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CAZyme Information: MGYG000002153_01197

You are here: Home > Sequence: MGYG000002153_01197

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 CAG-484 sp000431315
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; CAG-484; CAG-484 sp000431315
CAZyme ID MGYG000002153_01197
CAZy Family CBM10
CAZyme Description Negative regulator of genetic competence ClpC/MecB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
834 92378.9 5.8051
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002153 2088771 MAG Germany Europe
Gene Location Start: 104062;  End: 106566  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4

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 3 829 87 900
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 4 820 1 786
ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones].
TIGR03346 chaperone_ClpB 0.0 5 814 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]
NF033606 heat_AAA_ClpK 0.0 4 833 111 926
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.
CHL00095 clpC 0.0 1 812 1 805
Clp protease ATP binding subunit

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AGL63717.2 1.11e-191 173 791 107 710
AXG45674.1 4.36e-128 60 805 68 862
AXG41146.1 4.36e-128 60 805 68 862
AWK40335.1 1.68e-127 60 805 68 862

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 1 810 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 1 810 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 1 810 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 1 810 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]
6EM9_A 1.47e-317 1 806 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O78410 0.0 1 811 1 803
ATP-dependent Clp protease ATP-binding subunit ClpA homolog OS=Guillardia theta OX=55529 GN=clpC PE=3 SV=1
Q9SXJ7 0.0 1 804 114 916
Chaperone protein ClpC2, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC2 PE=1 SV=1
Q9FI56 0.0 1 804 94 895
Chaperone protein ClpC1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=CLPC1 PE=1 SV=1
Q2QVG9 0.0 1 803 88 889
Chaperone protein ClpC2, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC2 PE=2 SV=2
Q1XDF4 0.0 1 811 1 806
ATP-dependent Clp protease ATP-binding subunit ClpA homolog OS=Neopyropia yezoensis OX=2788 GN=clpC 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 MGYG000002153_01197.