SitesBLAST
Comparing WP_050655916.1 NCBI__GCF_002893965.1:WP_050655916.1 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)
40% identity, 85% coverage: 11:535/617 of query aligns to 58:578/595 of P54582
- W101 (= W54) 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 (= E88) mutation to A: Strongly decreased betaine transport.
- G149 (= G102) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M103) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G104) mutation to A: Nearly abolishes betaine transport.
- I152 (= I105) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 105:106) binding glycine betaine
- G153 (= G106) 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 (= F109) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W147) mutation to C: Mildly decreased betaine transport.
- W194 (= W152) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y155) mutation to L: Nearly abolishes betaine transport.
- R210 (= R168) mutation to A: Nearly abolishes betaine transport.
- S253 (= S211) binding glycine betaine
- G301 (= G258) mutation to L: Strongly decreased betaine transport.
- N309 (= N266) mutation to A: Decreases affinity for sodium ions.
- T351 (= T308) 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 (= W316) mutation to C: Strongly decreased betaine transport.
- W366 (= W320) mutation to C: No effect on betaine transport.
- F369 (= F323) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W325) mutation to L: No effect on betaine transport.
- W373 (= W327) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WWMSW 327:331) binding glycine betaine
- W374 (= W328) 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 (= W331) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F334) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F338) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R341) mutation to A: Mildly decreased betaine transport.
- R392 (= R346) mutation to K: Moderately decreased betaine transport.
8ybqA Choline transporter bett - cht bound (see paper)
42% identity, 80% coverage: 10:504/617 of query aligns to 4:496/502 of 8ybqA
4llhA Substrate bound outward-open state of the symporter betp (see paper)
39% identity, 85% coverage: 10:535/617 of query aligns to 1:519/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M103), G95 (= G104), D97 (≠ G106), W314 (= W327), W315 (= W328), W318 (= W331)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (≠ Y511), R499 (≠ S515)
- binding sodium ion: A91 (≠ S100), M94 (= M103), G95 (= G104), F405 (= F421), T408 (= T424), S409 (= S425)
3p03C Crystal structure of betp-g153d with choline bound (see paper)
41% identity, 80% coverage: 10:505/617 of query aligns to 1:488/508 of 3p03C
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
25% identity, 82% coverage: 11:517/617 of query aligns to 10:514/514 of B4EY22
- E111 (= E114) mutation to A: Abolishes transport activity.
- R262 (≠ N266) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W320) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V335) mutation to V: 10-fold decrease in Vmax.
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
26% identity, 79% coverage: 11:499/617 of query aligns to 15:501/508 of 2wswA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
27% identity, 79% coverage: 11:499/617 of query aligns to 10:496/504 of P31553
- Y114 (≠ H118) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W147) binding (R)-carnitine
- D288 (≠ Q292) 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 (≠ Q299) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ E303) 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 (= T308) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ AW 319:320) binding 4-(trimethylamino)butanoate
- W316 (= W320) mutation to L: Decrease in transport activity.
- W323 (= W327) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 327:328) binding (R)-carnitine
- W324 (= W328) mutation to L: Abolishes transport activity.
- Y327 (≠ W331) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WAPF 331:334) binding (R)-carnitine
- Q330 (≠ F334) mutation to L: Decrease in transport activity.
- M331 (≠ V335) binding 4-(trimethylamino)butanoate
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
26% identity, 79% coverage: 11:499/617 of query aligns to 2:488/495 of 4m8jA
3hfxA Crystal structure of carnitine transporter (see paper)
27% identity, 79% coverage: 15:499/617 of query aligns to 3:485/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 79% coverage: 11:499/617 of query aligns to 3:489/496 of 2wsxA