ID G8QJQ3_AZOOP Unreviewed; 861 AA.
AC G8QJQ3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Dsui_2161 {ECO:0000313|EMBL:AEV26527.1};
OS Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS suillum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Azospira.
OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV26527.1, ECO:0000313|Proteomes:UP000005633};
RN [1] {ECO:0000313|EMBL:AEV26527.1, ECO:0000313|Proteomes:UP000005633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC {ECO:0000313|Proteomes:UP000005633};
RX PubMed=22535943; DOI=10.1128/JB.00124-12;
RA Byrne-Bailey K.G., Coates J.D.;
RT "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT Azospira suillum strain PS.";
RL J. Bacteriol. 194:2767-2768(2012).
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; CP003153; AEV26527.1; -; Genomic_DNA.
DR RefSeq; WP_014237221.1; NC_016616.1.
DR AlphaFoldDB; G8QJQ3; -.
DR STRING; 640081.Dsui_2161; -.
DR KEGG; dsu:Dsui_2161; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005633; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 95481 MW; CADCBD9EA7BD5C8F CRC64;
MRFDKFTTKF QQALADAQSL AIGADNQFID PSHLLLALLN QDDGGTASLL ARAGVNVPPL
RTALEQAIAR LPKVEGHGGD VSIGRDLTNL LNLTDKEAQK RGDQFIASEM FLLALTGDKG
ETSRIAKQYG LEKKPLEAAI DAVRGGQGVD SQEAEGQRES LKKYCVDLTE RAAQGKLDPV
IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNDEVPE TLKGKKVLVL
DMAGLLAGAK YRGEFEERLK AVLNDIAKDE GRIILFIDEI HTMVGAGKAE GAIDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVDE PSVEATIAIL RGLQEKYELH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IKMEIDSKPE VMDKLDRRII
QLKIEREAVK KEKDEASKKR FGLIEDEIAK LQKEYSDLEE VWKAEKAQVH GAAHVKEEID
KIKAEIARLQ REGKLEKVAE LQYGKLPQLE AQLKVAEKAS EGGQQQNKLL RTQVGAEEIA
EVVSRATGIP VSKMMQGERD KLLKMEDRLH QRVVGQDEAV RLVSDAIRRS RAGLSDPNRP
YGSFLFLGPT GVGKTELCKA LAEFLFDSED HLIRIDMSEF MEKHSVARLI GAPPGYVGYE
EGGTLTEAVR RKPYSVILLD EVEKAHPDVF NVLLQVLDDG RMTDGQGRTV DFKNTVIVMT
SNLGSQMIQQ MAGDDYQLIK LAVMGEVKSY FRPEFINRID EAVVFHSLDE KNIRNIARIQ
LGYLEKRVAQ LEMRLEVADS ALDELAKAGF DPIFGARPLK RAIQQHIENP LAKQILEGNF
GPKDTILVSC DEGGVMRFAK G
//