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Database: UniProt
Entry: A0A068YLC7_9BURK
LinkDB: A0A068YLC7_9BURK
Original site: A0A068YLC7_9BURK 
ID   A0A068YLC7_9BURK        Unreviewed;       892 AA.
AC   A0A068YLC7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=ClpB protein {ECO:0000313|EMBL:CDS48470.1};
OS   Polaromonas sp. CG9_12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS48470.1, ECO:0000313|Proteomes:UP000043372};
RN   [1] {ECO:0000313|EMBL:CDS48470.1, ECO:0000313|Proteomes:UP000043372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Smith H.J., Foreman C.M., Ramaraj T.;
RT   "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT   Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT   Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 2:1-2(2014).
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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DR   EMBL; CCJP01000004; CDS48470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YLC7; -.
DR   STRING; 1504672.gene:199029830; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000043372; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          10..156
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   892 AA;  97355 MW;  E605DDA90F91306D CRC64;
     MAEISRTALF GKLNPLAYKA IEGATVLCKM RGNPYVELQH WLQQILNTQD SDLHRIVKHY
     ELDASALVAD LTRALDRLPR GASSVTDLSS FIEDAVERAW VYGSLMFGER QVRSGHLLVG
     MLKTASLRNT LFSISRQFER VKLEDLCDHF AQLLAGSPEN QLAASDAQGE PGEASGAMAP
     AAMGKQEALK RFTTDLTEQA RGGKMDPIVG RDDEIRQVVD ILMRRRQNNP ILVGEAGVGK
     TAVVEGFAQR IARGDVPPSL KDVALRALDI GLLQAGASMK GEFEQRLRSV IDEVQASAQP
     IILFIDETHT LVGAGGAAGT GDAANLLKPA LARGQLRTIG ATTFAEYKKH IEKDPALTRR
     FQSVQIDEPD EPKALLMMRG VASTMERHHK VQIFDEALEA AVKLSHRYIP ARQLPDKSVS
     LLDTACARVA VSLHATPAEV DDSAKRIEAL ETELQIIGRE SAIGVDTVQR EANAKALLSD
     ERTRFDAVNE RWRTEKELVD RLLALRARLR DGGAPVEGEA VGEGVLSPEA RAAALAQLKD
     LQAQLEQLQG ETPLILPTVD YQAVASVVAD WTGIPVGRMA ANEIGNILNL PATLGQRVIG
     QNHAMEMIAK RIQTSRAGLD NPGKPIGVFM LAGPSGVGKT ETAIALAEAL YGGEQNLITI
     NMSEYQEAHT VSTLKGAPPG YVGYGEGGVL TEAVRRKPYS VVLLDEVEKA HSDVHEIFFQ
     VFDKGFMEDG EGRFINFKNT LILLTTNVGT ELIASMCKDP SLMPDPESLA KSLRGPLLKV
     FPPALLGRLV TIPYFPLSDE MLGRIVTLQI GRVRRRVEQR YKIPFEVSDD VVKLVVSRCT
     ESESGGRMID AILTNTMLPD ISREFLKRML EGKPIQRVQV GVRDGAFDYA FG
//
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