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Database: UniProt
Entry: A0A0B2BTV4_9ACTN
LinkDB: A0A0B2BTV4_9ACTN
Original site: A0A0B2BTV4_9ACTN 
ID   A0A0B2BTV4_9ACTN        Unreviewed;       870 AA.
AC   A0A0B2BTV4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=CLV56_2247 {ECO:0000313|EMBL:PJJ58004.1};
OS   Mumia flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Mumia.
OX   NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ58004.1, ECO:0000313|Proteomes:UP000230842};
RN   [1] {ECO:0000313|EMBL:PJJ58004.1, ECO:0000313|Proteomes:UP000230842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ58004.1,
RC   ECO:0000313|Proteomes:UP000230842};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-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. {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:PJJ58004.1}.
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DR   EMBL; PGEZ01000001; PJJ58004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2BTV4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000230842; 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:PJJ58004.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PJJ58004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230842};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          443..501
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  94096 MW;  355DBA049D81A05E CRC64;
     MDASKLTTRS QQAVAAAIQH AAAAGNPAVD PVHLLDALLD AEGGTAVPLL QAVGADPATV
     RARTKEALGT LPSAAGQAVA SPGYARGTLE VLQRAQDLAD ELGDEFVSTE HLMVGLAVVD
     SKAKEVLGGV GATADALQDA FRSVRGSGRV TSQDAEDTYQ ALEKYGVDLT ASAREGKLDP
     VIGRDAEIRR TVQVLTRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP TSLQGRRLIA
     LDLGAMVAGA KYRGEFEERL KAVLNEIKES DGQIITFIDE LHTVVGAGAT GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRENIEKDPA LERRFQQVLV DEPSVEDTIA ILRGLKETYE
     AHHKVEIADA ALVAAASLSD RYITGRQLPD KAIDLVDEAS SRLRMEIDSN PVEIDTLRRS
     VDRMKMEELH LSKETDEASA ERLAKLRAEL ADDEEHLRAL EARWERERSG LNAVGEIKQK
     IDELRREAER AQNAGDLETA ARLNYAEIPT LEKQLSSAEA DEAESSEGEG AVEKMVNDEV
     GPDEIAEVVA SWTGIPTGRL LEGETGKLLR MESELGHRLI GQTTAVAAVS DAVRRSRAGI
     ADPNRPTGSF LFLGPTGVGK TELAKALAEF LFDDERAMVR IDMSEYSEKH SVSRLVGAPP
     GYVGYDEGGQ LTEAVRRRPY SVVLLDEVEK AHPEVFDILL QVLDDGRLTD GQGRTVDFRN
     VILILTSNLG SLYLADPALD DETKNAKVMD VVRTAFRPEF LNRLDEVVMF DPLSTDDLAH
     IVDLQVAALA QRLEARRIRL TVTDAARTWL ATTGFDPTYG ARPLRRLVQQ AIGDTLAREL
     LAGEVRDGDE VVVDVDPERE GLSVAAAPRT
//
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