ID A0A1I3IE90_9RHOB Unreviewed; 868 AA.
AC A0A1I3IE90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05216258_1072 {ECO:0000313|EMBL:SFI46252.1};
OS Albimonas pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFI46252.1, ECO:0000313|Proteomes:UP000199377};
RN [1] {ECO:0000313|EMBL:SFI46252.1, ECO:0000313|Proteomes:UP000199377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFI46252.1,
RC ECO:0000313|Proteomes:UP000199377};
RA de Groot N.N.;
RL Submitted (OCT-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; FOQH01000007; SFI46252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3IE90; -.
DR STRING; 1114924.SAMN05216258_1072; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199377; 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:SFI46252.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFI46252.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199377};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..490
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 95039 MW; 9427BF57DCC273FA CRC64;
MNLEKFTDRA RGFVQAAQTI AMRESHQRLT PDHLLKALLD DDQGFATALI GRAGGDAQKV
RAANDLSVAK LPKVQGGQVY LDQSFAQVVD QAEQLAKKAS DSFVTVERLL TALAIQKSDA
SKALADGGVT AQALNKAIED MRKGRTADSA GAEDQFEALK KYARDLTEAA REGKIDPVIG
RDEEIRRCVQ VLSRRTKNNP VLIGEPGVGK TAIAEGLAMR IVNGDVPESL QDKKLLSLDM
GSLIAGAKYR GEFEERLKGV LNEVTSSDGE IILFIDEMHT LVGAGKGDGA MDASNLLKPA
LARGELHCVG ATTLDEYRKH VEKDAALARR FQPVFVTEPS VEDAISILRG IKEKYEVHHG
VRISDAALVA AATLSNRYIS DRFLPDKAID LMDEAASRLR MEVDSKPEEL DQLDRDILQK
QIEAEALKKE TDQASQDRLA KITQDLAQLQ EQSAAMTARW QAERDKLQGS RDLKEQLDGA
RVELENAKRR GDLAKAGELA YGVIPDLEKR LAEAESQESK DVMVEEAVLP EHVAAVVSRW
TGVPVDKMLE GERDKLLRME EVIGARVVGQ EEAVRAVSNA VRRARAGLND PNRPIGSFLF
LGPTGVGKTE LTKALAEFLF DDDQAMVRID MSEFMEKHAV SRLIGAPPGY VGYDEGGVLT
EAVRRRPYQV VLFDEVEKAH PDVFNVLLQV LDEGRLTDGQ GRTVDFRNTL VILTSNLGAE
FLTSLPDGAA ASDARDAVMG AVRAHFRPEF LNRLDEIVLF ERLSREHMDG IVTIQLKGLE
ARLADRKIHL ELAPEARTWL ADRGYDPVYG ARPLKRVIQR ALQDPLAERL LAGTIRDGEE
VPVGCGPDGL LIGDRARGAS AEAGATLH
//
