ID M1LTZ1_9PROT Unreviewed; 865 AA.
AC M1LTZ1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CDSE_0420 {ECO:0000313|EMBL:AGF46744.1};
OS Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF46744.1, ECO:0000313|Proteomes:UP000011547};
RN [1] {ECO:0000313|EMBL:AGF46744.1, ECO:0000313|Proteomes:UP000011547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC079E {ECO:0000313|EMBL:AGF46744.1,
RC ECO:0000313|Proteomes:UP000011547};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003803; AGF46744.1; -; Genomic_DNA.
DR RefSeq; WP_015396155.1; NC_020294.1.
DR AlphaFoldDB; M1LTZ1; -.
DR STRING; 1208919.CDSE_0420; -.
DR KEGG; kde:CDSE_0420; -.
DR PATRIC; fig|1208919.3.peg.181; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000011547; 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: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 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 Hydrolase {ECO:0000313|EMBL:AGF46744.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AGF46744.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..491
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97262 MW; D00241ED8646F1F2 CRC64;
MRFDKLTTKF QQVFADAQSL AVVNDNQYIE PIHVLKILLN DSEGSAVSLL ARSGASIEKI
NSFLDKSLKS LPKVQNIDNV QISRDLQSLM IVMEKEAHQR NDSYISSELF LLAIALDKGD
LGKSLKESGL KVELLKVAIQ EMRGSSSINS SDDELNRNSL AKYTTDLTAK ASSGKLDPVI
GRDDEIRRTI QILQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNSEVPDN LKGKKVLSLD
MASLVAGAKF RGEFEERLKS VLKELSLDSG NNIIFIDELH TIMGAGKAEG SMDAGNMLKP
ALARGDLHCI GATTLDEYRK YIEKDAALER RFQKVLVDEP DVESTIAILR GLRERYEIHH
GIQITDPAIV AAAELSNRYI TDRFLPDKAI DLIDEAGSRI RMEIDSKPEV MDKLDRRIIQ
LKIEREAVKR ETDESSKKRL SFIEEELAKL QREYGDYEDI WKSEKAAVQG TQAIKEEIDN
LKAKMAELQR TGQYDKLAEI QYAVLPSLEL RLKASEAGLE NNHNSEERKF KLLRIQVGAE
EIAEVVSRAT GIPVSKMMKG EREKLLHLND FLSSRVVGQN EAVQAVSDAI LRSRAGLSDS
ARPSGSFLFL GPTGVGKTEL ARALTEFMFD SSDHIIRVDM SEFMEKHSVA RLIGAPPGYV
GYEEGGYLTE AVRRKPYCVI LLDEIEKAHP DVFNILLQVL DDGRLTDGQG RTVDFRNSVI
IMTSNLGSSE IQNMHEKTYE DVREVVLEKL KQVLRPEFLN RIDDIVVFHN LERKHMNSIV
RIQLERLKYR IENKGMYINL SDEAISELSN VGFDHQFGAR PLKRAIQNKI ENPLARLIIE
GNYVVGDTIF IDFQDNDFVF SKLDH
//
