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CAZyme Information: MGYG000001895_00651

You are here: Home > Sequence: MGYG000001895_00651

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 Zag111 sp900555325
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag111; Zag111 sp900555325
CAZyme ID MGYG000001895_00651
CAZy Family CBM81
CAZyme Description Negative regulator of genetic competence ClpC/MecB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
838 92900.52 6.1562
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001895 1985063 MAG Denmark Europe
Gene Location Start: 144831;  End: 147347  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
PRK10865 PRK10865 0.0 3 812 4 853
ATP-dependent chaperone ClpB.
NF033606 heat_AAA_ClpK 0.0 4 837 111 933
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.
COG0542 ClpA 0.0 4 819 1 786
ATP-dependent Clp protease ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones].
PRK11034 clpA 0.0 20 815 17 743
ATP-dependent Clp protease ATP-binding subunit; Provisional
TIGR03346 chaperone_ClpB 0.0 5 812 1 849
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 2.76e-199 172 814 107 732
AXG45674.1 3.80e-132 60 809 68 870
AXG41146.1 3.80e-132 60 809 68 870
AWK40335.1 1.47e-131 60 809 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 1 819 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 1 824 2 813
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 1 824 2 813
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 1 819 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 1 819 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 1 824 2 813
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=clpC PE=3 SV=1
Q7F9I1 0.0 1 812 87 899
Chaperone protein ClpC1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=CLPC1 PE=2 SV=2
Q7A797 0.0 1 824 2 813
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain N315) OX=158879 GN=clpC PE=1 SV=1
Q6GJE4 0.0 1 824 2 813
ATP-dependent Clp protease ATP-binding subunit ClpC OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=clpC PE=3 SV=1
Q8EU05 0.0 1 807 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 MGYG000001895_00651.