ID A0A497X9I7_9PROT Unreviewed; 868 AA.
AC A0A497X9I7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=DFR35_2457 {ECO:0000313|EMBL:RLJ62644.1};
OS Sulfurisoma sediminicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfurisoma.
OX NCBI_TaxID=1381557 {ECO:0000313|EMBL:RLJ62644.1, ECO:0000313|Proteomes:UP000268908};
RN [1] {ECO:0000313|EMBL:RLJ62644.1, ECO:0000313|Proteomes:UP000268908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26916 {ECO:0000313|EMBL:RLJ62644.1,
RC ECO:0000313|Proteomes:UP000268908};
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 (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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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:RLJ62644.1}.
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DR EMBL; RCCI01000007; RLJ62644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A497X9I7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000268908; 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:RLJ62644.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RLJ62644.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000268908};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 96071 MW; 5526CB0243F397C7 CRC64;
MRFDKFTTKF QQAVADAQSL AIGHDNQMIE PQHLLLALLN QDDGGTASLL ARAGVNVAPL
KKALDAAIDR LPQVEGTGGE VTIGRDLGNL LNLADKEAQK AGDAFIASEM FLLALTQDKG
ETGRLLKEHG LSRPALEQAI AAVRGGQNVG SQEAEGQREA LKKYCLDLTD RARQGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE TLKDKKVLVL
DMAGLLAGAK YRGEFEERLK AVLKEVALDE GRIILFIDEL HTMVGAGKAE GAIDAGNMLK
PALARGELHC IGATTLNEYR KYIEKDAALE RRFQKVLVDE PSVEATIAIL RGLQEKYEIH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAASR IKMEIDSKPE AMDKLDRRLI
QLKIEREAVR KEKDEASKKR FELIEEEIAK LAKEYSDLEE IWKAEKAQVQ GTQHIKEEIE
KLRTQIADLQ RKGQYDKLAE LQYGRLPQLE AQLTAAEKIS EGTQSAGAGD AAKPNKLLRT
QVGAEEIAEV VSRATGIPVS KMMQGEREKL LKMEDKLHGR VVGQDEAVRL VADAIRRSRA
GLSDENRPYG SFLFLGPTGV GKTELCKTLA EFLFDSEEHL IRIDMSEFME KHSVARLIGA
PPGYVGYEEG GYLTEQVRRK PYSVILFDEV EKAHPDVFNV LLQVLDDGRM TDGQGRTVDF
KNTVIVMTSN LGSQMIQQMS GDDYQVIKLA VMGEVKTHFR PEFVNRIDEI VVFHALDEKH
IASIAKIQLG YLEKRLVRMD MTLSVDDAAL ANIAAAGFDP VFGARPLKRA IQERIENPLA
RAILEGRFAA KDHIKVTAKA GRIEFAKG
//