ID A0A1X1Y7N9_9MYCO Unreviewed; 848 AA.
AC A0A1X1Y7N9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:BBX98521.1};
GN ORFNames=MLAC_38150 {ECO:0000313|EMBL:BBX98521.1};
OS Mycobacterium lacus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=169765 {ECO:0000313|EMBL:BBX98521.1, ECO:0000313|Proteomes:UP000466396};
RN [1] {ECO:0000313|EMBL:BBX98521.1, ECO:0000313|Proteomes:UP000466396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98521.1,
RC ECO:0000313|Proteomes:UP000466396};
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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; AP022581; BBX98521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1Y7N9; -.
DR STRING; 169765.AWC15_20750; -.
DR KEGG; mlj:MLAC_38150; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000466396; Chromosome.
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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000466396};
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..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 848 AA; 92782 MW; 822E4CB49B208A58 CRC64;
MDSFNPTTKT QAALTSALQA ASAAGNPEIR PAHLLMALLT QNDGIAAPLL EAVGVEPATV
RAEAQRLLDR LPQASGASSQ PQLSRESLAA ITTAQQLATE MDDEYVSTEH LMVGLATGDS
DVAKLLTGHG ASPQALRDGF VKVRGSARVT SPEPEATYQA LEKYSTDLTA QAREGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVDGDVPE SLRDKTIVAL
DMGSMVAGSK YRGEFEERLK AVLDDIKNSA GQIITFIDEL HTIVGAGATG EGAMDAGNMI
KPMLARGELR LVGATTLDEY RKHVEKDAAL ERRFQQVYVG EPSVEDTIGI LRGLKDRYEV
HHGVRITDSA LVAAAALSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL AKEEDEASKE RLEKLRAELA DKKEELAELT ARWQNEKNAI EIVRELKEQL
ETLRGESERA ERDGDLAKAA ELRYGRIPEV EKKLTAALPQ AEAREQVMLK EEVGPDDIAD
VVSAWTGIPA GRLLEGETAK LLRMEDELGK RVVGQKRAVQ AVSDAVRRSR AGVSDPNRPT
GAFMFLGPTG VGKTELAKAL ADFLFDDERA MVRIDMSEYG EKHTVARLIG APPGYIGYEQ
GGQLTESVRR RPYTVVLFDE VEKAHPDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
NLGSGGNEEQ VMAAVRATFK PEFINRLDDV LIFEGLNPEE LVQIVDIQLA QLGKRLAQRR
LQLEVSLPAK QWLAHRGFDP VYGARPLRRL VQQAIGDQLA KMLLAGEVHD GDTVPVNVSP
DGDSLILG
//