ID A0A1I4ACV7_9ACTN Unreviewed; 883 AA.
AC A0A1I4ACV7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04488085_102154 {ECO:0000313|EMBL:SFK53636.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFK53636.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFK53636.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFK53636.1,
RC ECO:0000313|Proteomes:UP000199152};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOSW01000002; SFK53636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ACV7; -.
DR STRING; 504800.SAMN04488085_102154; -.
DR InParanoid; A0A1I4ACV7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199152; 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:SFK53636.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFK53636.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199152};
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 417..538
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 883 AA; 98179 MW; C17785760EB8D076 CRC64;
MDLNRLTQKS QEALAAAQAL AIQHGHTEVD VEHLLLALLD QSEGLVPRLL AAMDVDLAAL
RRDVEAEVSR KPRTTGAAPQ PGQVSLTQRV ARVLETADRE ARRMKDEYVS VEHLLVALVE
TGQTTGAGRV LAQHGVTRDA FLSALTQIRG NQRVTSATPE GTYEALAKYG MDLVEAARTG
RMDPVIGRDA EIRRVIQILS RKSKNNPVLL GEPGVGKTAI VEGLAQRIVN GDVPEGLRDR
TIFALDMGLL VAGAKYRGEF EERLQAVLTE VKAAEGRVLL FIDEVHNVVG AGASEGAMDA
GNMLKPMLAR GELHMIGATT LTEYRKYIEK DAALERRFQP VFVEEPSVED TISILRGLRE
RFEVFHGVRI LDGALVAAAT LSHRYLTDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
TRRVMRLEIE EAALEKEDDP ASIARLDQLR RELADLRAEA DAMRAQWNAE RQAIQRVQEL
RAELEQVRRE IEEAERSYDL NRAAELRYGR LAELERKLEA EEQRLAAKQG ENRLLREVVT
PEEIAEIVSS WTGIPVSRLT EGEREKLLRL DELLHQRVIG QEEAVQAVAD AIIRARSGVK
DPRRPTGSFI FLGPTGVGKT ELAKALAEAL FDSEENIVRI DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRRPYA VVLFDEIEKA HPDVFNTLLQ VLDDGRLTDA QGRTVDFRNT
VIIMTSNIGS QYLLDGVTAD GQLKPEARDL VLAELRSHFR PEFLNRVDDT VLFKPLTPAQ
IEHIVELMLA DLRKRLAERN ITLEVTDEAR RFIAREGYDP VYGARPLRRF IAKEVETRVA
RALLRAGALE GETIRVDVEG GHLVVAVQAP TGAQADQQAG AQV
//