ID A0A2T6F613_9BURK Unreviewed; 864 AA.
AC A0A2T6F613;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PUA18486.1};
GN ORFNames=C7W93_00530 {ECO:0000313|EMBL:PUA18486.1};
OS Glaciimonas sp. PCH181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Glaciimonas.
OX NCBI_TaxID=2133943 {ECO:0000313|EMBL:PUA18486.1, ECO:0000313|Proteomes:UP000244112};
RN [1] {ECO:0000313|EMBL:PUA18486.1, ECO:0000313|Proteomes:UP000244112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH181 {ECO:0000313|EMBL:PUA18486.1,
RC ECO:0000313|Proteomes:UP000244112};
RA Kumar V., Thakur V., Kumar S., Singh D.;
RT "Genome analysis of a novel bacterium Glaciimonas sp. PCH181 isolated from
RT glacier stream of Indian trans-Himalaya.";
RL Submitted (MAR-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:PUA18486.1}.
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DR EMBL; PYFP01000001; PUA18486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6F613; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244112; 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: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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000244112};
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"
FT COILED 780..807
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 95955 MW; CE729DDF5CB6E2CA CRC64;
MRFDKLTTKL QEAISDAQSQ AVGNDNQYID PIHVILALLN QDDGSARSLL QRAGVNIAAF
STGLKAAQER LPKVSGNSGE VQIGRELLGL LNLADKEAQK HGDQFIASEM LLLGLLDDKS
DAGQLARQHG LTRKALEAAI SAVRGGDNVA SQDGDGQREA LKKYTLDLTE RARQGKLDPV
IGRDDEIRRA IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPD SLKSKRVLSL
DMASLLAGAK FRGEFEERLK AVLKEIALDE GQTIVFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKILVDE PSVEATIAIL RGLQEKYEVH
HGVQITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKIEIDSKPE VMDKLDRRLI
QLKIEREAVK KEKDEASKRR FDLIEQEIEK LEREYADLEE VWKSEKANAL GSQHLKEEIE
KLRLQIDEAT RNSDWQKVSE LKYGKLNPLE QALEAQQKQD ALADANPDPS VKPRLVRTQV
GAEEIAEIVS RSTGIPVSKM MQGEREKLLK MEDELHRRVV GQDEAIAAVS DAIRRSRAGL
SDPDRPYGSF MFLGPTGVGK TELCKALAGF LFDTQDAMIR IDMSEFMEKH SVSRLIGAPP
GYVGYEEGGY LTEAVRRKPY SVILLDEIEK AHPDVFNVLL QVLDDGRMTD GQGRTVDFKN
TVIVMTSNLG SHRIQAMEGS DPAEVRTEVM AEVRNHFRPE FINRIDEIVV FHSLDEKNIG
AIAKIQLKIL EQRLAKLEMR LEISEGGLQK IAEAGFDPIY GARPLKRAIQ QQIENPLSKL
ILEGKFGPKD VIHISVNNGE IVFN
//
