ID A0A061JJ00_9PROT Unreviewed; 854 AA.
AC A0A061JJ00;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=K737_300109 {ECO:0000313|EMBL:ETZ05449.1};
OS Holospora undulata HU1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC Holospora.
OX NCBI_TaxID=1321371 {ECO:0000313|EMBL:ETZ05449.1, ECO:0000313|Proteomes:UP000026922};
RN [1] {ECO:0000313|EMBL:ETZ05449.1, ECO:0000313|Proteomes:UP000026922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HU1 {ECO:0000313|EMBL:ETZ05449.1,
RC ECO:0000313|Proteomes:UP000026922};
RX PubMed=23969064;
RA Dohra H., Suzuki H., Suzuki T., Tanaka K., Fujishima M.;
RT "Draft Genome Sequence of Holospora undulata Strain HU1, a Micronucleus-
RT Specific Symbiont of the Ciliate Paramecium caudatum.";
RL Genome Announc. 1:E00664-13(2013).
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|ARBA:ARBA00004496,
CC 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:ETZ05449.1}.
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DR EMBL; ARPM03000047; ETZ05449.1; -; Genomic_DNA.
DR RefSeq; WP_006290058.1; NZ_ARPM03000047.1.
DR AlphaFoldDB; A0A061JJ00; -.
DR Proteomes; UP000026922; 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 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; 1.
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:UP000026922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..140
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..487
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 854 AA; 95837 MW; 624AC7C0146E1947 CRC64;
MNFEHYTEKA QGFLQEAQSI AIQNSHPQIL AEHLAFALIQ DAQGVGASLL QSASINANQV
KSVLERLLKK MPSAKGGQCS AGSSLLQALK EAQEFSQKIG DTFVTVQALL YGVLKVLDLD
LSPKIDMKAL EKSIQELRKG RNAHSASSDA HYDALEKYTK DVTALAQQGK LDPVIGREEE
IRRTIQVLSR RSKNNPVLIG EPGVGKTAVV EGLAQRIASC DVPDTLRNMR IMALDLGAML
AGSKFRGEFE ERLKAVLDEI EHSKGDIVLF IDELHTLVGA GKTDGAMDAS NMLKPPLARG
DLHCIGATTL KEYRQYIEKD GALARRFQPV FVEEPSVAET VSILRGLRER YELHHGGVRI
TDSALVSAAT LSDRYINDRF LPDKAIDLID EAASRLRMEV HSKPEALDEI DRRIVQLRIE
KEALKKENDL AAKTRLQGCI KELENLEEQS RILSTQWEQD RTALHSVKTL KTDLEKARND
LIQAQKESQW EKASKLMYST IPDLESRIRD EREKSSHALL KEEVTEGDIA AVVSRWTGVA
IDKILTQERQ KLLQMENLLR QRVVGQSEAI CAVSRAICRA RVGLADTKRP IGSFLFLGPT
GVGKTELAKA LAEFLFDDET AMLRIDMSEY MEKHSVSRLI GAPPGYVGYE EGGVLTESVR
RRPYQLILLD EVEKAHGDVF NLFLQILDDG RLTDSQGRVV GFSNTLLILT SNLGSQYMMQ
EKSSDLSSKT RSQVMEVVRH TFRPEFLNRL DDILFFHKLT EQHMHQVVRI QLDNVHRLLS
NKHIRLHLDD SAIEFLANEG FEPEYGARPL KRIIQRRVLD PLSTLILEDK LHEGEEIFGK
LSENGNGVTF QIRQ
//