ID A0A239K5K4_9ACTN Unreviewed; 868 AA.
AC A0A239K5K4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05216276_102568 {ECO:0000313|EMBL:SNT12434.1};
OS Streptosporangium subroseum.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT12434.1, ECO:0000313|Proteomes:UP000198282};
RN [1] {ECO:0000313|EMBL:SNT12434.1, ECO:0000313|Proteomes:UP000198282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT12434.1,
RC ECO:0000313|Proteomes:UP000198282};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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}.
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DR EMBL; FZOD01000025; SNT12434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239K5K4; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000198282; 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:SNT12434.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNT12434.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 410..504
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 96887 MW; DC132E9970D20E16 CRC64;
MDLNQLTQKS QEALHDAQTK ALRFGHTEID GEHLLLALID QPEGLIPRLM LAADADPNRL
REELEAELNR RPRVSGPGVE PGQVYVTQRL SRLLEAAKRE ADRLKDEYVS VEHLLIALIE
EGSETAAGRL LHEAGLSRDT FLKALTSIRG NQRVTSAMPE VAYEALEKYG RDLVADAVAG
KLDPVIGRDA EIRRVIQILS RKTKNNPVLV GDPGVGKTAI VEGLAQRIGN GDVPEGLKGK
TVFSLDMGSL VAGAKYRGEF EERLKAVLNE VKAAEGRILL FVDEMHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LGEYRKHIEK DAALERRFQP VMIDEPSVED AVSILRGLRE
RLEVFHGVKI QDSALVAAVV LSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
TRRVMRLEIE ETALAKEEDA ASGARLEELR RELSDLRAEA DAMRAQWEAE RQALRTVQAL
RVEIEQVRAE AERAERDYDL NRAAELRHGR LPELERRLQT EEERLLSKQG VARLLREVVT
DDEISMIVSR WTGIPVSRLQ EGEREKLLRL DEILHERVVG QDEAVQLVAD AVIRARSGIK
DPRRPIGSFI FLGPTGVGKT ELARALAEAL FDTEDNMVRI DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEVEKA HSDVFNTLLQ VLDDGRLTDA QGRTVDFRNT
VLIMTSNIGS VYLLEGVTPG GEIKQDAKQQ VMAELRSRFR PEFLNRVDDI VIFKPLTPDE
IERIVGLMLG ELRARLDQRG IRLEITEDAL RYIAEQGYDP VYGARPLRRF IAREVETRIG
RALITGEAQE GAVIRVGLAE GELVVTYE
//