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
//