SitesBLAST
Comparing SMa1668 FitnessBrowser__Smeli:SMa1668 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 10 hits to proteins with known functional sites (download)
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 89% coverage: 2:420/473 of query aligns to 7:413/445 of P60061
- I23 (≠ M18) binding ; binding
- S26 (≠ A21) binding
- Y93 (= Y91) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ G94) binding ; binding
- C97 (≠ S95) binding
- N101 (= N99) binding ; 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 (≠ Y102) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F206) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V207) binding
- I205 (= I209) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W297) binding ; 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 (≠ T359) binding ; 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)
26% identity, 89% coverage: 2:420/473 of query aligns to 7:413/445 of P60063
- N22 (≠ S17) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M18) binding
- GSG 25:27 (≠ GAG 20:22) Helix-breaking GSG motif TM1
- S26 (≠ A21) binding ; mutation to K: 5% Agm antiport.
- G27 (= G22) binding
- Y74 (≠ F72) 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 (≠ F85) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y91) 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 (≠ G94) binding
- C97 (≠ S95) binding
- N101 (= N99) binding
- W202 (≠ F206) Periplasmic (proximal) gate; binding
- I205 (= I209) binding
- GVESA 206:210 (≠ GIEGA 210:214) Helix-breaking GVESA motif TM6
- E208 (= E212) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W297) binding
- F337 (= F341) mutation to A: Severely decreased antiport.
- S357 (≠ T359) binding
- Y365 (= Y367) 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)
26% identity, 89% coverage: 2:420/473 of query aligns to 3:409/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
27% identity, 89% coverage: 2:420/473 of query aligns to 1:396/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
24% identity, 93% coverage: 2:441/473 of query aligns to 4:431/444 of P0AAE8
- C12 (≠ L10) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ A39) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ I41) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ R55) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F57) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y74) 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 (= E77) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y91) 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 (≠ W92) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ T109) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ V123) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F178) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ L193) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T204) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E212) 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 (≠ G237) 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 (≠ L248) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V290) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ V307) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ T311) 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 (≠ F318) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y367) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ V370) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ A372) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (= E382) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ I397) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ A402) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ T405) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (≠ V417) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (≠ W433) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
22% identity, 91% coverage: 2:431/473 of query aligns to 6:425/439 of P0AAF1
- C62 (≠ L60) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K64) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ K76) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ E77) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ D81) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ F89) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y91) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (≠ F206) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E212) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (vs. gap) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V290) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L291) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W297) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y306) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ D313) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ T428) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y431) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
Sites not aligning to the query:
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 65% coverage: 7:315/473 of query aligns to 15:313/438 of O34739
- C94 (≠ S87) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ S130) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A164) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A293) 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.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
22% identity, 81% coverage: 1:382/473 of query aligns to 8:387/469 of P46349
- G33 (≠ L26) mutation to D: Lack of activity.
- G42 (= G35) mutation to S: Lack of activity.
- G301 (≠ W297) mutation to V: Lack of activity.
- G338 (≠ T334) mutation to E: Lack of activity.
- F341 (≠ V337) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 67% coverage: 1:315/473 of query aligns to 1:308/433 of 6f2wA
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 78% coverage: 1:371/473 of query aligns to 13:390/489 of P25737
- Y102 (= Y91) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ S95) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ T155) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F206) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E212) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (≠ A214) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E257) 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 (≠ A260) 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.
Query Sequence
>SMa1668 FitnessBrowser__Smeli:SMa1668
MAQKLSLFALTGMVVGSMVGAGIFSLPRTFGVATGPFGAIIAWCIAGGGMYMLARVFQSL
AERKPDLDAGVFAYAKEGFGDYPGFLSAFGYWIGSCIGNVSYWVLIKSTLGNFFPVFGDG
NTVVAILFASVGIWLFHFMILRGIQQAAFVNTVVTVAKVIPIIAFIIILFFFFKLDLFRL
NFWGGEGMPEATLLQQIQATMLATVFVFIGIEGASNYSRYAQARSDIGTATIMGFIGVSA
LMVLVTLLPYAALTRPEIAAMSQPSMAGVLAAVVGPWGAVFISIGVIVSVLGAYLAWSLV
CAEVLYVAARTDDMPRLFGTENQNKVPAAALWLTNIVVQLFVISTYWSQDAFALMLNLTS
SMSLIPYMFVAAFGFMLAQRAETYEVRPRERTRDLIIASIAAVYTFFMIVAGGIKFVLLS
ALLYAPGTILYFWARRERGKRVFNTSIDWLIFATAVIGCFAAIIGLSTGYLTI
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