SitesBLAST
Comparing WP_019895193.1 NCBI__GCF_000384235.1:WP_019895193.1 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 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 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 6 papers)
35% identity, 92% coverage: 13:514/543 of query aligns to 58:568/595 of P54582
- W101 (= W56) 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 (= E90) mutation to A: Strongly decreased betaine transport.
- G149 (= G104) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (≠ T105) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (= G106) mutation to A: Nearly abolishes betaine transport.
- I152 (≠ V107) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (≠ VG 107:108) binding glycine betaine
- G153 (= G108) 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 (= F111) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W148) mutation to C: Mildly decreased betaine transport.
- W194 (= W153) mutation to L: Strongly decreased betaine transport.
- Y197 (≠ F156) mutation to L: Nearly abolishes betaine transport.
- R210 (= R169) mutation to A: Nearly abolishes betaine transport.
- S253 (≠ T211) 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 (≠ WWLAW 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.
4llhA Substrate bound outward-open state of the symporter betp (see paper)
35% identity, 92% coverage: 13:514/543 of query aligns to 2:509/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ T105), G95 (= G106), D97 (≠ G108), W314 (= W327), W315 (= W328), W318 (= W331)
- binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (vs. gap), R499 (= R505)
- binding sodium ion: A91 (= A102), M94 (≠ T105), G95 (= G106), F405 (= F424), T408 (= T427), S409 (= S428)
3p03C Crystal structure of betp-g153d with choline bound (see paper)
35% identity, 92% coverage: 13:514/543 of query aligns to 2:508/508 of 3p03C
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
30% identity, 82% coverage: 55:499/543 of query aligns to 56:496/514 of B4EY22
- E111 (≠ Q116) 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)
30% identity, 82% coverage: 55:499/543 of query aligns to 61:501/508 of 2wswA
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
30% identity, 82% coverage: 55:499/543 of query aligns to 48:488/495 of 4m8jA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
31% identity, 83% coverage: 55:504/543 of query aligns to 56:501/504 of P31553
- Y114 (≠ Q120) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W148) binding (R)-carnitine
- D288 (≠ E292) 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 (= R303) 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 (≠ DW 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 (≠ WSPF 331:334) binding (R)-carnitine
- Q330 (≠ F334) mutation to L: Decrease in transport activity.
- M331 (≠ V335) binding 4-(trimethylamino)butanoate
3hfxA Crystal structure of carnitine transporter (see paper)
31% identity, 83% coverage: 55:504/543 of query aligns to 45:490/493 of 3hfxA
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
31% identity, 83% coverage: 55:504/543 of query aligns to 49:494/496 of 2wsxA
Query Sequence
>WP_019895193.1 NCBI__GCF_000384235.1:WP_019895193.1
MYNQATSGFFKGMNPLLTVSALFLVVLSVMAGSFYTDESALLISALRGALNPFLEWYYVV
LVAFLLFFMIWLGVGRYKNVRLGRDFEKPEFTFFSWVSMLFAAGTGVGILFWSVAQPILQ
FRENPFIDVAATDADAAVVALRLTFFHWGINGWAIFSFVALAMGYFAFRHDLPLTVRSVL
YPILKERVHGRWGDLVDLLAVFATIFGIATTLGLGVQQMNAGLESVFGWETTTQLQLIVI
GVIMTIATVSIVSGVSKGVRLLSEMNFWLSIAAVVFILTLGPTQYLIGLTVEATGDYIQN
LLRMTFHTNVTHQTEWQADWTVFFWGWWLAWSPFVGMFIARISRGRTFREFVMGVLLVPT
LITIVWIGLFGGTALFHELFGGGGVVAAVENNVSTALYVTIERLDLGWIGTMVSGLLIVL
IGTFLITSANAGTLVVNTILSGGDSNPPTLHRIIWGIFLGGLTATLLVLGGLETLQSAVI
AAAVPFSVIVVMMIVGLVKALEDERYSARAGERKTAPAEPWIVAETTDDPRDDTTAAVDK
KAS
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