ID A0A1M5Q2F3_9RHOB Unreviewed; 870 AA.
AC A0A1M5Q2F3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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 ORFNames=SAMN05444003_1996 {ECO:0000313|EMBL:SHH08086.1};
OS Cognatiyoonia sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatiyoonia.
OX NCBI_TaxID=1508389 {ECO:0000313|EMBL:SHH08086.1, ECO:0000313|Proteomes:UP000184074};
RN [1] {ECO:0000313|EMBL:SHH08086.1, ECO:0000313|Proteomes:UP000184074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28715 {ECO:0000313|EMBL:SHH08086.1,
RC ECO:0000313|Proteomes:UP000184074};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQXB01000002; SHH08086.1; -; Genomic_DNA.
DR RefSeq; WP_072900758.1; NZ_FQXB01000002.1.
DR AlphaFoldDB; A0A1M5Q2F3; -.
DR STRING; 1508389.SAMN05444003_1996; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000184074; 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: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:SHH08086.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHH08086.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184074};
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 870 AA; 95496 MW; FAAE161EDBB1066D CRC64;
MNLDKFTERS RGFIQAAQTI AMRENNQSLM PEHLLKALMD DEEGLSANLI TKSAGDAASV
RQSVDVAVAR LPKVTGASGQ IYMDAATGRV LAEAEKLASK ASDSFVPVER LLTALAVVKS
KAKEALVAGM VTAKGLNSAI NELRKGRTAD SATAEDSFDA LNKYARDLTE AAEQGKIDPI
IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKKLMSL
DMGALIAGAK YRGEFEERLK AILKEIEAAA GEIILFIDEM HQLVGAGKTD GAMDAANLIK
PALARGELHC IGATTLDEYR KYVEKDAALA RRFQALIVEE PTVVDTISIL RGIKEKYELH
HGVRISDSAL VSAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRQIM
QLQIEQEALK KEDDKASKDR LLKLDEELAN LQDRATEMTA KWEAERAKLE GSRELKEQLD
RARAELDIAK REGNLAKAGE LSYGVIPDLE RKLSEAEDND DLMVEEAVRP EQIADVVERW
TGIPTSKMLE GEREKLLRME EELGKRVIGQ KAAVTSVSNA VRRARAGLND ENRPLGSFLF
LGPTGVGKTE LTKAVAEYLF DDDSAMVRID MSEFMEKHAV ARLIGAPPGY VGYDEGGVLT
EAVRRRPYQV VLFDEVEKAH PDVFNVLLQV LDDGVLTDGQ GRTVDFKQTL IILTSNLGAQ
ALSQLPDGAD ASDAKRDVMD AVRAHFRPEF LNRLDETVIF DRLVREDMAG IVAIQLRRLT
DRLASRHITL DLDDGAMTWL ADEGYDPVFG ARPLKRVIQR ALQDQLAEMI LAGDVLDGST
VSVSAGADGL IVGDRLSVSN KPKPDDAIVH
//
