ID A0A6H9Y7L5_9PROT Unreviewed; 864 AA.
AC A0A6H9Y7L5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
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:KAB2313922.1};
GN ORFNames=F8A87_01405 {ECO:0000313|EMBL:KAB2313922.1};
OS Betaproteobacteria bacterium SCN2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=2651628 {ECO:0000313|EMBL:KAB2313922.1, ECO:0000313|Proteomes:UP000430388};
RN [1] {ECO:0000313|Proteomes:UP000430388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCN2 {ECO:0000313|Proteomes:UP000430388};
RA Liu L.;
RT "Puniceibacterium HSS470 sp.nov, a marine bacterium isolated from Pacific
RT Ocean:the Okinawa trough.";
RL Submitted (SEP-2019) 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:KAB2313922.1}.
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DR EMBL; WBSG01000002; KAB2313922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6H9Y7L5; -.
DR Proteomes; UP000430388; 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:UP000430388};
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 864 AA; 95739 MW; 6E434CD5B4D054C1 CRC64;
MRFDKLTTQF QQAIADAQSY AVGSDQQFIE PLHLMAALLD QEGGGASGLL AKAGARVPAL
KNGIEEAIAR LPRVEGHGGD VTISRDLNNL LNLTDREAQK RGDAYIASEL FLLAALEDKG
ELGRQMKQHG VTRAALEQAI NTVRGGEAVQ SQEAEGQREA LKKYTLDLTE RAVQGKLDPV
IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE TLKDKKVLVL
DMAGLLAGAK YRGEFEERLK AVLKEVAQDE GRIILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVMVDE PSVEDTIAIL RGLQEKYELH
HGVEITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAASR IKMEIDSKPE SMDKLDRRLI
QLKIEREAVK KEKDEASQKR FALIEDEIAR LSREYADLEE VWKAEKAQVH GAAHIKEEID
RLKIEMAELQ RKGQFDKLAE IQYGKLPQLE AQLKHAEASG EGPALKLLRT QVGAEEIAEV
VSRATGIPVS KMMEGERDKL MHMEDALHER VVGQDEAVRL VSDAIRRSRA GLGDPNRPYG
SFLFLGPTGV GKTELCKALA GFLFDSEEHM IRIDMSEFME KHSVARLIGA PPGYVGYEEG
GYLTEAVRRK PYSVILLDEV EKAHPDVFNV LLQALDDGRM TDGQGRTVDF KNTVIVMTSN
LGSQMIQQMA GDDYQVVKLA VMAEVKNYFR PEFINRIDEV VVFHALGEAH IASIAKIQLK
YLEQRLARME MNLEVSDAAV TEIAKAGFDP VFGARPLKRA IQSQIENPLA KEILSGHFAA
KDVIRVDARD GRIVFDKGTL VQAA
//
