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Database: UniProt
Entry: A0A497X9I7_9PROT
LinkDB: A0A497X9I7_9PROT
Original site: A0A497X9I7_9PROT 
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
//
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