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Database: UniProt
Entry: A0A660LD86_9ACTN
LinkDB: A0A660LD86_9ACTN
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ID   A0A660LD86_9ACTN        Unreviewed;       854 AA.
AC   A0A660LD86;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C8N24_2058 {ECO:0000313|EMBL:RKQ92215.1};
OS   Solirubrobacter pauli.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Solirubrobacteraceae; Solirubrobacter.
OX   NCBI_TaxID=166793 {ECO:0000313|EMBL:RKQ92215.1, ECO:0000313|Proteomes:UP000278962};
RN   [1] {ECO:0000313|EMBL:RKQ92215.1, ECO:0000313|Proteomes:UP000278962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14954 {ECO:0000313|EMBL:RKQ92215.1,
RC   ECO:0000313|Proteomes:UP000278962};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKQ92215.1}.
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DR   EMBL; RBIL01000001; RKQ92215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A660LD86; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000278962; 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:RKQ92215.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKQ92215.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          406..498
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   854 AA;  94332 MW;  E2AC0F7B9C66B5A5 CRC64;
     MQADRFTIKS QEALQAAIAV AAARNHTETQ PEHLLVALLE QPESVVVPVL RKLGARPETI
     KGEVEQALNQ LPTITAGAKE PTTSRELMDV LRLAEREAGK LRDEYISTEH ILLALAAAQG
     GEAAKSLNRN GATHKALTTA IEQVRGPHRV TDQSPEDKYQ ALQKFGRDLT ADAEDGKLDP
     VIGRDDEIRR VIQVLSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVSGDIP ESLKDRKVIS
     LDIGALLAGS KYRGEFEERL KAVLKEIADA EGQIILFMDE LHTIVGAGAA EGAVDASQLL
     KPMLARGELR AVGATTLDEY KKHVEKDAAL ERRFQPIYVG EPTLEGTIAI LRGLKERYEA
     HHGVTITDAA LIAAATLSDR YIADRFLPDK AIDLVDEAAS RVSIELSSVP TEIDEVERRI
     KQLEIEQVAV GKDDTAAERK AEIERELGDL REQANAMRAQ WEREKEQAEG HGKLRERLDE
     ARRELERAER ELNYQRAAEL RHGEIPDLEA KLADAESRPA ESYEPPVYLS ERVDVDEIAE
     VVGKWTGIPV SRLVEGEVEK LIHMEERLHQ RVIGQHEAVT AVSDALRRSR AGLSDPDRPI
     GTFLFLGPTG VGKTELARAL AEFMFDSQDA MIRIDMSEYM EKHSVARLVG APPGYVGYEE
     GGQLTEAVRR RPYSVVLLDE IEKAHNDVFN ILLQVFDDGR LTDGQGRTVD FKNTVLIMTS
     NIPGGRAGVE ANFKPEFVNR LDDIVEFEPL SREQLREIVD LQVARLIVRV AERGVDVALT
     DAARDLLGDL GYDPAYGARP LKRVISKYLV DPMALGLLKN EYAAGDHVEV DAEDGALRFT
     RVRVSEEAKT PTPA
//
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