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Database: UniProt
Entry: A0A4R1LE58_9BACT
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Original site: A0A4R1LE58_9BACT 
ID   A0A4R1LE58_9BACT        Unreviewed;       874 AA.
AC   A0A4R1LE58;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C7378_0093 {ECO:0000313|EMBL:TCK75113.1};
OS   Acidipila rosea.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidipila.
OX   NCBI_TaxID=768535 {ECO:0000313|EMBL:TCK75113.1, ECO:0000313|Proteomes:UP000295210};
RN   [1] {ECO:0000313|EMBL:TCK75113.1, ECO:0000313|Proteomes:UP000295210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 103428 {ECO:0000313|EMBL:TCK75113.1,
RC   ECO:0000313|Proteomes:UP000295210};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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:TCK75113.1}.
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DR   EMBL; SMGK01000001; TCK75113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R1LE58; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295210; 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:TCK75113.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCK75113.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295210};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          5..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   874 AA;  97159 MW;  5A56843F1889A95A CRC64;
     MAIRWDKFTV KSQEAVQNAS TLASENGSPE LLPLHMLAAL VEDKDGIIVP VLEKVGVPSS
     QLRAKVTEAL GKLPKVSGAG AQPAMSQAMQ RVLDQATKEA QDFKDEYIST EHLLLALTRE
     KNDGAQLLLA SFGATHDAIL KGLTAIRGSQ RVTDQNPEAK YQALEKYAKD LTELARRGKL
     DPVIGRDEEI RRVVQVLSRR TKNNPVLIGE PGVGKTAIVE GLARRIVHGD VPEVLRDKRV
     ISLDLGSMLA GAKYRGEFED RLKAILKEIE ESNGQIILFI DELHTLVGAG AAEGAIDASN
     MLKPALARGE LRAIGATTLN EYRKYIEKDA ALERRFQIVY VGEPNVEDTI AILRGLKERY
     EAHHNVRIKD AAIVAAATLS HRYISDRFLP DKAIDLVDEA AASLAIQIGS VPTEIDQLER
     EATSLEIEKA ALKRESDPNS RERLQIVERE LATLREKSTG LRARWQKERE AITRLAELKK
     QVESLRFEAE EQTRLGNLER AAQIQYGDLP RLESELKQLN AVQDGAAAGP RMLKEEVDEE
     DIAGIVSKWT GIPVSKMLEG EVQKLVAMEQ RLRERVIGQD DALTTVANAI RRSRAGLSDP
     KRPIGSFIFL GPTGVGKTET ARALAEFLFD DEQAMVRIDM SEYMEKHAVS RLIGAPPGYI
     GFDEGGQLTE AVRRRPYAVI LFDEIEKAHP DVFNVLLQVL DDGRLTDSKG RTVDFKNTVL
     IMTSNLGAHA LQGEALDSEA AFDRAREQVM EILKQSFRPE FLNRVDDIVI FRPLGEEQLS
     HIIDLRLEDM RRLLADRKIT FELTDGARHQ LLLTGYDRAY GARPLKRALQ KLIQDPLAIK
     ILDGEVLHGD HLLIDADPLN NRLKFEVATR AVEA
//
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