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Database: UniProt
Entry: A0A4R2D4A3_9NOCA
LinkDB: A0A4R2D4A3_9NOCA
Original site: A0A4R2D4A3_9NOCA 
ID   A0A4R2D4A3_9NOCA        Unreviewed;       851 AA.
AC   A0A4R2D4A3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=EV641_11697 {ECO:0000313|EMBL:TCN49248.1};
OS   Rhodococcus sp. SMB37.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2512213 {ECO:0000313|EMBL:TCN49248.1, ECO:0000313|Proteomes:UP000295305};
RN   [1] {ECO:0000313|EMBL:TCN49248.1, ECO:0000313|Proteomes:UP000295305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMB37 {ECO:0000313|EMBL:TCN49248.1,
RC   ECO:0000313|Proteomes:UP000295305};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
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}.
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:TCN49248.1}.
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DR   EMBL; SLVY01000016; TCN49248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R2D4A3; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295305; 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:TCN49248.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCN49248.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295305};
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   851 AA;  92172 MW;  0B63F5726A533522 CRC64;
     MDSFNPTTKT QAALTAALQS ASAAGNPDIR PAHLLVALLD QTDGIAGPLL KAVGVDPAQI
     RSEAHELVDK LPTATGATTT PQLGREAIAA LSGAQKLATE LDDEFVSTEH VLVGLASGDS
     DVATLLAGKG ATPEALREAF TTVRGTGRVT SADPEGTFQA LEKYSTDLTA RAREGKLDPV
     IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRVVAGDVPE SLRGKSVISL
     DLGSMVAGAK YRGEFEERLK AVLDEIKASA GQIITFIDEL HTIVGAGATG ESAMDAGNMI
     KPMLARGELR LVGATTLDEY RKYIEKDAAL ERRFQQVLVG EPSVEDTVGI LRGLKERYEV
     HHGVRITDSA LVSAATLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSRP EEIDTVERIV
     RRLEIEEMAL QKETDAASKD RLDKLRGELA DEREKLSQLT ARWQNEKTAI DSVREVKEQL
     EALRGEEERA ERDGDLGKAA ELRYGRIPEL EKKLEAAAKA SGAASDGDVM LKEEVGPDDV
     AEVVAAWTGI PAGRMLEGET EKLLRMEDEI GNRVVGQAEA VQAVSDAVRR SRAGVADPNR
     PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YSEKHSVARL VGAPPGYVGY
     DAGGQLTEAV RRRPYTVVLF DEVEKAHPDV FDTLLQVLDD GRLTDGQGRT VDFRNTILIL
     TSNLGAGGDK DHVMAAVRMA FKPEFINRLD DVVIFDPLSE EQLEKIVDIQ IDQLAKRLEA
     RRLTLDVDGA ARMWLAVRGY DPQYGARPLR RLIQQAIGDQ LAKKLLAGEI RDGDTVKVGV
     SDNADGLVLG V
//
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