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
//