ID A0A3N8MF82_9BURK Unreviewed; 956 AA.
AC A0A3N8MF82;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RQS67302.1};
GN ORFNames=DID96_22370 {ECO:0000313|EMBL:RQS67302.1};
OS Burkholderia sp. Bp8963.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2184547 {ECO:0000313|EMBL:RQS67302.1, ECO:0000313|Proteomes:UP000274808};
RN [1] {ECO:0000313|EMBL:RQS67302.1, ECO:0000313|Proteomes:UP000274808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8963 {ECO:0000313|EMBL:RQS67302.1,
RC ECO:0000313|Proteomes:UP000274808};
RA Hall C., Sahl J., Wagner D.;
RT "Comparative analysis of Burkholderia isolates from Puerto Rico.";
RL Submitted (AUG-2018) 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, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQS67302.1}.
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DR EMBL; QTQP01000027; RQS67302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N8MF82; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000274808; Unassembled WGS sequence.
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; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA/B PROTEASE ATP BINDING SUBUNIT-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; 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|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:RQS67302.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RQS67302.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 87..230
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 894..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 499..545
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 935..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 104727 MW; 876AD115A77BE72E CRC64;
MPALCDICHA RPAVARATVT QNGERKSISI CDYHYRQLMR HQSMLNPFDT LLGGGSDLSH
FFGGFGDEGH DDGHLAAELP RESVDATDAF SEQTLELLQR AAEKAHELRR TELDTEHLLY
VLADTDVCAA LLKELKLSPD DIRRYIDEHA QTGTADPDAP VDRMTISPRV KKAIQFAFQA
SRDLGHSYIG PEHLLIGLAA VPDSIAGALL KKYGVTPEAL RQKVVKVVGK GAEDGRIDTP
TGTPNLDKFG RDLTALARQG KLDPVLGRAQ EIESTIEVLA RRKKNNPVLI GEPGVGKTAI
VEGLAQRIVN GDVPEVLRNK RLVEVNINSM VAGAKYRGEF EERAKQLIDE VTAKQDELVL
FIDELHTIVG AGQGGGEGGL DIANVLKPAL ARGELSLIGA TTLNEYQKYI EKDAALERRF
QPVLVPEPSV EQTIVILRGL RDKLEAHHQV TFTDDAFVAA AEFADRYITS RFLPDKAIDL
IDQAAARVRI GSTSRPAAIQ ELEAELAQLK REQDYASSRK RFDEAKRFEE RIADKQTQLD
EQMEAWQRKT GSETLEVTVA SVADVVSRLT GIPVSELTQE ERQKLLQMEA RLRERVVGQA
DAVVAVSDAV RLSRAGLGHT HRPIATFLFL GPTGVGKTEL AKALAETVFG DEQAIVRIDM
SEYMERHAVA RLIGAPPGYV GYDEGGQLTE RVRRRPYSVI LLDEIEKAHP DVYNVLLQVF
DDGRLTDGKG RVVDFSNTIL IATSNLGAAI IMDNLTQPDA ARKTDKAIKG ELMQVLKGHF
RPEFLNRIDE IIVFDALSKD DIRAIVKIQL DRVIRTAAAQ DITLTFGDAL VDHLADVGHQ
PEFGARELKR QIRQIIETRL AKEILGDTLK SGDRVEIDYD KASDVVTFNK LSPAQDASKD
GKAADDANAS GDTSGDGHVA AEAAGDLPSD IRDAAAKAPA RKTSRAKSSG DKKEAR
//