ID A9D7P8_HOEPD Unreviewed; 874 AA.
AC A9D7P8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HPDFL43_16626 {ECO:0000313|EMBL:EDQ33119.2};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ33119.2, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ33119.2, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33119.2,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ33119.2, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ33119.2,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-2012) 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:EDQ33119.2}.
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DR EMBL; ABIA03000004; EDQ33119.2; -; Genomic_DNA.
DR RefSeq; WP_040449361.1; NZ_CM002917.1.
DR AlphaFoldDB; A9D7P8; -.
DR STRING; 411684.HPDFL43_16626; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004291; Chromosome.
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:UP000004291};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 96178 MW; 62D1AB2FBDF1CDAC CRC64;
MNIEKYSERV RGFIQSAQSH ALAEGHQQFV PEHLLKVLMD DDQGMASSLI ERAGGRPADV
RLANDAALAK LPKVSGGNGQ LYLSQPMAKV FQTAEDAAKK AGDSFVTVER LLLALAIESS
AATSKTLSKA GLTAQALNQT INEIRKGRTA DSAGAEQGFD ALKKYARDLT QAARDGKLDP
VIGRDDEIRR TIQVLSRRTK NNPVLIGEPG VGKTAIAEGL ALRIVNGDVP ESLKDKELMA
LDMGALIAGA KYRGEFEERL KAVLSEIQAN NGEIILFIDE MHTLVGAGKA DGAMDASNLL
KPALARGELH CVGATTLDEY RKHVEQDAAL ARRFQPVMVE EPSVEDTVSI LRGLKEKYEQ
HHKVRVSDSA LVSAAVLSNR YITDRFLPDK AIDLVDESAA RLRMQVDSKP EELDELDRRI
MQLKIEREAL KKEADQASKD RLERLERELS DIEEKSDALT ARWQSEKQKL GLAADIKLQL
EEARNELAIA QRKGEFQRAG ELAYGEIPAL EQQLVEAEAH GEADTGMVEE TVTPDHIAHI
VSRWTGIPVD RMLEGERDKL LRMEDEIGKR VIGQGEAVQA VSKAVRRARA GLQDPNRPMG
SFIFLGPTGV GKTELTKALA EFLFDDETAL IRMDMSEYME KHSVARLIGA PPGYVGYDEG
GALTEAVRRR PYQVILFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRTVDF RNTLIVMTSN
LGAEYLVALG EDQDADAARD DVMNVVRSAF RPEFLNRVDE IILFHRLRRS EMGAIVDIQL
GRLGKLLADR KIEVALDDPA RDWLAEKGYD PAYGARPLKR VVQKYVQDPL AEKLLMGEVG
DGAKVSVSAG SDRLLFSVTD QKVADADGPE VEAA
//