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CAZyme Information: MGYG000000363_01787

You are here: Home > Sequence: MGYG000000363_01787

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 Zag1 sp001917115
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1; Zag1 sp001917115
CAZyme ID MGYG000000363_01787
CAZy Family GH128
CAZyme Description Negative regulator of genetic competence ClpC/MecB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
832 92463.89 5.6976
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000363 2012818 MAG Sweden Europe
Gene Location Start: 79755;  End: 82253  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000363_01787.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
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.
PRK11034 clpA 0.0 20 826 17 755
ATP-dependent Clp protease ATP-binding subunit; Provisional
COG0542 ClpA 0.0 4 818 1 786
ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones].
PRK10865 PRK10865 0.0 3 811 4 853
ATP-dependent chaperone ClpB.
NF033606 heat_AAA_ClpK 0.0 4 832 111 926
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AGL63717.2 1.47e-191 171 818 107 737
AXG45674.1 5.13e-130 60 802 68 861
AXG41146.1 5.13e-130 60 802 68 861
AWK40335.1 1.98e-129 60 802 68 861

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]
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]
3J3R_A 0.0 1 808 2 798
Structuraldynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3R_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_A Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_B Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_C Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_D Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_E Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168],3J3U_F Structural dynamics of the MecA-ClpC complex revealed by cryo-EM [Bacillus subtilis subsp. subtilis str. 168]
6EM8_A 4.52e-319 1 804 2 794
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q2QVG9 0.0 1 804 88 892
Chaperone protein ClpC2, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC2 PE=2 SV=2
Q1XDF4 0.0 1 809 1 806
ATP-dependent Clp protease ATP-binding subunit ClpA homolog OS=Neopyropia yezoensis OX=2788 GN=clpC PE=3 SV=1
Q9SXJ7 0.0 1 804 114 918
Chaperone protein ClpC2, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC2 PE=1 SV=1
Q9FI56 0.0 1 804 94 897
Chaperone protein ClpC1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC1 PE=1 SV=1
Q8EU05 0.0 1 794 2 787
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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000363_01787.