ID A0A0H3KGF1_BURM1 Unreviewed; 889 AA.
AC A0A0H3KGF1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Protease associated ATPase {ECO:0000313|EMBL:BAG42285.1};
GN Name=clpB {ECO:0000313|EMBL:BAG42285.1};
GN OrderedLocusNames=BMULJ_00310 {ECO:0000313|EMBL:BAG42285.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG42285.1, ECO:0000313|Proteomes:UP000008815};
RN [1] {ECO:0000313|EMBL:BAG42285.1, ECO:0000313|Proteomes:UP000008815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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DR EMBL; AP009385; BAG42285.1; -; Genomic_DNA.
DR RefSeq; WP_012214249.1; NC_010804.1.
DR AlphaFoldDB; A0A0H3KGF1; -.
DR STRING; 395019.BMULJ_00310; -.
DR KEGG; bmj:BMULJ_00310; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_4; -.
DR OMA; YGGERKM; -.
DR Proteomes; UP000008815; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PF02861; Clp_N; 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 Hydrolase {ECO:0000313|EMBL:BAG42285.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:BAG42285.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 154..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 96117 MW; 7EE455DB0E5FF57B CRC64;
MSTPLKTLIT KLNPLCRHAA ERAASACLAR GHYEVDLEHL FLALLEEPAG DLSLALRASR
IDAHALRADL ERELTRLKTG NTRTPVFSVH LIALFEQAWL IASLDSQLGR IRSGHLLLAL
LTAPDLAQFA QRMSARFSEV NVTDLKHKFD EITAGSSEAE PHRADAEHGD AAAPAEGGAP
AAGASKTPAL DTYTTNLTQR ARDGKIDPVI GREAEIRQAI DILMRRRQNN PIMTGEAGVG
KTAVVEGLAL RIAADDVPPP LRGVALHVLD MGLLQAGASV KGEFENRLKS VIDEVKKSPH
PIILFIDEAH TIIGAGGQAG QNDAANLLKP ALARGELRTI AATTWSEYKK YFEKDAALAR
RFQVVKVEEP SESLAAAMLR GMAGLMEKHF NVRILDDAIT EAVRLSHRYI SGRQLPDKAI
SVLDTACAKV ALAHSATPAA IDDTKKRTER IDAEIASLER DAASGAAHDE RLGELRGARD
AALEQLAKDE ARYEAERAIV AEITALRETL DRARAPADDG QPVDVQATRE KLAERVAALH
ALQGGEPMVP LQVDGHVVAE IVAAWTGIPL GRMVKDEIGT VLNLKPLLAA RVIGQDHALE
AIAQRVRTAS ANLEDPNKPR GVFMFVGPSG VGKTETALAL ADILYGGERK MITINMSEYQ
EAHSVSGLKG SPPGYVGYGE GGVLTEAVRR NPYSVVLLDE VEKAHPDVLE MFFQVFDKGM
MDDAEGREID FRNTLIILTS NVGSAAVMQA CLNKPAEELP DPDALAEALR PQLYKAFKPA
FLGRMKVVPY YPISDDVLAE IIELKLERIR SRIEANHKAA FEWDESLVEA VLARCTEVDS
GARNVDHILN GTLLPEIAGH VLGRIADGAS IARIAVRADD AGEFAYTVE
//