ID A0A1I1K8U2_9BURK Unreviewed; 778 AA.
AC A0A1I1K8U2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SFC56951.1};
GN ORFNames=SAMN05216344_12269 {ECO:0000313|EMBL:SFC56951.1};
OS Polaromonas sp. OV174.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1855300 {ECO:0000313|EMBL:SFC56951.1, ECO:0000313|Proteomes:UP000218980};
RN [1] {ECO:0000313|EMBL:SFC56951.1, ECO:0000313|Proteomes:UP000218980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV174 {ECO:0000313|EMBL:SFC56951.1,
RC ECO:0000313|Proteomes:UP000218980};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKZ01000022; SFC56951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1K8U2; -.
DR STRING; 1855300.SAMN05216344_12269; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000218980; 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:SFC56951.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFC56951.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218980};
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..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 85272 MW; F845E982CD0A50CB CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN VDDLRKSLGN
FIKDNTPQVA GTDDVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNYIA HGIKKTDPPE PAKAGESAAE NEEGGEKNEK ASPLEQFTVN
LNQLAKDGKI DPLIGRNYEV ERVIQILCRR RKNNPLLVGE AGVGKTAIAE GLAWRITQKD
VPEILAEANV YSLDMGALLA GTKYRGDFEQ RLKGVLKALK DKPNAILFID EIHTLIGAGA
ASGGTLDASN LLKPALSSGQ LKCIGATTFT EYRGIFEKDA ALSRRFQKVD VVEPTVQETV
DILKGLKSRF EEHHGVKYAL AALQAAAELS AKYINDRHLP DKAIDVIDEA GAAQRILPPS
KRKKTITKAE VEEIVAKIAR IPPANVSNDD RGKLKTLERD LKSVVFGQDK ALDVLASAVK
MARSGLGKDD KPIGSFLFSG PTGVGKTEAA KQLAYIMGIE LIRFDMSEYM ERHAVSRLIG
APPGYVGFDQ GGLLTEAITK KPHAVLLLDE IEKAHPDIFN VLLQVMDHGT LTDNNGRKAD
FRNVIIVMTT NAGAETMNKA TIGFTNPREA GDEMADIKRL FTPEFRNRLD AVVSFKALDE
TVILRVVDKF LLQLETQLAE KKVEVTFTDT LRKYLGKKGF DPLMGARPMQ RLIQDTIRRA
LADELLFGRL MDGGRLTVDM KVTTDEKGVE NGEVELDIQP LAKKEGKAKP EAEAAETN
//
