SitesBLAST
Comparing WP_012169059.1 NCBI__GCF_000010525.1:WP_012169059.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AAI3 ATP-dependent zinc metalloprotease FtsH; Cell division protease FtsH; EC 3.4.24.- from Escherichia coli (strain K12) (see 4 papers)
58% identity, 99% coverage: 6:638/640 of query aligns to 3:624/644 of P0AAI3
- L201 (= L205) mutation to N: No in vivo protease activity, no in vitro ATPase activity.
- F225 (= F229) mutation F->A,D,E,G,N,Q,R,S,T: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo.; mutation F->C,H: Partially complements ftsH1 at 42 degrees Celsius, some protease activity in vivo.; mutation F->I,L,M,V,W,Y: Complements ftsH1 at 42 degrees Celsius, restores protease activity in vivo.
- G227 (= G231) mutation to A: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo.
- T297 (= T301) mutation to A: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius.
- N298 (= N302) mutation to A: No in vivo protease activity.
- D304 (= D308) mutation D->A,N: No in vivo protease activity, no in vitro ATPase activity; probably still binds ATP.; mutation to E: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius.
- L307 (= L311) mutation to A: Low protease activity in vivo.
- R309 (= R313) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- R312 (= R316) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- H414 (= H418) mutation to Y: Loss of protease function.
- E415 (= E419) mutation to Q: Loss of protease activity in vivo.
- H418 (= H422) mutation to Y: In tolZ21; loss of protease function in vivo, retains about 25% ATPase activity, temperature sensitive.
- E463 (≠ T467) mutation to K: In ftsH1; a temperature-sensitive mutant which increases the frequency of lysogenization of phage lambda; when associated with A-587.
- E476 (= E480) mutation E->D,K,V: Severe loss of protease function that is restored by excess Zn.; mutation to Q: Little effect on protease function.
- H536 (≠ N540) mutation to R: In hflB29; increases the frequency of lysogenization of phage lambda.
- E582 (= E586) mutation E->D,K,Q: No effect on protease function.; mutation to V: Decreased protease function.
Q9WZ49 ATP-dependent zinc metalloprotease FtsH; EC 3.4.24.- from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see 2 papers)
52% identity, 93% coverage: 1:598/640 of query aligns to 1:602/610 of Q9WZ49
- G164 (≠ A159) binding ATP
- GTGKT 204:208 (= GTGKT 199:203) binding ATP
- L209 (= L204) binding ATP
- H343 (= H338) binding ATP
- E371 (≠ A366) binding ATP
- G404 (= G399) mutation to L: Complete loss of protease activity and of oligomerization.
- H423 (= H418) binding Zn(2+)
- E424 (= E419) active site
- H427 (= H422) binding Zn(2+)
- D500 (= D496) binding Zn(2+); mutation to A: Complete loss of protease activity.
P37476 ATP-dependent zinc metalloprotease FtsH; Cell division protease FtsH; EC 3.4.24.- from Bacillus subtilis (strain 168) (see paper)
51% identity, 95% coverage: 1:605/640 of query aligns to 1:610/637 of P37476
- K207 (= K202) mutation to N: Does not complement an ftsH deletion, loss of ATPase activity.
- E424 (= E419) mutation to Q: Does not complement an ftsH deletion, loss of protease activity against casein.
Q5SI82 ATP-dependent zinc metalloprotease FtsH; EC 3.4.24.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
52% identity, 93% coverage: 8:601/640 of query aligns to 6:595/624 of Q5SI82
- G399 (= G399) mutation to L: No effect on protease activity against alpha-casein.
3kdsE Apo-ftsh crystal structure (see paper)
57% identity, 70% coverage: 152:598/640 of query aligns to 2:426/427 of 3kdsE
7wi4B Cryo-em structure of e.Coli ftsh protease cytosolic domains (see paper)
56% identity, 72% coverage: 145:602/640 of query aligns to 1:407/410 of 7wi4B
- binding phosphoaminophosphonic acid-adenylate ester: V14 (= V158), A15 (= A159), P54 (= P198), G55 (= G199), G57 (= G201), K58 (= K202), T59 (= T203), L60 (= L204)
- binding magnesium ion: A79 (= A234), S80 (= S235)
- binding zinc ion: H236 (= H418), H240 (= H422), D314 (= D496)
7wi4A Cryo-em structure of e.Coli ftsh protease cytosolic domains (see paper)
56% identity, 72% coverage: 145:602/640 of query aligns to 1:407/410 of 7wi4A
- binding phosphoaminophosphonic acid-adenylate ester: A15 (= A159), P54 (= P198), G55 (= G199), T56 (= T200), G57 (= G201), K58 (= K202), T59 (= T203), L60 (= L204), H156 (= H338)
- binding zinc ion: H236 (= H418), H240 (= H422), D314 (= D496)
Q9FGM0 ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial; AtFTSH11; EC 3.4.24.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
52% identity, 78% coverage: 96:597/640 of query aligns to 289:784/806 of Q9FGM0
- G564 (= G362) mutation to A: In atts244; loss of thermotolerance.
2dhrA Whole cytosolic region of atp-dependent metalloprotease ftsh (g399l) (see paper)
58% identity, 72% coverage: 142:601/640 of query aligns to 1:453/458 of 2dhrA