ID K5XPP4_9PROT Unreviewed; 859 AA.
AC K5XPP4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=MXAZACID_14718 {ECO:0000313|EMBL:EKM98629.1};
OS Acidocella sp. MX-AZ02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKM98629.1, ECO:0000313|Proteomes:UP000006217};
RN [1] {ECO:0000313|EMBL:EKM98629.1, ECO:0000313|Proteomes:UP000006217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKM98629.1,
RC ECO:0000313|Proteomes:UP000006217};
RX PubMed=23405365;
RA Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT AZ02.";
RL Genome Announc. 1:E00041-12(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}.
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:EKM98629.1}.
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DR EMBL; AMPS01000203; EKM98629.1; -; Genomic_DNA.
DR RefSeq; WP_008495247.1; NZ_JH976209.1.
DR AlphaFoldDB; K5XPP4; -.
DR STRING; 1214225.MXAZACID_14718; -.
DR PATRIC; fig|1214225.3.peg.2861; -.
DR HOGENOM; CLU_005070_4_1_5; -.
DR Proteomes; UP000006217; 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 Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 94189 MW; 887ADCB96C95C3A3 CRC64;
MDFEKFTERA RGFVQAAQTI AMREYNQQIT PEHLLKAFLD DEEGAASGLI RIAGGDPQAA
KQAVDAAVAK LPKVQGAGAG QPNVTPDLVR VLDAAQQAAQ KAGDSFVAQD RMLVALAAGE
TAAARALKTA GVSAQALEKA VADMRKGRKV DSATAEQQFD ALKKYAKDVT QLAREQKLDP
VIGRDEEIRR AIQVLARRTK NNPVLIGEPG VGKTAIVEGL ALRIVNGDVP ESLRNKRVLA
LDLGALVAGA KFRGEFEERL KAVLKEIESA EGEIILFIDE MHTLVGAGKS DGAMDASNLL
KPELARGALH CVGATTLDEY RKYVEKDAAL ARRFQPVFVS EPSVADTISI LRGIKEKYEL
HHGVRIADNA LVAAATLSNR YITDRFLPDK AIDLVDEAAS RLRMQVDSKP EALDELDRRL
IQLKIEREAL KKETDTASRE RLEKLEFELG ELEERSAEMT AKWQAEKAQL TDVQKVKEQL
EQARNEVELA QRKGDLGKAS ELLYGRIPEL EKQLAAQQDG QMVNDAVTED SIAAVVSRWT
GVPVEKMLEG ERAKLLRMED DLRHRVVGQE AALVAVSNAV RRARAGLQDP NRPIGSFLFL
GPTGVGKTEL TKALAEFLFD DERAMVRIDM SEFMEKHAVS RLIGAPPGYV GYDEGGVLTE
AVRRRPYQVV LFDEVEKAHE DVFNVLLQVL DDGRLTDGQG RTVDFKNTII VLTSNLGSDI
LAAQTEGEDV RLAEAGVMAR VREHFRPEFL NRLDEIVLFG RLQRADMGAI VSIQLKRLEA
LLAERNIRLE LDQSARDWLA EAGYDPVYGA RPLKRVIQRN LQNPLAGLIL EGAVKDGESV
KVSGSPDGLV IGGHLAEAA
//
