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CAZyme Information: MGYG000004841_01612

You are here: Home > Sequence: MGYG000004841_01612

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
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag111;
CAZyme ID MGYG000004841_01612
CAZy Family GH128
CAZyme Description Negative regulator of genetic competence ClpC/MecB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
841 93076.59 5.9863
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004841 2009543 MAG China Asia
Gene Location Start: 12501;  End: 15026  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004841_01612.

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 3 806 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.
COG0542 ClpA 0.0 4 822 1 786
ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones].
PRK11034 clpA 0.0 20 830 17 755
ATP-dependent Clp protease ATP-binding subunit; Provisional
PRK10865 PRK10865 0.0 3 815 4 853
ATP-dependent chaperone ClpB.
NF033606 heat_AAA_ClpK 0.0 4 840 111 930
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 3.07e-196 175 815 107 730
AXG45674.1 9.73e-129 60 812 68 870
AXG41146.1 9.73e-129 60 812 68 870
AWK40335.1 3.75e-128 60 812 68 870

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3J3T_A 0.0 1 822 2 808
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]
6EM8_A 0.0 1 808 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]
6EM9_A 0.0 1 808 2 794
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]
3J3R_A 0.0 1 822 2 808
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]
7ABR_A 0.0 1 822 2 808
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]

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 1 808 2 794
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=clpC PE=3 SV=1
Q7F9I1 0.0 1 805 87 888
Chaperone protein ClpC1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC1 PE=2 SV=2
Q7A797 0.0 1 808 2 794
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain N315) OX=158879 GN=clpC PE=1 SV=1
Q6GJE4 0.0 1 808 2 794
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=clpC PE=3 SV=1
Q8EU05 0.0 1 810 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004841_01612.