ID A0A1A0PIS6_9MYCO Unreviewed; 848 AA.
AC A0A1A0PIS6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A5662_08505 {ECO:0000313|EMBL:OBB09633.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBB09633.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBB09633.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBB09633.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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|ARBA:ARBA00004496,
CC 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:OBB09633.1}.
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DR EMBL; LZSH01000092; OBB09633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0PIS6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000091934; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 78, MITOCHONDRIAL; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
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..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 848 AA; 92714 MW; 57D53B4859FF546C CRC64;
MDSFNPTTKT QAALTAALQA ATTAGNPQIM PAHLLMALLT QNDGIAAPLL EAVGVDPATV
RTETQRLLDR LPSASGASSQ PQLSRESIAA ITTAQNLATE MDDEYVSTEH LMVGLATGDS
DVAKLLTGHG ASPQALREAF VKVRGSARVT NPDPEGSYQA LEKYSTDLTA RAREGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTVISL
DLGSMVAGSK YRGEFEERLK AVLDDIKNSA GQIITFIDEL HTIVGAGATG DSSMDAGNMI
KPMLARGELR LVGATTLDEY RKYIEKDAAL ERRFQQVFVG EPSVEDTVGI LRGLKDRYEV
HHGVRITDSA LVAAATLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL AKEEDDASRE RLEKLRAELA DHQEKLAQLT TRWQNEKNAI DVVRELKEQL
EELRGEADRA ERDGNLEKAA ELRYGRIPEA EKKLDAALPT AQAQEAQMLK EEVGPDDIAD
VVSAWTGIPA GRMLEGETAK LLRMESELGK RVVGQKKAVQ AVSDAVRRSR AGVADPNRPT
GSFMFLGPTG VGKTELAKAL AEFLFDDERA MVRIDMSEYG EKHSVARLVG APPGYIGYDQ
GGQLTEAVRR RPYTVILFDE IEKAHPDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
NLGAGGSEEM VMAAVRSAFK PEFINRLDDV IIFDGLNPEE LVSIVDIQLE QLSKRLAQRR
LTLEVSLPAK KWLAERGFDP LYGARPLRRL IQQAIGDQLA KMLLAGDVHD GDIVPVNVSA
DGDSLVLG
//
