ID A0A099TB47_9RHOB Unreviewed; 871 AA.
AC A0A099TB47;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=PM04_08380 {ECO:0000313|EMBL:KGL01457.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL01457.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL01457.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL01457.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) 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}.
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:KGL01457.1}.
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DR EMBL; JHAK01000003; KGL01457.1; -; Genomic_DNA.
DR RefSeq; WP_038005626.1; NZ_JHAK01000003.1.
DR AlphaFoldDB; A0A099TB47; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000029829; 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:UP000029829};
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..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 95430 MW; F8BC19A8AA09EB52 CRC64;
MDLEKFTERS RGFLQAAQTI AMRESHQQLA PEHVLKALMD DDQGMASNLI SAAGGNAKRV
AEAVDSAIAK LPKVSGDSGQ TYMDRTLGQV LSEAEKLSKK AGDSFVTVER ILMALNMVKS
KAKDALDAGG VNAQGLNAAI NEIRKGRTAD SASAEDSYEA LKKYATDLTE AARAGRIDPI
IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLRNKTLMAL
DMGALIAGAK YRGEFEERLK AVLNEVTAAA GEIILFIDEM HTLVGAGKSD GAMDAANLIK
PALARGELHC IGATTLDEYR KYVEKDAALA RRFQTLMVEE PTVPDTISIL RGIKEKYELH
HGVRISDSAL VAAATLSQRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRDIL
QKQIEVEALR LEDDTASQDR LKKLEAEVAD LQQQSAEMTA QWQAERDKLE SARGLKEQLD
RARVDLDAAK REGNLARAGE LSYGVIPQLE KQLSDAENRE DEVLVEEAVR PEQIASVVER
WTGVPVSKML EGEREKLLRM EEEIASRVIG QTQAVTAVAN AVRRARAGLN DENRPLGSFL
FLGPTGVGKT ELTKALAEFL FDDDNAMVRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIILTSNLGA
QALSQLPDGA DAAEAKRDVM DAVRGHFRPE FLNRLDETII FDRLARADMN GIVDIQLNRL
TKRLAGRNIV LELDDAAKTW LADEGYDPVF GARPLKRVIQ RSLQNELAEM ILSGDVADGA
VVPVSASSDG LLVGDRIARS DRQPRQEAVV H
//
