ID A2S0W7_BURM9 Unreviewed; 884 AA.
AC A2S0W7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Putative ATP-dependent Clp protease, ATP-binding subunit ClpB {ECO:0000313|EMBL:ABN00275.2};
GN OrderedLocusNames=BMA10229_1788 {ECO:0000313|EMBL:ABN00275.2};
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN00275.2, ECO:0000313|Proteomes:UP000002283};
RN [1] {ECO:0000313|EMBL:ABN00275.2, ECO:0000313|Proteomes:UP000002283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN00275.2,
RC ECO:0000313|Proteomes:UP000002283};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (JAN-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; CP000545; ABN00275.2; -; Genomic_DNA.
DR RefSeq; WP_011832137.1; NC_008835.1.
DR AlphaFoldDB; A2S0W7; -.
DR KEGG; bml:BMA10229_1788; -.
DR HOGENOM; CLU_005070_1_1_4; -.
DR Proteomes; UP000002283; Chromosome II.
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; 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, ECO:0000313|EMBL:ABN00275.2};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:ABN00275.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:ABN00275.2};
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 884 AA; 96021 MW; 634D5B163A032E78 CRC64;
MSDIGRVTLF GKLNTFLYET LEQATGFCRL RGNPYVELAH WLNQMLRRPD SDVHRILRRF
DIDAAAIDRG IVSALDRLPR GAGSVSDLSA HIDDAVERAW VYATLKYDAA QIRGAVLLLA
LVKTPQLRNV LYAIARDFER IVPDVLADEL ERIVAGSPEA PSPAARAAAG AIGDAGAAPS
AAREGSALAR YAIDLTARAR AGEIDPVVGR DGEIRQIVDI LLRRRQNNPL LVGEAGVGKT
AVAEGFALRI VAGDVPPPLR DVELYLLDIG LLQAGASVKG EFESRLRGVI DEASSSERPV
ILFIDEVHTL VGAGGAAGTG DAANLLKPAL ARGLLRTIGA TTWSEYKQYI EKDPALTRRF
QLVQVREPEE GAALAMLRGL AAKLEAHHRV LVLDDALQAA VTLSHRYIPA RQLPDKAISL
LDTACARVAV SQYAVPAPIE DVRRRIDSLR VERELIAREC ALGAGDAQRL DAIDASIAGE
QTTLDALDAR WQAERDALGK IVDWRASLLA DDSSRVLDEA ARADVQAKLS AALRALAELQ
GETPLVLPAV DTHAVAAVVS DWTGIPLGRM VRDEMQSVLK LAETLAERVV GQPHAVELIA
ERIQTARARL DDPAKSHGVF LLCGPSGVGK TETALALAEM LYGGEHNAIT INMSEFQEAH
TVSTLKGAPP GYVGYGQGGV LTEAVRRRPY SVVLLDEIEK AHRDVHEIFF QVFDKGWMED
GEGRYIDFRN TVILLTSNVG SERVMQLCRD PQRLPDAQTL TDALREVFPA ALLGRLTVVP
YYPLTDEMLA RIVALQLARI ERRIEAHHGI ALRCADSATA LIAERCRTIE SGGRMVDAIL
THTVLPRISQ EILRATIEGR ALRAIDVSAE DGQFVYRFEE EGAT
//
