ID A0A0N9ZZU7_9RHOB Unreviewed; 875 AA.
AC A0A0N9ZZU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=IMCC12053_1971 {ECO:0000313|EMBL:ALI55918.1};
OS Celeribacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI55918.1, ECO:0000313|Proteomes:UP000064920};
RN [1] {ECO:0000313|EMBL:ALI55918.1, ECO:0000313|Proteomes:UP000064920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI55918.1,
RC ECO:0000313|Proteomes:UP000064920};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP012023; ALI55918.1; -; Genomic_DNA.
DR RefSeq; WP_062218520.1; NZ_FOSM01000010.1.
DR AlphaFoldDB; A0A0N9ZZU7; -.
DR STRING; 1397108.IMCC12053_1971; -.
DR KEGG; cmar:IMCC12053_1971; -.
DR PATRIC; fig|1397108.4.peg.2014; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000064920; 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:UP000064920};
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 875 AA; 95521 MW; 1FA41E1B0D5D60EE CRC64;
MDMEKFTERS RGFLQAAQTI AMRENHQSLK PEHLLKALMD DSEGFASNLI MRAGGDAKAV
AASVDVAVGK LPRVSGDAGQ TYMDQSTAKV LDEAEKIAAK AGDSFVPVER LLTALALSRS
EAKKALESGG VTAQNLNEAI NDIRKGRTAD SASAEDGYEA LKKYARDLTE AAEQGKIDPI
IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIINGDVPE SLKNKKLMAL
DMGALIAGAK YRGEFEERLK SILKEIEAAS GEIILFIDEM HTLVGAGKSD GAMDAANLIK
PALARGELHC VGATTLDEYR KYVEKDAALA RRFQPIVVEE PTVEDTVSIL RGIKEKYELH
HGVRISDSAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDQLDRQIL
QLQIEAMALG KEDDDASKSR LEKLEGELAT LQEQSASMTA KWENERRKLE GARDLKEQLE
HARATLEIAK REGNLAKAGE LSYGVIPQLE KQLAEAEAVE AAGDGDLMVE EAVRPEQIAQ
VVERWTGVPT SKMLEGERDK LLRMEDGLHK RVIGQHAAVH AVANAVRRAR AGLNDENRPL
GSFLFLGPTG VGKTELTKAV AEFLFDDDNA MVRIDMSEFM EKHAVSRLIG APPGYVGYDE
GGVLTEAVRR RPYQVVLFDE VEKAHPDVFN VLLQVLDDGI LTDGQGRTVD FKQTLIILTS
NLGAQALSQM PDGADPSQAK RDVMDAVRAH FRPEFLNRLD ETIIFDRLGR ADMGGIVDIQ
LGLLAKRLAK RDITLTLDDG AKQWLADEGY DPVFGARPLK RVIQRALQDP LAESLLGGDV
NDGDSIAVMA GSDGLIIGDR KGASNRPKPD DAVVH
//