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Database: UniProt
Entry: A0A2L2X490_9BACT
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Original site: A0A2L2X490_9BACT 
ID   A0A2L2X490_9BACT        Unreviewed;       866 AA.
AC   A0A2L2X490;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:GBF22841.1};
GN   ORFNames=tpqmel_0245 {ECO:0000313|EMBL:GBF22841.1};
OS   Candidatus Gastranaerophilus sp. (ex Termes propinquus).
OC   Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales;
OC   Candidatus Gastranaerophilus.
OX   NCBI_TaxID=2029980 {ECO:0000313|EMBL:GBF22841.1, ECO:0000313|Proteomes:UP000243008};
RN   [1] {ECO:0000313|EMBL:GBF22841.1, ECO:0000313|Proteomes:UP000243008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tpqmel {ECO:0000313|EMBL:GBF22841.1};
RX   PubMed=29415909; DOI=10.1264/jsme2.ME17137;
RA   Utami Y.D., Kuwahara H., Murakami T., Morikawa T., Sugaya K., Kihara K.,
RA   Yuki M., Lo N., Deevong P., Hasin S., Boonriam W., Inoue T., Yamada A.,
RA   Ohkuma M., Hongoh Y.;
RT   "Phylogenetic Diversity and Single-Cell Genome Analysis of
RT   "Melainabacteria", a Non-Photosynthetic Cyanobacterial Group, in the
RT   Termite Gut.";
RL   Microbes Environ. 33:50-57(2018).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBF22841.1}.
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DR   EMBL; BEIT01000010; GBF22841.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2X490; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000243008; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Hydrolase {ECO:0000313|EMBL:GBF22841.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GBF22841.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243008};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          4..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          419..503
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  97217 MW;  6AA6B45D8C79CD1D CRC64;
     MFDFNRLTQS SQKIILEAQN LVRVNKNSLL ESAHITLAMA ETSDGVCVDL FNLLKLNSKL
     FKEDIQKIVN ELPKVDTAPE QMFFSQNALK VLQGSLDEAK ILKDKFASPE HILLSILANE
     ENKSPVGRLF HKFSVTKEKV FEVMKKLRGG KMQGGVDTDT ADEEFNVMEK YSQDLTERAR
     QGKLDPVIGR DEEVRRIIQV LNRRTKNNPV LIGEAGVGKT AIVEGLAQRI IRGDVPEGLK
     DTKLLSLDMG ALIAGAKYRG EFEERLKKVL DEVSKSEGSI IMFIDELHTV VGAGAAEGST
     DASNLLKPML ARGELRTVGA TTVNEYRKYI EKDPALERRF QPVMVDEPSV EDTISILRGL
     KDRYEVHHGV RIKDSALTAA ASLSDRYIAD RFLPDKAIDL IDEAASSVRI EIDSMPKELD
     MLERQRLQLQ IELEALKSEG AVDKMARVEQ ILKEISDKAD TLKARWEREK STLKGEVGIK
     SEIEKTKIEI ENAERDADLE LAAKLKYGKL PELEKQLRDV EKTETTEGAP LLKEEIDEND
     IAQIVSKWTG VPVTKLVEDE AKKLIEMEDV LHKRVIGQGE AVEVVSDAIR RTRAGLKNPK
     RPIGVFLFLG PTGVGKTELA KSLAEYMFMD EDSLIRIDMS EYMEKHSVSR LIGAPPGYIG
     HDEGGQLTEK VRRKPYSVVL FDEVEKAHPD VFNIMLQIFD DGRLTDSRGR TVDFKNTVII
     MTSNIGSDVI LESALAGVQK NIEETKEAVM EKLRSHFKPE FLNRVDETVF FEALKMADLE
     KIVDIQMKAL KGLLSERNIS LEITEDARER LAIDGYNPMY GARPLKRVIS KKVENQLSKA
     LLKGEFKDGD TVVVDVKDTE IVFEKG
//
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