ID A0A399IZ79_9RHOB Unreviewed; 872 AA.
AC A0A399IZ79;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:RII37579.1};
GN ORFNames=DL237_17005 {ECO:0000313|EMBL:RII37579.1};
OS Pseudopuniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudopuniceibacterium.
OX NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII37579.1, ECO:0000313|Proteomes:UP000265848};
RN [1] {ECO:0000313|EMBL:RII37579.1, ECO:0000313|Proteomes:UP000265848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY03 {ECO:0000313|EMBL:RII37579.1,
RC ECO:0000313|Proteomes:UP000265848};
RA Zhang Y.-J.;
RT "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
RL Submitted (AUG-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:RII37579.1}.
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DR EMBL; QWJJ01000016; RII37579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399IZ79; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000265848; 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 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 872 AA; 95741 MW; B53440A768EFE61A CRC64;
MDLTKFTERS RGFIQAAQTI AIRENHQRLL PEHILKALMD DDEGLASNLI GKAGGDVGAV
TQALAVALKK VPVIGGDSGQ IYMDNQTVKV IAEAEKVAKQ AKDTFVPVER LLTALALVKG
GARDTLEAGG VSAQKLNAAI NDIRKGRTAD TASAEDTFEA LEKYALDLTA RAEEGKIDPI
IGRDDEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLRNKRLLAL
DMGSLIAGAK YRGEFEERLK AILKEIESAA GEVILFIDEM HTLVGAGKAD GAMDAANLIK
PALARGELHC IGATTLDEYR KYVEKDAALA RRFQPVMVSE PTVEDTISIL RGIKEKYELH
HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDQLDRNIL
QMQIEIEALR NEDDAASKDR LETLERDLAD VQERSDSMTA KWQAERDKLA GARELKEQLD
RARADLEIAK RNGDLARAGE LSYGIIPQLE KQLGEAEEQE AEGVMVEEAV RPEQIAQVVE
RWTGIPTAKM LEGDREKLLR MEDGLHKRVI GQNSAVRALS NAVRRARAGL NDENRPLGSF
LFLGPTGVGK TELTKAVAEY LFDDDNAMVR IDMSEFMEKH SVARLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHPDVFNVLL QVLDDGVLTD GQGHKVDFKQ TLIILTSNLG
AQALSRLPEG ADAGEAKRDV LEAVRAHFRP EFLNRLDEII VFDRLARKDM NGIVDIQMSR
LLKRLAARKI TLQLDDGARQ WLADEGYDPV FGARPLKRVI QRVLQDPLAE ALLAGEVRDG
DTVPVTAGAE GLLIGNRVGA SQRGKPDEAT VH
//