SitesBLAST
Comparing WP_057687532.1 NCBI__GCF_001431535.1:WP_057687532.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 hits to proteins with known functional sites (download)
P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
38% identity, 88% coverage: 56:510/517 of query aligns to 100:547/595 of P54582
- W101 (= W57) 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 (≠ A91) mutation to A: Strongly decreased betaine transport.
- G149 (= G105) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ I106) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G107) mutation to A: Nearly abolishes betaine transport.
- I152 (= I108) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ IA 108:109) binding
- G153 (≠ A109) 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 (≠ Y112) 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 (≠ N210) binding
- G301 (= G257) mutation to L: Strongly decreased betaine transport.
- N309 (= N265) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ I307) 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 (= W317) mutation to C: Strongly decreased betaine transport.
- W366 (= W321) mutation to C: No effect on betaine transport.
- F369 (= F324) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W326) mutation to L: No effect on betaine transport.
- W373 (= W328) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (≠ WWIAW 328:332) binding
- W374 (= W329) 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 (= W332) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (= F335) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F339) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R342) mutation to A: Mildly decreased betaine transport.
- R392 (= R347) mutation to K: Moderately decreased betaine transport.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
38% identity, 88% coverage: 56:510/517 of query aligns to 44:488/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I106), G95 (= G107), D97 (≠ A109), W314 (= W328), W315 (= W329), W318 (= W332)
- binding sodium ion: A91 (≠ S103), M94 (≠ I106), G95 (= G107), F405 (≠ L423), T408 (= T426), S409 (≠ P427)
Sites not aligning to the query:
3p03C Crystal structure of betp-g153d with choline bound (see paper)
38% identity, 88% coverage: 56:510/517 of query aligns to 44:487/508 of 3p03C
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
29% identity, 92% coverage: 18:494/517 of query aligns to 6:477/495 of 4m8jA
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
29% identity, 92% coverage: 18:494/517 of query aligns to 19:490/508 of 2wswA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
28% identity, 92% coverage: 18:494/517 of query aligns to 14:485/514 of B4EY22
- E111 (= E117) mutation to A: Abolishes transport activity.
- R262 (≠ N265) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W321) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V336) mutation to V: 10-fold decrease in Vmax.
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
28% identity, 92% coverage: 18:494/517 of query aligns to 7:478/496 of 2wsxA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 92% coverage: 18:494/517 of query aligns to 14:485/504 of P31553
- Y114 (≠ D120) binding ; mutation to L: Small decrease in transport activity.
- W142 (= W147) binding
- D288 (≠ Q291) 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 (≠ A298) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (= R302) 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 (≠ L309) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (≠ SW 320:321) binding
- W316 (= W321) mutation to L: Decrease in transport activity.
- W323 (= W328) binding ; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 328:329) binding
- W324 (= W329) mutation to L: Abolishes transport activity.
- Y327 (≠ W332) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WAPF 332:335) binding
- Q330 (≠ F335) mutation to L: Decrease in transport activity.
- M331 (≠ V336) binding
3hfxA Crystal structure of carnitine transporter (see paper)
28% identity, 92% coverage: 18:494/517 of query aligns to 3:474/493 of 3hfxA
Query Sequence
>WP_057687532.1 NCBI__GCF_001431535.1:WP_057687532.1
MSSKASSAPSPLRLNGFVFFSSALSIGVLGLLTVLNPQASEHWLQVAQAQVSAAFGWWYM
LLIVACLGFVLWLAFSRYGSIRLGHNEESPAFAYVPWVSMLFSAGIGIALLYYGAYEPLD
HFLTPPGQQGGTVAASREAMVLTFLHWGLHGWALYALVGVALGYFAYRRSLPLALRSALY
PIFGERIHGRIGDMVDGFGILATLVSMVTNLGIGALVVQSGLTYLFKMPDTPQTLVVIVL
VMMVVATIGVVAGVEKGIAWLSNLNVRLLCLLLLFVLVTGPTLHLLDGLVQNTGDYLASF
VRKSFDIYLNQPDGRDWLGSWTLFYWAWWIAWAPFVGLFVARISRGRTIREVILGVLLIP
LGFTLAWLSIFGNTAIDLVLNHGQAVLGEVAKADAAMTLFKLLEYLPWAPYVAGAAVLIG
FVLFLTPVDSGTLMIANLCTRRVDGGVEDGHDAPIWLRVFWAVVITVVSIGLLLAGNFGA
MQTAVVLCGLPFSFTLAFYMVGLLRALRTDPDAPHRH
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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