SitesBLAST
Comparing WP_012504720.1 NCBI__GCF_000020625.1:WP_012504720.1 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)
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)
47% identity, 88% coverage: 26:638/699 of query aligns to 7:603/610 of Q9WZ49
- G164 (≠ A200) binding ATP
- GTGKT 204:208 (= GTGKT 240:244) binding ATP
- L209 (= L245) binding ATP
- H343 (= H380) binding ATP
- E371 (≠ A408) binding ATP
- G404 (= G441) mutation to L: Complete loss of protease activity and of oligomerization.
- H423 (= H460) binding Zn(2+)
- E424 (= E461) active site
- H427 (= H464) binding Zn(2+)
- D500 (= D537) 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)
49% identity, 87% coverage: 29:636/699 of query aligns to 9:601/637 of P37476
- K207 (= K243) mutation to N: Does not complement an ftsH deletion, loss of ATPase activity.
- E424 (= E461) mutation to Q: Does not complement an ftsH deletion, loss of protease activity against casein.
P0AAI3 ATP-dependent zinc metalloprotease FtsH; Cell division protease FtsH; EC 3.4.24.- from Escherichia coli (strain K12) (see 4 papers)
46% identity, 88% coverage: 27:642/699 of query aligns to 4:603/644 of P0AAI3
- L201 (= L246) mutation to N: No in vivo protease activity, no in vitro ATPase activity.
- F225 (= F270) 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 (= G272) mutation to A: Does not complement ftsH1 at 42 degrees Celsius, no protease activity in vivo.
- T297 (= T343) mutation to A: Low protease activity in vivo, low ATPase activity in vitro, complements ftsH1 at 42 degrees Celsius.
- N298 (= N344) mutation to A: No in vivo protease activity.
- D304 (= D350) 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 (= L353) mutation to A: Low protease activity in vivo.
- R309 (= R355) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- R312 (= R358) mutation R->A,L,K: No in vivo protease activity, no ATPase activity in vitro; probably still binds ATP.
- H414 (= H460) mutation to Y: Loss of protease function.
- E415 (= E461) mutation to Q: Loss of protease activity in vivo.
- H418 (= H464) mutation to Y: In tolZ21; loss of protease function in vivo, retains about 25% ATPase activity, temperature sensitive.
- E463 (≠ F510) mutation to K: In ftsH1; a temperature-sensitive mutant which increases the frequency of lysogenization of phage lambda; when associated with A-587.
- E476 (= E523) 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 (≠ K579) mutation to R: In hflB29; increases the frequency of lysogenization of phage lambda.
- E582 (= E625) mutation E->D,K,Q: No effect on protease function.; mutation to V: Decreased protease function.
P39925 Mitochondrial inner membrane m-AAA protease component YTA10; ATPase family gene 3 protein; Tat-binding homolog 10; EC 3.4.24.-; EC 3.6.-.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
52% identity, 72% coverage: 150:653/699 of query aligns to 231:746/761 of P39925
- K334 (= K243) mutation to A: Slightly impaired respiratory growth. Impaired maturation of CCP1.
- M360 (= M269) mutation to K: Slightly decreased ATPase activity, highly impaired maturation of CCP1.
- F361 (= F270) mutation F->A,E: Decreased ATPase activity and maturation of CCP1.
- G363 (= G272) mutation to A: Impaired maturation of CCP1.
- E388 (= E297) mutation to Q: Abolished ATPase activity, leading to impaired respiratory growth. Does not affect the protease activity.
- R447 (= R355) mutation R->G,K: Suppressor mutation; able to complement a mutation in the Walker B motif of YTA12.
- E559 (= E461) mutation to Q: Abolishes proteolytic activity; impairs synthesis of respiratory chain proteins COB and COX1. No effect on m-AAA protease assembly. Decreased ATPase activity and maturation of CCP1.
- D634 (= D537) mutation to A: Does not affect maturation of CCP1.
Q8JZQ2 Mitochondrial inner membrane m-AAA protease component AFG3L2; AFG3-like protein 2; EC 3.4.24.-; EC 3.6.-.- from Mus musculus (Mouse) (see 3 papers)
46% identity, 88% coverage: 29:640/699 of query aligns to 144:748/802 of Q8JZQ2
- R389 (= R279) to G: in par
- E574 (= E461) mutation to Q: Absence of proteolytic activity. Loss of its processing into the mature form.
- M665 (= M554) mutation to R: Knockin heterozygous mice develop normally but adult mice show signs of cerebellar ataxia. Cells from mutant mice display altered mitochondrial bioenergetics, with decreased basal oxygen consumption rate, ATP synthesis and mitochondrial membrane potential. Mitochondrial network formation and morphology is also altered, with greatly reduced expression of fusogenic Opa1 isoforms.
