ID A0A2S5R6R4_9PROT Unreviewed; 852 AA.
AC A0A2S5R6R4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HCUR_01558 {ECO:0000313|EMBL:PPE03004.1};
OS Holospora curviuscula.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC Holospora.
OX NCBI_TaxID=1082868 {ECO:0000313|EMBL:PPE03004.1, ECO:0000313|Proteomes:UP000239425};
RN [1] {ECO:0000313|EMBL:PPE03004.1, ECO:0000313|Proteomes:UP000239425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=02AZ16 {ECO:0000313|Proteomes:UP000239425};
RA Garushyants S.K., Beliavskaya A., Malko D.B., Logacheva M.D., Rautian M.S.,
RA Gelfand M.S.;
RT "Comparative genomic analysis of Holospora spp., intranuclear symbionts of
RT paramecia.";
RL Submitted (NOV-2017) 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:PPE03004.1}.
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DR EMBL; PHHC01000146; PPE03004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5R6R4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000239425; 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; 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:UP000239425};
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 852 AA; 94987 MW; E223D812E22ED1D7 CRC64;
MNFEHYTEKA KAFLQEAQSL AVTAGHPQIL AEHLALVLIK DSQGMATALI NASSLNAAQI
ISELERLLRK IPPVKGGQCS AGTSLLQALS EAQSCSQRLG DTFVTAETLL YGALKVLDLD
ISPKLDAVIL EKSIQELRKG KNAHSASSDA HYNAIEKYTK DVTALAHQGK LDPVIGREEE
IRRTIQVLSR RSKNNPVLIG EPGVGKTAVV EGLAQRIASR DVPDTLRNTR IMALDLGAML
AGSKFRGEFE ERLKAVLDEI THSQGEIILF IDELHTLVGA GKTDGAMDAS NMLKPPLARG
ELHCIGATTL KEYRQYIEKD GALARRFQPV FVEEPSVAET ISILRGLRER YELHHGGIRI
TDTALVSAAT LSDRYINDRF LPDKAIDLID EAASRLRMEV HSKPEALDEI DRRIVQLRIE
KEALKKESDP AARTRLEACL KELANLEEQS RTLGTQWEQD RTALRSAQTL KTELEKARTN
LAQAQKESQW EKASKLMYSV IPDLESRIKS EREKGSPALL KEEVTEGDIA AIVSRWTGVP
IDKILTQERQ KLLQMEGVLR QRVVGQDSAV SAVSRAICRA RVGLADAGRP MGSFLFLGPT
GVGKTELAKA LAEFLFDDDT AMLRIDMSEY MEKHSVSRLI GAPPGYVGYE EGGVLTEAVR
RRPYQLILLD EVEKAHGDVF NLFLQILDDG RLTDSQGRVV GFNNTLLILT SNLGSQYMMQ
DTHQDLSSKT RSQVMEVVRQ AFRPEFLNRL DDILFFHRLT EDHMSQVVHI QLDRVHRLLA
PKRIRLHLDS KVINLLAKEG FEPEYGARPL KRVIQRRVLD PLSILILEET LHDGQDVFGK
MVDGEIVFQP HG
//
