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Database: UniProt
Entry: A0A1G6VJD6_9NOCA
LinkDB: A0A1G6VJD6_9NOCA
Original site: A0A1G6VJD6_9NOCA 
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
//
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