ID A0A1G6VJD6_9NOCA Unreviewed; 850 AA.
AC A0A1G6VJD6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05444580_10532 {ECO:0000313|EMBL:SDD53732.1};
OS Rhodococcus tukisamuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=168276 {ECO:0000313|EMBL:SDD53732.1, ECO:0000313|Proteomes:UP000199417};
RN [1] {ECO:0000313|EMBL:SDD53732.1, ECO:0000313|Proteomes:UP000199417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11308 {ECO:0000313|EMBL:SDD53732.1,
RC ECO:0000313|Proteomes:UP000199417};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. {ECO:0000256|RuleBase:RU362034}.
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}.
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DR EMBL; FNAB01000005; SDD53732.1; -; Genomic_DNA.
DR RefSeq; WP_072847252.1; NZ_FNAB01000005.1.
DR AlphaFoldDB; A0A1G6VJD6; -.
DR STRING; 168276.SAMN05444580_10532; -.
DR Proteomes; UP000199417; 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:SDD53732.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDD53732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199417};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 850 AA; 92075 MW; 99C143D3FCC8C3C4 CRC64;
MDSFSPTTKT QAALTAALQS ASAAGNPDIR PAHLLVALLD QTDGIAAPLL KAVGVDPAVV
HREAQTMVDR LPKATGATTT PQLGREALAA LTAAQRLATE LDDEYVSTEH LMVGLADGDS
DVAKLLVGHG ATAQTLRDAF TAVRGSARVT SPDPEGSYQA LEKYSTDLTE AARSGKLDPV
IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRGKTVISL
DLGSMVAGAK YRGEFEERLK AVLDDIKNSA GQVITFIDEL HTIVGAGATG ESAMDAGNMI
KPMLARGELR LVGATTLEEY RKYIEKDAAL ERRFQQVLVG EPSVEDTVGI LRGLKERYEV
HHGVRITDSA LVAAATLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEIERIV
RRLEIEEMAL AKETDEASKA RLAKLRQELA DAREKLGQLS TRWQNEKQAI DSVREVKEQL
ETLRRESDRA ERDGDLGKAA ELRYGRIPEL EKRLEAAVEA SGGASDGDVM LKEEVGPDDV
ADVVAAWTGI PAGRMMEGET AKLLRMESEL GKRVVGQADA VQAVSDAVRR ARAGVADPNR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
EAGGQLTEAV RRRPYTVVLF DEVEKAHPDV FDILLAVLDE GRLTDGQGRT VDFRNTILIL
TSNLGAGGTK EQVMDAVRHA FKPEFINRLD DVVIFDPLSE EQLESIVDIQ LGQLARRLAT
RRLTLEVSQP AKAWLAKRGY DPQYGARPLR RLVQQSIGDQ LAKLLLAGEI KDGDVVPVNV
TADGDGLTLG
//