GenomeNet

Database: UniProt
Entry: A0A1D8UT69_9PROT
LinkDB: A0A1D8UT69_9PROT
Original site: A0A1D8UT69_9PROT 
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
//
DBGET integrated database retrieval system