ID A3JMV1_9RHOB Unreviewed; 884 AA.
AC A3JMV1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=RB2150_13206 {ECO:0000313|EMBL:EBA05049.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA05049.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA05049.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA05049.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
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:EBA05049.1}.
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DR EMBL; AAXZ01000001; EBA05049.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JMV1; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000004731; 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:UP000004731};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 16..159
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 425..505
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 884 AA; 96765 MW; 3FEA3D14420B13B8 CRC64;
MGRSNAALYK ENDMNLEKFT ERSRGFLQAA QTIAQREDHQ RLLPIHLLKA LLDDEEGLAS
NLISNAGGDA QQVLELTSAE LAKMPSVSGD GSQLYMDNQT NKVLIEAEKV AKKAGDSFVP
VERILTALAM VKSKAREALD AGGVSAQKLN AAINDIRKGR TADSASAENG YDALKKYAHD
LTAAAQEGKI DPIIGRDEEI RRAMQVLSRR TKNNPVLIGE PGVGKTAIAE GLALRIVNGD
VPESLRNKRL LSLDMGALIA GAKYRGEFEE RLKAVLSEVT DAAGEIVLFI DEMHTLVGAG
KADGAMDASN LLKPALARGE LHCVGATTLD EYRKYVEKDA ALARRFQPVV VAEPTVTDTV
SILRGIKEKY ELHHGVRISD SALVSAATLS HRYITDRFLP DKAIDLMDEA ASRLRMEVDS
KPEALDALDR DIMQKQIEVE ALKLEDDKAS KTRLAKLQKE VSELMEKSSE MSAKWQAERD
KLAVARDLKE RLDRARADLD IAKREGNLGK AGELSYGVIP DLEKALAESE ANESDAVVEE
AVRPEQIAAV VERWTGIPTT RMLEGERDKL LRMEDELGRR VIGQKSAVRS VSNAVRRARA
GLNDEARPLG SFLFLGPTGV GKTELTKAVA EFLFDDDSAM VRIDMSEFME KHAVARLIGA
PPGYVGYEEG GVLTEAVRRR PYQVVLFDEV EKAHPDVFNV LLQVLDDGIL TDGQGRTVDF
KQTLIILTSN LGAQALSNMP EGADPSDARR DVMDAVRAHF RPEFLNRLDE TIIFDRLARD
DMAGIVDIQI GLLQKRLAMQ GIKMDLASEA RDWLANEGYD PVFGARPLKR VIQRALQDQL
AEMLLAGDLG DGDVIPISAG AEGLLIGDRV ATSNRTPPED SVIH
//
