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CAZyme Information: MGYG000001874_01124
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | QAMI01 sp900554095 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; QAMI01; QAMI01 sp900554095 | |||||||||||
| CAZyme ID | MGYG000001874_01124 | |||||||||||
| CAZy Family | GH128 | |||||||||||
| CAZyme Description | Negative regulator of genetic competence ClpC/MecB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 34060; End: 36561 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| NF033606 | heat_AAA_ClpK | 0.0 | 4 | 800 | 111 | 892 | heat shock survival AAA family ATPase ClpK. ClpK, a Clp family AAA ATPase, was discovered as a plasmid-encoded determinant for survival of heat shock along with other putative heat shock proteins. ClpK requires the presence of ClpP to confer heat resistance. ClpK is about 65% identical to ClpG. Note that PMID:26974352 and PMID:29263094 discuss both ClpG itself and a member of this family (ClpK) that they call ClpG-GI. |
| NF033607 | disagg_AAA_ClpG | 0.0 | 3 | 802 | 87 | 872 | AAA family protein disaggregase ClpG. ClpG, as characterized in Pseudomonas aeruginosa, is a Clp family member of the AAA+ family of ATPases. ClpG has stand-alone ability to disaggregate proteins from aggregates that result from heat stess. Both ClpG and its mobilized homolog ClpK provide increased survival of exposure to heat. |
| PRK10865 | PRK10865 | 0.0 | 3 | 812 | 4 | 854 | ATP-dependent chaperone ClpB. |
| COG0542 | ClpA | 0.0 | 4 | 814 | 1 | 782 | ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones]. |
| TIGR03346 | chaperone_ClpB | 0.0 | 5 | 812 | 1 | 850 | ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization] |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGL63717.2 | 1.49e-197 | 171 | 789 | 107 | 710 |
| AXG45674.1 | 4.65e-132 | 60 | 808 | 68 | 870 |
| AXG41146.1 | 4.65e-132 | 60 | 808 | 68 | 870 |
| AWK40335.1 | 1.80e-131 | 60 | 808 | 68 | 870 |
| QIE96744.1 | 2.29e-10 | 358 | 431 | 1 | 74 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 7ABR_A | 0.0 | 1 | 808 | 2 | 798 | ChainA, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_B Chain B, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_C Chain C, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_D Chain D, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_E Chain E, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168],7ABR_F Chain F, Negative regulator of genetic competence ClpC/MecB [Bacillus subtilis subsp. subtilis str. 168] |
| 6EM8_A | 0.0 | 1 | 802 | 2 | 792 | S.aureusClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_B S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_C S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_D S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_E S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_F S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_G S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_H S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_I S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus],6EM8_L S.aureus ClpC resting state, C2 symmetrised [Staphylococcus aureus] |
| 6EM9_A | 0.0 | 1 | 802 | 2 | 792 | S.aureusClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_B S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_C S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_D S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_E S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_F S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_G S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_H S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_I S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122],6EM9_L S.aureus ClpC resting state, asymmetric map [Staphylococcus aureus RF122] |
| 3J3T_A | 0.0 | 1 | 808 | 2 | 798 | Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3T_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168] |
| 3J3S_A | 0.0 | 1 | 808 | 2 | 798 | Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3S_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q6GBW3 | 0.0 | 1 | 802 | 2 | 792 | ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=clpC PE=3 SV=1 |
| Q7F9I1 | 0.0 | 1 | 801 | 87 | 888 | Chaperone protein ClpC1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC1 PE=2 SV=2 |
| Q7A797 | 0.0 | 1 | 802 | 2 | 792 | ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain N315) OX=158879 GN=clpC PE=1 SV=1 |
| Q6GJE4 | 0.0 | 1 | 802 | 2 | 792 | ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=clpC PE=3 SV=1 |
| Q8EU05 | 0.0 | 1 | 806 | 2 | 799 | Chaperone protein ClpB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=clpB PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |