SitesBLAST
Comparing WP_034526228.1 NCBI__GCF_000740055.1:WP_034526228.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
3l1lA Structure of arg-bound escherichia coli adic (see paper)
29% identity, 82% coverage: 8:410/490 of query aligns to 3:383/423 of 3l1lA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 83% coverage: 2:410/490 of query aligns to 3:400/445 of P60061
- I23 (= I22) binding agmatine; binding L-arginine
- S26 (≠ G25) binding L-arginine
- Y93 (= Y95) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S98) binding agmatine; binding L-arginine
- C97 (≠ A99) binding agmatine
- N101 (= N103) binding agmatine; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
- M104 (≠ Y106) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W212) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V213) binding agmatine
- I205 (= I215) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W303) binding agmatine; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
- S357 (≠ A368) binding L-arginine; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
28% identity, 83% coverage: 2:410/490 of query aligns to 3:400/445 of P60063
- N22 (≠ S21) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (= I22) binding L-arginine
- GSG 25:27 (≠ GGG 24:26) Helix-breaking GSG motif TM1
- S26 (≠ G25) binding L-arginine; mutation to K: 5% Agm antiport.
- G27 (= G26) binding L-arginine
- Y74 (= Y76) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (≠ F89) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y95) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (≠ S98) binding L-arginine
- C97 (≠ A99) binding L-arginine
- N101 (= N103) binding L-arginine
- W202 (= W212) Periplasmic (proximal) gate; binding L-arginine
- I205 (= I215) binding L-arginine
- GVESA 206:210 (≠ GIEGA 216:220) Helix-breaking GVESA motif TM6
- E208 (= E218) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W303) binding L-arginine
- F337 (= F347) mutation to A: Severely decreased antiport.
- S357 (≠ A368) binding L-arginine
- Y365 (= Y373) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
29% identity, 82% coverage: 8:410/490 of query aligns to 5:396/437 of 5j4nA
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
25% identity, 91% coverage: 1:446/490 of query aligns to 1:437/439 of P0AAF1
- C62 (≠ L64) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ D70) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E80) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ A81) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (= K85) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W93) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y95) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W212) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E218) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ V221) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V296) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ I297) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W303) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y312) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ T319) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ I431) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y434) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
- E433 (≠ N442) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
25% identity, 78% coverage: 4:383/490 of query aligns to 2:376/444 of P0AAE8
- C12 (≠ L14) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I43) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ I45) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ K59) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F61) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y78) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- E76 (≠ A81) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y95) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- Y90 (≠ W96) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ A113) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A133) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F182) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (= D193) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T210) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E218) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (= Y248) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (≠ M259) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V296) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ E313) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ E317) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ F324) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y373) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ F375) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ A377) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 377 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 389 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 394 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 397 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 408 E→Q: Moderate decrease in cadaverine uptake.
- 423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 68% coverage: 2:333/490 of query aligns to 4:323/438 of O34739
- C94 (≠ S98) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (= C140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ M173) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A299) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 72% coverage: 6:359/490 of query aligns to 14:371/489 of P25737
- Y102 (≠ S91) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W96) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ T159) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ W212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (≠ R226) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G263) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (≠ E266) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
21% identity, 67% coverage: 8:335/490 of query aligns to 3:325/433 of 6f2wA
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
23% identity, 72% coverage: 6:358/490 of query aligns to 36:384/531 of Q9QXW9
- Y130 (≠ W100) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N103) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (≠ M207) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
23% identity, 80% coverage: 2:394/490 of query aligns to 9:396/457 of P15993
- Y103 (≠ A99) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
22% identity, 72% coverage: 6:358/490 of query aligns to 37:385/535 of Q9UHI5