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Database: UniProt
Entry: A0A0H3KGF1_BURM1
LinkDB: A0A0H3KGF1_BURM1
Original site: A0A0H3KGF1_BURM1 
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
//
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