logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000572_01222

You are here: Home > Sequence: MGYG000000572_01222

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; Zag1;
CAZyme ID MGYG000000572_01222
CAZy Family CBM5
CAZyme Description Negative regulator of genetic competence ClpC/MecB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
836 92897.59 6.1187
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000572 1867050 MAG Madagascar Africa
Gene Location Start: 3235;  End: 5745  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.4 3.2.1.91

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.
COG0542 ClpA 0.0 4 818 1 786
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]
NF033606 heat_AAA_ClpK 0.0 4 830 111 924
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 1 810 1 805
Clp protease ATP binding subunit

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AGL63717.2 5.27e-187 171 811 107 730
AXG45674.1 2.91e-130 60 802 68 861
AXG41146.1 2.91e-130 60 802 68 861
AWK40335.1 1.12e-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]
6EM9_A 5.17e-316 1 804 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
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 MGYG000000572_01222.