ID A0A523Q4S9_9BURK Unreviewed; 770 AA.
AC A0A523Q4S9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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:TDM06485.1};
GN Name=clpA {ECO:0000313|EMBL:TDM06485.1};
GN ORFNames=C4K60_18230 {ECO:0000313|EMBL:TDM06485.1};
OS Ideonella sp. MAG2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Ideonella.
OX NCBI_TaxID=2083017 {ECO:0000313|EMBL:TDM06485.1, ECO:0000313|Proteomes:UP000319140};
RN [1] {ECO:0000313|EMBL:TDM06485.1, ECO:0000313|Proteomes:UP000319140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAG2 {ECO:0000313|EMBL:TDM06485.1};
RA Richards S., Han Y., Dugan S., Qu J., Doddapaneni H., Dinh H., Chao H.,
RA Hughes D., Muzny D., Lee S., Murali S., Worley K., Gibbs R., Poynton H.,
RA Poelchau M., Werren J., Bowen J., Vineis J.;
RT "Bacterial draft genomes recovered from genome assembly of Hyalella
RT azteca.";
RL Submitted (FEB-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:TDM06485.1}.
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DR EMBL; PTEU01000002; TDM06485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A523Q4S9; -.
DR Proteomes; UP000319140; 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:TDM06485.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDM06485.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000319140};
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 144..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 83910 MW; 9AE353077DB1068D CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACAAN IEELRKSLVA
FIRENTPTVG GAEEVDTQPT LGFQRVIQRA IMHVQSTGGG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKSDPPE PAKGSAEGGS PQEAEKEEGA EGKGSPLEQF
TANLNQMAKD GKIDPLIGRE HEVERVIQVL CRRRKNNPLL VGEAGVGKTA IAEGLAWRIT
EGDVPEVLAD ATVYALDMGA LLAGTKYRGD FEQRLKGVLK QLKESPKSIL FIDEIHTLIG
AGAASGGTLD ASNLLKPALS SGAMKCLGAT TFQEYRGIFE KDAALSRRFQ KVDVVEPSVE
QTVEILKGLK SRFEEHHSVK YALGALQAAA ELSAKYINDR HLPDKAIDVI DEAGAAQRIL
PKSKQKKTIT KAEVEEIVAK IARIPPASVS ADDRGKLKSL ERDLKSVVFG QDPAVDALAA
AIKMARSGLG KSDKPIGAFL FSGPTGVGKT EVAKQLAYIL GIELIRFDMS EYMERHAVSR
LIGAPPGYVG FDQGGLMTEA ITKKPHCVLL LDEIEKAHPD VFNVLLQVMD HGTLTDNNGR
KADFRNVIII MTTNAGAETM QKSTIGFTTR REQGDEMGDI KRLFTPEFRN RLDTIVNFKA
LDEEVILRVV DKFLLQLEQQ LAEKKVEVTF SDALRKHLGK RGFDPLMGAR PMQRLIQDTI
RRALADELLF GRLVDGGRLS VDVDAEGNTT LDIQPSGKSG DKPKAEAAAV
//