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Database: UniProt
Entry: A0A2T4K0X7_9RHOB
LinkDB: A0A2T4K0X7_9RHOB
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ID   A0A2T4K0X7_9RHOB        Unreviewed;       870 AA.
AC   A0A2T4K0X7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:PTE23815.1};
GN   ORFNames=C5F48_00015 {ECO:0000313|EMBL:PTE23815.1};
OS   Cereibacter changlensis JA139.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=1188249 {ECO:0000313|EMBL:PTE23815.1, ECO:0000313|Proteomes:UP000241010};
RN   [1] {ECO:0000313|EMBL:PTE23815.1, ECO:0000313|Proteomes:UP000241010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA139 {ECO:0000313|EMBL:PTE23815.1,
RC   ECO:0000313|Proteomes:UP000241010};
RA   Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA   Chintalapati V.R.;
RT   "Cereibacter changlensis.";
RL   Submitted (MAR-2018) 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|ARBA:ARBA00004496,
CC       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:PTE23815.1}.
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DR   EMBL; PZKG01000001; PTE23815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4K0X7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000241010; 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 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   Reference proteome {ECO:0000313|Proteomes:UP000241010};
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   870 AA;  95957 MW;  5521A01B1793A571 CRC64;
     MNLEKFTERS RGFLQAAQTI AARESHQRLA PEHLLKALMD DDQGLAANLI RRSGGEPQRV
     TETLELTLAK LPKVTGDAQP FMDPGLVRVL DEAEKVAKKA GDSFVPVERI LMALCMVSSK
     AKEALDAGAV SAQKLNAAIN DIRKGRTADS ASAEEGYDAL KKYARDLTEA ARDGKIDPII
     GRDEEIRRAM QVLSRRTKNN PVLIGEPGVG KTAIAEGLAL RIVNGDVPES LKNKSLMALD
     MGALIAGAKY RGEFEERLKA VLNEVTQAAG EIILFIDEMH TLVGAGKSEG AMDAANLIKP
     ALARGELHCV GATTLDEYRK YVEKDAALAR RFQPVMVEEP TVEDTISILR GIKEKYELHH
     GVRISDSALV AAATLSHRYI TDRFLPDKAI DLMDEAASRL RMEVDSKPEE LDALDRQILQ
     LQIEAEALKK EEDAASKDRL ERLQKELSEL TERSSEMTAK WQDERDKLEA SRELKEQLDR
     ARAELDQVKR EGNLGRAGEL SYGIIPGLEK RLAEAEAREG DLLVSEAVWP EQIAEVVERW
     TGIPTSRMLE GEREKLLRME EELGKRVVGQ RVALTAVANA VRRARAGLND ENRPLGSFLF
     LGPTGVGKTE LTKAVAEYLF DDDQAMVRID MSEFMEKHAV ARLIGAPPGY VGYDEGGVLT
     EAVRRRPYQV ILFDEVEKAH PDVFNVLLQV LDDGVLTDGQ GRTVDFKQTL IVLTSNLGAY
     ALSQLADGAD PTAARASVME AVRGHFRPEF LNRLDETVIF ERLGRADMGA IVEIQLKRLE
     KRLAGRKIAL DLDAAAKQWL ADEGYDPVFG ARPLKRVIQR HLQDPLAEMI LSGDVMDGAT
     VHVSAGSEGL IIGDRISASR RERPQEAVVH
//
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