SitesBLAST
Comparing WP_041277635.1 NCBI__GCF_000025945.1:WP_041277635.1 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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
39% identity, 91% coverage: 42:521/525 of query aligns to 67:547/595 of P54582
- W101 (≠ L73) 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 (≠ D107) mutation to A: Strongly decreased betaine transport.
- G149 (= G121) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
- M150 (= M122) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
- G151 (≠ A123) mutation to A: Nearly abolishes betaine transport.
- I152 (= I124) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
- IG 152:153 (= IG 124:125) binding glycine betaine
- G153 (= G125) 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 (= F128) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
- W189 (= W167) mutation to C: Mildly decreased betaine transport.
- W194 (= W172) mutation to L: Strongly decreased betaine transport.
- Y197 (= Y175) mutation to L: Nearly abolishes betaine transport.
- R210 (≠ N188) mutation to A: Nearly abolishes betaine transport.
- S253 (= S230) binding glycine betaine
- G301 (= G277) mutation to L: Strongly decreased betaine transport.
- N309 (= N285) mutation to A: Decreases affinity for sodium ions.
- T351 (≠ H326) 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 (= W333) mutation to C: Strongly decreased betaine transport.
- W366 (= W337) mutation to C: No effect on betaine transport.
- F369 (= F340) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
- W371 (= W342) mutation to L: No effect on betaine transport.
- W373 (= W344) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
- WWISW 373:377 (= WWISW 344:348) binding glycine betaine
- W374 (= W345) 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 (= W348) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
- F380 (≠ C351) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- F384 (= F355) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
- R387 (= R358) mutation to A: Mildly decreased betaine transport.
- R392 (= R363) mutation to K: Moderately decreased betaine transport.
3p03C Crystal structure of betp-g153d with choline bound (see paper)
39% identity, 91% coverage: 42:521/525 of query aligns to 11:487/508 of 3p03C
4llhA Substrate bound outward-open state of the symporter betp (see paper)
39% identity, 91% coverage: 42:521/525 of query aligns to 11:488/524 of 4llhA
- binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (= M122), G95 (≠ A123), D97 (≠ G125), W314 (= W344), W315 (= W345), W318 (= W348)
- binding sodium ion: A91 (= A119), M94 (= M122), G95 (≠ A123), F405 (= F438), T408 (= T441), S409 (= S442)
Sites not aligning to the query:
3hfxA Crystal structure of carnitine transporter (see paper)
29% identity, 79% coverage: 75:490/525 of query aligns to 44:462/493 of 3hfxA
P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
29% identity, 79% coverage: 75:490/525 of query aligns to 55:473/504 of P31553
- Y114 (≠ A136) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
- W142 (= W167) binding (R)-carnitine
- D288 (≠ T310) 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 (vs. gap) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
- R299 (≠ N318) 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 (≠ S323) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
- GW 315:316 (= GW 336:337) binding 4-(trimethylamino)butanoate
- W316 (= W337) mutation to L: Decrease in transport activity.
- W323 (= W344) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
- WW 323:324 (= WW 344:345) binding (R)-carnitine
- W324 (= W345) mutation to L: Abolishes transport activity.
- Y327 (≠ W348) mutation to L: Strong decrease in transport activity.
- YAIQ 327:330 (≠ WSPC 348:351) binding (R)-carnitine
- Q330 (≠ C351) mutation to L: Decrease in transport activity.
- M331 (≠ V352) binding 4-(trimethylamino)butanoate
2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
29% identity, 79% coverage: 75:490/525 of query aligns to 48:466/496 of 2wsxA
B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
29% identity, 77% coverage: 89:490/525 of query aligns to 69:473/514 of B4EY22
- E111 (= E133) mutation to A: Abolishes transport activity.
- R262 (≠ N285) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
- W316 (= W337) mutation to A: 2.5-fold decrease in Vmax.
- M331 (≠ V352) mutation to V: 10-fold decrease in Vmax.
2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
29% identity, 77% coverage: 89:490/525 of query aligns to 74:478/508 of 2wswA
Sites not aligning to the query:
4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
29% identity, 77% coverage: 89:490/525 of query aligns to 61:465/495 of 4m8jA
Query Sequence
>WP_041277635.1 NCBI__GCF_000025945.1:WP_041277635.1
MKQGRGKYSIDTTDYTIGQDNIQKWGFDVHNIVFGVSAGLILLFLLATLFSDPHTAKMAL
DGVKWKIIANFDLLFIWSVNIFVLFCLGLIVSPYGKIRLGGDDAVPDYSVCSWLAMLFAA
GMAIGLMFWSVAEPVAYFTGWYKTPLNVVPNSPEAARLAMGATMFHWGLHPWATYAVVGL
SLAYFTYNKGLPLSIRSIFYPILGERAWGWAGHIVDILAVLATLFGLATSLGLGAQQAAS
GINNVFGLENTIGLQIGVICGVTLLATISVVRGIEGGVKVLSNINMIIAFFLLVAVIVLG
GGVVLKSLPTTMGAYLENIIPLSNPHGREDQAWFQGWTVFYWAWWISWSPCVGMFIARVS
KGRTIRQFLIAVLIVPTLVTFVWMSTFGGIAIDQVVRGVGALGTEGLKSVPLAMFQMFDV
LPFSNFLSIIGIILVLVFFITSSDSASLVIDSITAGGKVEAPVPQRVFWALTEGAIAAAL
LWVGGTEAIQALQAGAICTALPFTVIILFMCLSLILGLRTEPRKL
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