ID A0A1Y6ENU8_9SPHN Unreviewed; 858 AA.
AC A0A1Y6ENU8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN06297468_0665 {ECO:0000313|EMBL:SMQ62192.1};
OS Altererythrobacter xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ62192.1, ECO:0000313|Proteomes:UP000194420};
RN [1] {ECO:0000313|Proteomes:UP000194420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Varghese N., Submissions S.;
RL Submitted (APR-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|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FXWG01000001; SMQ62192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6ENU8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000194420; 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:SMQ62192.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SMQ62192.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194420};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 94591 MW; EA798892908E55FB CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQRIT PLHLLKALLE DEEGMAAGLI QRAGGTPMLA
VDAVDQELAK IPAVSGGGAQ ATPGLDNDAV RILDQAEQMA EKAGDSYVPV ERILTALAAS
SGKAGEALKA ASITPQSLNA AINELRGGRT ADTASAENAY DAMKKFARDL TEAAREGKLD
PVIGRDEEIR RTIQILARRT KNNPALIGEP GTGKTAIAEG LALRIANGDV PDSLKGRTLM
SLDMGALIAG AKYRGEFEER LKSVLDEVKG SDGQIILFID EMHTLIGAGA SEGSMDASNL
LKPALSRGEL HCIGATTLDE YQKYVEKDPA LQRRFQPVFI EEPSVEDTIS ILRGIKEKYE
LHHGVNITDN ALVAAAQLSN RYIQNRFLPD KAIDLMDEAA SRIRMEVESK PEEIESLDRR
IIQLKIEESA LSKESDDASK DRLQALRKEL AELEQQSSEL TTRWQNERDK IHAESRIKED
LDAARLELEQ AQREGDLAKA GELSYGKIPE LEKQLEAARA QSENALLREE VTEEDIASVV
SRWTGIPIDK MLEGEREKLL QMEEILGKRV IGQSQAIEAV SKAVRRARAG LQDPNRPLGS
FLFLGPTGVG KTELTKALAA FLFDDDQAMV RIDMSEFMEK HAVARLIGAP PGYVGYEEGG
VLTEAVRRRP YQVVLFDEVE KAHGDVFNVL LQVLDDGRLT DGQGRVVDFS NTLIILTSNL
GSQYLSQMTD DQKVEDVEPQ VMDVVRGHFR PEFLNRLDEI ILFHRLGQEH MAPIVEIQVG
RVQKLLKDRK ITLDLSDAAL RWLGRVGYDP VYGARPLKRA VQRYVQDPLA EMILEGEVPD
GSTVQIEEGD GELKMTVA
//