ID A0A3N8LNQ8_9BURK Unreviewed; 766 AA.
AC A0A3N8LNQ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RQS76297.1};
GN Name=clpA {ECO:0000313|EMBL:RQS76297.1};
GN ORFNames=DID96_03240 {ECO:0000313|EMBL:RQS76297.1};
OS Burkholderia sp. Bp8963.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2184547 {ECO:0000313|EMBL:RQS76297.1, ECO:0000313|Proteomes:UP000274808};
RN [1] {ECO:0000313|EMBL:RQS76297.1, ECO:0000313|Proteomes:UP000274808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8963 {ECO:0000313|EMBL:RQS76297.1,
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:RQS76297.1}.
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DR EMBL; QTQP01000002; RQS76297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N8LNQ8; -.
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:0043335; P:protein unfolding; IEA:InterPro.
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 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; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 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.
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 Hydrolase {ECO:0000313|EMBL:RQS76297.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RQS76297.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 84373 MW; 1852DD366A26C001 CRC64;
MIAQELEVSL HMAFMEARQA RHEFITVEHL LLALLDNPTA AEVLRACAAN IEDLRQNLRN
FIHDNTPTVP GTDDVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFIS HGIAKTNSGE AAKASDANSE SEDANAQKET PLAQFTQNLN
QMAKDGRIDP LIGRESEVER VVQVLCRRRK NNPLLVGEAG VGKTAIAEGL AYRITRGEVP
DILANAQVYS LDMGALLAGT KYRGDFEQRL KTVLKELKER PHAILFIDEI HTLIGAGAAS
GGTLDASNLL KPALSSGTLK CIGATTFTEY RGIFEKDAAL SRRFQKIDVT EPTVEQTVAI
LRGLKSRFEE HHGVKYSSGA LSAAAELSAR FITDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKSEIE EIIAKIARVP AQSVSQDDRS KLQTLDRDLK SVVFGQDPAI DALAASIKMA
RAGLGKMDKP IGAFLFSGPT GVGKTEVARQ LAFTLGIELI RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAVTKKP HCVLLLDEIE KAHPDIFNVL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESMQKATI GFTTRRETGD EMADIKRLFT PEFRNRLDSI ISFRSLDEEI
IMRVVDKFLI QLEEQLHEKK VDALFTDALR KHLAKHGFDP LMGARPMQRL IQDTIRRALA
DELLFGKLVN GGHVTVDVDE NDKVQLSFDK LANPPHKPNE EAVEVE
//