ID A0A0U5AQ63_9BACL Unreviewed; 869 AA.
AC A0A0U5AQ63;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:BAU25957.1};
GN ORFNames=CB4_00008 {ECO:0000313|EMBL:BAU25957.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU25957.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU25957.1, ECO:0000313|Proteomes:UP000217696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU25957.1,
RC ECO:0000313|Proteomes:UP000217696};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; AP017312; BAU25957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5AQ63; -.
DR KEGG; asoc:CB4_00008; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000217696; Chromosome.
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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000217696};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 417..538
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 97464 MW; 51B3E1F6E2FC0032 CRC64;
MDLNKFTQKS IEAVQQAEMK ALRYGNPEIE PEHLLLVLLE QHEGLLARLL VKMNVSPEKL
KRDVEQRLEQ KPRVSGPGKE AGKIYVSSAT NQVFLKAEDE AKAMGDEYIS VEHLFLGILA
EAEKTTFGKL IAGVGITRAQ FLEALSSVRG SQRVTSATPE STYEVLDKYG HDLVSAAEQS
KLDPVIGRDG EIRHVIRILS RKTKNNPVLI GEPGVGKTAI VEGLAHRIVR GDVPEGLRDK
RIFALDMGAL IAGAKYRGEF EERLKAVLQE IKQSEGQILL FIDEIHTIVG AGKTEGAMDA
GNLLKPMLAR GELHCIGATT LDEYRKYIEK DAALERRFQT VLADEPTVED TISILRGLRE
RFEVFHGVKI HDNALVSAAV LSHRYITDRF LPDKAIDLVD EACAMIRTEI DSMPAELDEV
ARRVMQLEIE EAALKKETDA ASRDRLTHLQ KELAERREIL SAMKAQWENE KHALQSIQKL
REEIEGVHRA VAQAERDYDL NKAAELKYGR LPELEKQLRE AEVSHANKQN EQSLLREEVT
DDEITRIISR WTGIPLAKLA EGEREKLLKL DTILHERVVG QDEAVQRVTD AILRARAGIS
DPRRPIGSFI FLGPTGVGKT ELAKALAETL FDTEENIIRI DMSEYMEKHT VSRLIGAPPG
YVGFEEGGQL TEAVRRKPYS VILFDEIEKA HPDVFNVLLQ VLDDGRVTDS QGRTVDFKNT
VIIMTSNIGS AFLLEGITEA GEIREEARQH VMHELRMSFR PEFLNRVDEI VLFKPLTAGE
IGGIVELLID DLRRRLADRK ITLVLSDEAK AYIAREGYDP VYGARPLRRF LQRHLETLLA
RELIGGRIVD GARIQVGLTN ETLTVETSV
//