ID A0A4R6UFR7_9BURK Unreviewed; 781 AA.
AC A0A4R6UFR7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TDQ43735.1};
GN ORFNames=DFR43_10585 {ECO:0000313|EMBL:TDQ43735.1};
OS Tepidicella xavieri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidicella.
OX NCBI_TaxID=360241 {ECO:0000313|EMBL:TDQ43735.1, ECO:0000313|Proteomes:UP000295510};
RN [1] {ECO:0000313|EMBL:TDQ43735.1, ECO:0000313|Proteomes:UP000295510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19605 {ECO:0000313|EMBL:TDQ43735.1,
RC ECO:0000313|Proteomes:UP000295510};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-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:TDQ43735.1}.
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DR EMBL; SNYL01000005; TDQ43735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6UFR7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295510; 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:TDQ43735.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDQ43735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295510};
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 143..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85946 MW; 04BEE73217F90E98 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN IDDLRKSLTN
FIKDNTPQVA GTEEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNYIA HGIRKSDPPE PSKPSEGGAA DQEEAPETRG SHEKASPLEQ
FTLNLNQAAK DGKIDPLIGR EYEVERVIQI LCRRRKNNPL LVGEAGVGKT AIAEGLAWRI
VQKDVPEILA DATVYSLDMG ALLAGTKYRG DFEQRLKGVL KTLKDKPNAI LFIDEIHTLI
GAGAASGGTL DASNLLKPAL SSGQLKCIGA TTFTEYRGIF EKDAALSRRF QKVDVLEPTV
EQTVDILKGL KSRFEEHHSV KYAHAALQAA AELSAKYIND RHLPDKAIDV IDEAGAAQRI
QVPSKRKKTI GKAEIEEIVA KIARIPPASV SSDDRSKLQT LERDLKAVVF GQDKALEVLA
SAVKMSRSGL GKPDKPIGAF LFSGPTGVGK TEAARQLAYI LGIELIRFDM SEYMERHAVS
RLIGAPPGYV GFDQGGLLTE AVTKKPHCVL LLDEIEKAHP DIFNVLLQVM DHGTLTDNNG
RKADFRNVII IMTTNAGAET MNKATIGFTT ERQAGDEMAD IKRLFTPEFR NRLDAIVSFK
ALDEQIILRV VDKFLLQLEQ QLAEKKVEVT FTDALRRYLA KKGFDPLMGA RPMQRLIQDT
IRRALADELL FGRLTEGGRL TVDIDTAVED KPEVKLDIQP LAKKERPSKA EPAEPEEATA
D
//
