ID A0A4U8VCG0_9BURK Unreviewed; 761 AA.
AC A0A4U8VCG0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TMS56593.1};
GN Name=clpA {ECO:0000313|EMBL:TMS56593.1};
GN ORFNames=MW7_016035 {ECO:0000313|EMBL:TMS56593.1};
OS Burkholderiaceae bacterium PBA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae.
OX NCBI_TaxID=795666 {ECO:0000313|EMBL:TMS56593.1, ECO:0000313|Proteomes:UP000004277};
RN [1] {ECO:0000313|EMBL:TMS56593.1, ECO:0000313|Proteomes:UP000004277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBA {ECO:0000313|EMBL:TMS56593.1,
RC ECO:0000313|Proteomes:UP000004277};
RA Gan H.M.;
RT "Revised genome assembly of Burkholderiaceae (previously Ralstonia) sp.
RT PBA.";
RL Submitted (MAY-2019) 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:TMS56593.1}.
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DR EMBL; AKCV02000026; TMS56593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8VCG0; -.
DR STRING; 795666.MW7_2624; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004277; 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:TMS56593.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TMS56593.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004277};
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 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83427 MW; 63419DE179B01225 CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LQALLDNPTA AEVLRACAAN IEDLRTSLKN
FIVDNTPVVS GTDEVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFIS HGIRKDQAEA AKQGEGSAET EAGDGKESPL EQYTQNLNAL
AKAGKIDPLI GREQEVERVV QILCRRRKNN PLLVGEAGVG KTAIAEGLAW RITKGEVPEI
LEKASVYSLD MGALLAGTKY RGDFEQRLKG VLKSLKDNPN AILFIDEIHT LIGAGAASGG
TLDASNLLKP ALSSGQLKCI GATTFTEYRG IFEKDAALSR RFQKVDVVEP SVEQTVQILR
GLKSRFEEHH GVKYAAAALT AAAELSARFI TDRHLPDKAI DVIDEAGAAQ RILPKSKQKK
TIGKDEIEDI VSRIARIPPQ SVSQDDRSKL QTLDRDLKSV VFGQDPAIEA LAAAIKMSRA
GLGKTDKPIG SFLFSGPTGV GKTEVAKQLA FILGIELLRF DMSEYMERHA VSRLIGAPPG
YVGFDQGGLL TEAVTKKPHC VLLLDEIEKA HPDIFNILLQ VMDHGSLTDN NGRKADFRNV
IIIMTTNAGA ETMNKAVIGF TAAREAGDEM ADIKRMFTPE FRNRLDAMIS FRALDEEIIL
RVVDKFLMQL EEQLHEKKVD ATFSEALRKY LAKKGFDPLM GARPMQRLIQ DLIRKALADE
LLFGRLVKGG KVHVDLDEHE AIQLAFEEPA SAPPTQEAAE A
//