) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPF 322:325) binding (R)-carnitine
- Q330 (≠ F325) mutation to L: Decrease in transport activity.
- M331 (≠ V326) binding 4-(trimethylamino)butanoate
3hfxA Crystal structure of carnitine transporter (see paper)
30% identity, 91% coverage: 27:491/510 of query aligns to 23:492/493 of 3hfxA
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
30% identity, 90% coverage: 27:485/510 of query aligns to 39:502/508 of 2wswA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
30% identity, 90% coverage: 27:485/510 of query aligns to 26:489/495 of 4m8jA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
29% identity, 91% coverage: 27:491/510 of query aligns to 27:496/496 of 2wsxA
Query Sequence
>WP_035702077.1 NCBI__GCF_000691145.1:WP_035702077.1
MKNVSSVFWIVIAITFIAVLWGALSPDTLQNVTDQIQTYITNDFGWYYLLVVSLLVGFCL
FFIFSPIGKITLGKPGEEPEFGLFSWFAMLFSAGMGIGLVFYGAAEPISHFAIQSPTGET
ENAQAFRDSLRYTFFHWGLHAWAIYAIVALCIAYFKFRKDAPGLISSTLYPVFGNRIHGW
IGKTIDCIAVFATVVGVATSLGLGAAQINGGLNYLFGIPNNFLTQLIIIAIVTVLFLLSA
WSGIGKGIKYLSNSNMIFAALLMIFLLIVGPTVYILNSFTDSIGQYLSNIVQMSFRLSPN
DPEKREWINGWTIFYWAWWISWSPFVGIFIARVSRGRTIREFLIGVLVAPSILVFLWFSI
FGVSAMDLQQNNIVDVANMSTETMLFGVLNEYPLAMITSILALILIAVFFITSADSATFV
LGMQTTYGSLNPANSVKISWGIIQSAVAAVLLFSGGLQALQNTAKLAALPFSVVIILMIV
SLYKSLNEERRAIKQANKYNKPRSPRVKKA
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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