Sites not aligning to the query:
- 1:38 modified: transit peptide, Mitochondrion
3kdsE Apo-ftsh crystal structure (see paper)
56% identity, 64% coverage: 193:638/699 of query aligns to 2:427/427 of 3kdsE
Q9Y4W6 Mitochondrial inner membrane m-AAA protease component AFG3L2; AFG3-like protein 2; Paraplegin-like protein; EC 3.4.24.-; EC 3.6.-.- from Homo sapiens (Human) (see 18 papers)
47% identity, 86% coverage: 41:640/699 of query aligns to 148:749/797 of Q9Y4W6
- V191 (≠ A74) to I: in SCA28; uncertain significance
- F289 (≠ M175) mutation to A: Reduced rate of protein degradation.
- L299 (= L188) mutation to A: Reduced rate of protein degradation.
- K306 (≠ T195) to E: in SPAX5; uncertain significance
- G337 (= G226) to E: in OPA12; loss-of-function variant resulting in aberrant OPA1 processing and mitochondrial fragmentation; dbSNP:rs1908566777
- L346 (= L235) to F: in OPA12; uncertain significance; dbSNP:rs755893615
- K354 (= K243) mutation to A: Does not effect activity of the m-AAA protease complex.
- E376 (≠ D265) to K: in OPA12; uncertain significance
- F377 (= F266) to S: in OPA12; uncertain significance; dbSNP:rs1908507433
- M380 (= M269) mutation to K: Abolished ATPase and protease activities.; mutation to V: Increased ATP hydrolysis.
- D407 (= D296) to G: in OPA12; uncertain significance; decreased proteolytic function; dbSNP:rs1908371616
- E408 (= E297) mutation to Q: Abolished ATPase activity, leading to impaired activity of the m-AAA protease complex, preventing cleavage and degradation of substrate proteins.
- R416 (= R305) to S: in OPA12; uncertain significance
- F421 (≠ M311) mutation to A: Impairted protease activity without affecting the ATPase activity.
- T430 (= T320) to I: in OPA12; uncertain significance; dbSNP:rs1908369114
- N432 (= N322) to T: in SCA28; abolished ability to degrade substrate proteins; dbSNP:rs151344512
- A462 (= A352) to V: in OPA12 and SPAX5; decreased proteolytic function; dbSNP:rs912546325
- R465 (= R355) to K: in OPA12; decreased proteolytic function; dbSNP:rs1908309088
- R468 (= R358) to C: in OPA12; decreased proteolytic function resulting in impaired autocatalytic processing and impaired proteolytic maturation of SPG7; does not affect the interaction with SPG7; dbSNP:rs1020764190
- P514 (= P400) to L: in OPA12; decreased proteolytic function; dbSNP:rs1908300748
- A572 (= A458) to T: found in patients from a consanguineous family with progressive microcephaly, early onset seizures, spasticity and basal ganglia involvement; uncertain significance; decreased ATPase and ability to degrade substrate proteins
- H574 (= H460) binding Zn(2+)
- E575 (= E461) mutation to Q: Abolished protease activity. Loss of autocatalytic processing. Impaired proteolytic maturation of SPG7.
- H578 (= H464) binding Zn(2+)
- Y605 (= Y492) to C: in OPA12; uncertain significance; dbSNP:rs773240455
- Y616 (≠ M504) to C: in SPAX5 and SCA28; hypomorphic mutation in SPAX5; in SCA28, compound heterozygous with M-723; impaired oligomerization with itself and SPG7; increased ATPase and proteolytic activities; dbSNP:rs387906889
- Q620 (≠ E508) to K: in SPAX5; impaired function shown in a yeast complementation assay; dbSNP:rs1907907851
- L621 (= L509) to V: in SCA28; uncertain significance
- T644 (= T532) to S: in OPA12; uncertain significance; dbSNP:rs1226952405
- D649 (= D537) binding Zn(2+)
- M666 (= M554) to R: in SCA28; abolished ability to degrade substrate proteins; dbSNP:rs151344515
- P688 (≠ K579) to T: in SCA28; uncertain significance; slightly decreased ability to degrade substrate proteins
- E691 (≠ D582) to K: in SCA28; impaired function shown in a yeast complementation assay; dbSNP:rs151344520
- V723 (≠ L614) to M: in SCA28; compound heterozygous with C-616
Sites not aligning to the query:
- 74 E → A: in OPA12; uncertain significance
- 779 W→R: Impaired ability to degrade substrates without affecting the ATPase activity.
Q920A7 Mitochondrial inner membrane m-AAA protease component AFG3L1; AFG3-like protein 1; EC 3.4.24.-; EC 3.6.-.- from Mus musculus (Mouse) (see paper)
54% identity, 67% coverage: 174:640/699 of query aligns to 280:741/789 of Q920A7
- E567 (= E461) mutation to Q: Absence of proteolytic activity. Loss of its processing into the mature form.
Sites not aligning to the query:
- 1:70 modified: transit peptide, Mitochondrion
6nyyD Human m-aaa protease afg3l2, substrate-bound (see paper)
56% identity, 65% coverage: 188:640/699 of query aligns to 11:461/491 of 6nyyD