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Entry: A0A3N8LNQ8_9BURK
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Original site: A0A3N8LNQ8_9BURK 
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
//
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