ID A0A132PHV4_9MYCO Unreviewed; 848 AA.
AC A0A132PHV4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AFM11_23605 {ECO:0000313|EMBL:KWX21834.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX21834.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX21834.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX21834.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-2015) 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. 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}.
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:KWX21834.1}.
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DR EMBL; LGTW01000017; KWX21834.1; -; Genomic_DNA.
DR RefSeq; WP_067853275.1; NZ_LGTW01000017.1.
DR AlphaFoldDB; A0A132PHV4; -.
DR STRING; 59750.AWC31_28330; -.
DR PATRIC; fig|59750.3.peg.2077; -.
DR Proteomes; UP000070612; 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 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:UP000070612};
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; 92459 MW; 940B583D0186B4E2 CRC64;
MDSFNPTTKT QAALTSALQA ATAAGNPQIT PAHLLMALLT QNDGIAAPLL EAVGVEPATI
RTEAERLIGR LPSATGSSSQ PQLSPEAITA ITTAQHLATE MDDEYVSTEH LMVGLATGSS
EVAKLLTNNG ASPQALREAF TKVRGSARVT SPDPEGSYQA LEKYSTDLTA RAREGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTVISL
DLGSMVAGAK YRGEFEERLK AVLDDIKNSA GQVITFIDEL HTIVGAGATG ESAMDAGNMI
KPMLARGELR LVGATTLDEY RKYIEKDAAL ERRFQQVLVG EPSVEDTVGI LRGLKDRYEV
HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL EKESDEASKD RLEKLRAELA DHKEKLAELT TRWQNEKGAI DVVRELKEQL
DTLRGEADRA ERDGDLAKAA ELRYGRIPEV EKKLDAALPV AEARENVMLK EEVGPDDIAE
VVEAWTGIPA GRMLEGETAK LLRMEEELGK RVVGQKKAVV AVSDAVRRSR AGVADPNRPT
GSFMFLGPTG VGKTELAKAL AEFLFDDERA MVRIDMSEYG EKHSVARLVG APPGYIGYDQ
GGQLTEAVRR RPYTVVLFDE IEKAHPDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
NLGAGGTEEH VMAAVRAAFK PEFINRLDDV IIFDGLNPEE LVSIVDIQLG QLAKRLAQRR
LTLEVSLPAK KWLAERGFDP LYGARPLRRL VQQAIGDQLA KMLLAGEVHD GDIVPVNLSP
DGESLVLG
//