ID A0A0H0XQG1_9SPHN Unreviewed; 859 AA.
AC A0A0H0XQG1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AAV99_00995 {ECO:0000313|EMBL:KLI64261.1};
OS Aurantiacibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI64261.1, ECO:0000313|Proteomes:UP000053455};
RN [1] {ECO:0000313|EMBL:KLI64261.1, ECO:0000313|Proteomes:UP000053455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI64261.1,
RC ECO:0000313|Proteomes:UP000053455};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL Submitted (APR-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}.
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:KLI64261.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBHU01000001; KLI64261.1; -; Genomic_DNA.
DR RefSeq; WP_047092123.1; NZ_LDCP01000001.1.
DR AlphaFoldDB; A0A0H0XQG1; -.
DR STRING; 874156.GCA_001021555_01084; -.
DR PATRIC; fig|874156.12.peg.209; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000053455; 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 Reference proteome {ECO:0000313|Proteomes:UP000053455};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..495
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 94179 MW; 583183D6289DAF48 CRC64;
MNLEKFTDRA RGFLQSAQTV AIRNSHQRIS PEHILKALLE DEEGMAAGLI QRAGGNPGTA
VQQVDALLAK IPAVSGGGAQ QTPGLDNDAV RVLDSAEQVA AKAGDEYVTV ERLLLALALA
KDSKAGKALA DAGLTAQALN TAINELRGGK TADSANAEAS YDAMKKYARD LTEVAREGKL
DPVIGRDEEI RRVIQILARR TKNNPVVIGE PGTGKTAIAE GLALRIANGD VPDSLKDRRL
MSLDLGALIA GAKYRGEFEE RLKSVLDEVK GADGEIILFI DEMHTLIGAG ASEGSMDASN
LLKPALARGE LHCIGATTLD EYQKYVEKDA ALQRRFQPVF VDEPSVEDTI SILRGIKEKY
ELHHGVRITD AAVVAAAQLS ERYISDRFLP DKAIDLMDEA ASRIRMEVES KPEEIENLDR
RIFQLKIEES ALSKETDSAS EDRLKVLREE LANVEQQSSE LTTRWQNERD KINAEAKIKE
ALDAARIELE QAQRGGDLAA AGELQYGTIP GLEKQLAEAA GHAENALLRE EVTEDDIASV
VSRWTGIPME KMLEGEREKL LNMEDVLSKR VIGQEKAINS VSKAVRRARA GLQDPGRPMG
SFLFLGPTGV GKTELTKALA EFLFDDDQAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGHL TDGQGRKVDF SNTLIILTSN
LGSQFLSNLG DDQTVADVED QVMEVVRSHF RPEFLNRLDE IILFHRLAME HMAPIVDIQV
GRVQKLLKDR KIELDLTDGA RKWLGRVGYD PVYGARPLKR AVQRYLQDPL AEMLLAGEVP
DGSTVKIDEG DGALEMVVS
//