ID A0A4Q7YWP9_9BACT Unreviewed; 883 AA.
AC A0A4Q7YWP9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BDD14_3146 {ECO:0000313|EMBL:RZU41621.1};
OS Edaphobacter modestus.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Edaphobacter.
OX NCBI_TaxID=388466 {ECO:0000313|EMBL:RZU41621.1, ECO:0000313|Proteomes:UP000292958};
RN [1] {ECO:0000313|EMBL:RZU41621.1, ECO:0000313|Proteomes:UP000292958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18101 {ECO:0000313|EMBL:RZU41621.1,
RC ECO:0000313|Proteomes:UP000292958};
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 (FEB-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:RZU41621.1}.
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DR EMBL; SHKW01000001; RZU41621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7YWP9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000292958; 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 78, MITOCHONDRIAL; 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:RZU41621.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZU41621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000292958};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 5..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 883 AA; 97275 MW; BE7791216882E2EE CRC64;
MAIKWEKLTV KSQEAVQGAV QHAAENGNPE VLPLHLMAAL LEDREGVVIP VLDKVGVPVE
QLLSGVNSAV QKLPKVQGGG QPGLAQATQK ILEQAFKEAD NFKDEYVSTE HLLLALSKQK
GDAVASALAS FGATYDAILK ALAEVRGSQR VTDQTPEGKF QALEKYAKDL TELARKGRLD
PVIGRDEEIR RVIQVLARRT KNNPVLIGEP GVGKTAIVEG LARRIVQGDV PEILKNKRVC
ALDLASMVAG AKFRGEFEER LKAVLKEIED SNGEIILFID ELHTLVGAGA AEGAMDASNM
LKPALARGGL RAIGATTLNE YRKYIEKDAA LERRFQVVYV GEPNVEDTIA ILRGLKEKYE
AHHKVRIKDA AIVAAATLSH RYISDRFLPD KAIDLVDEAA AALAIQIGSV PVEIDDLERR
ATSLEIERAA LQREKDPNSQ ERLEVVEREL AEIKEQASAL RARWQKERGA IGRIAELKEQ
LEGLRFQMQE ETRKGNLQRA AELQYGEIPK LEAELRELTA LQDAAVAEDA AEAATGAATR
PSRMLKEEVD EEDIAAIVSK WTGIPVSKML EGETQKLVQM EDRLRERVVG QDEALSAVAN
AIRRSRAGLS DPKRPIGSFI FLGPTGVGKT ETARALAEFL FDDEKAMVRL DMSEYMEKHA
VARLIGAPPG YVGYDEGGQL TEAVRRRPYS VILFDEIEKA HPDVFNVLLQ VLDDGRLTDS
KGRTVDFKNT VLIMTSNTGA DKLTSAWAQG EDGFEEAKAR VIDALKQVFR PEFLNRVDDI
VVFHPLDDKE LTHIVDLRLK DLEKLLADRR ITLELTDAAR KAIFKAGYDR AYGARPLKRA
IQRMVQDKLA VKILDGTVLH GDHVVVDAGK DGLTFSVKER VAA
//
