ID A0A1D8UT69_9PROT Unreviewed; 867 AA.
AC A0A1D8UT69;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:GEL64735.1};
GN ORFNames=A0U89_06520 {ECO:0000313|EMBL:AOX16843.1}, KBA01_20210
GN {ECO:0000313|EMBL:GEL64735.1};
OS Kozakia baliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Kozakia.
OX NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX16843.1, ECO:0000313|Proteomes:UP000179145};
RN [1] {ECO:0000313|EMBL:AOX16843.1, ECO:0000313|Proteomes:UP000179145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16843.1,
RC ECO:0000313|Proteomes:UP000179145};
RX PubMed=27716345;
RA Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL Microb. Cell Fact. 15:170-170(2016).
RN [2] {ECO:0000313|EMBL:AOX16843.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16843.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL64735.1, ECO:0000313|Proteomes:UP000321177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL64735.1,
RC ECO:0000313|Proteomes:UP000321177};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL Submitted (JUL-2019) 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 ---------------------------------------------------------------------------
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; CP014674; AOX16843.1; -; Genomic_DNA.
DR EMBL; BJVW01000009; GEL64735.1; -; Genomic_DNA.
DR RefSeq; WP_070402561.1; NZ_CP014674.1.
DR AlphaFoldDB; A0A1D8UT69; -.
DR STRING; 153496.A0U89_06520; -.
DR KEGG; kba:A0U89_06520; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000179145; Chromosome.
DR Proteomes; UP000321177; 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:UP000179145};
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..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 95328 MW; FC7E8097D1396696 CRC64;
MNIEKFTERS RGFLQAAQTI ALRDYHQQLT PEHLLKALLD DEEGATSGLI RAAGGDPAAV
RRANDAALAK LPKVQGGGAG QPQATPDFVR LLDHAEQSAQ KGGDAFVAQD RLLIAIAASK
TAAGQALAEG KASADALERA VAQLRKGRTV DSANAEAGFD ALKKYARDVT AVAQAGKLDP
VIGRDEEIRR TIQVLARRTK NNPVLIGEPG VGKTAIVEGL ALRIVNGDVP EALRNKKLLS
LDMGALVAGA KYRGEFEERL KAVLKEIESA EGQIILFIDE MHTLVGAGRS DGAMDASNLI
KPELARGVLH CVGATTLDEY RKYIEKDAAL ARRFQPVFVG EPSVADTISI LRGIKEKYEL
HHGVRITDNA LVAAATLSNR YITDRFLPDK AIDLVDEAAS RLRMQIDSKP EALDELDRRI
IQLKIEREAI RKEDDTASKE RLERLEAELA DLQEQSDSMS AAWHAEKDRV NSVQKLKEQL
DQARSDVDVA QRKGDLGKAS ELMYATIPNL EKQINEAQEA EQEASNKSGL FADSVTDQGI
AAVVSRWTGV PVDRMLEGER VKLLRMEDEL RKRVVGQEAA LKAVSNAVRR ARAGLQDPHR
PIGSFLFLGP TGVGKTELTK ALAQFLFDDD RAMLRIDMSE FMEKHSVARL IGAPPGYVGY
EEGGVLTEAV RRRPYQVILF DEVEKAHEDV FNVLLQVLDD GRLTDGQGRV VDFRNTIIVL
TSNLGSDILA QQPDGESTAM VQAQVMAVVR NHFRPEFLNR LDEIILFSRL QRSDMNKIVD
IQLGRLRSLL EDRKISLKLD DAATHWLAEE GYDPVYGARP LKRVIQRSLQ NPLAGLLLDG
TIHDGQEVDV SADDKGLKID GKHVEQD
//