ID A0A1H8GTF1_9BURK Unreviewed; 768 AA.
AC A0A1H8GTF1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SEN47246.1};
GN ORFNames=SAMN05428959_10236 {ECO:0000313|EMBL:SEN47246.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN47246.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
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; FODC01000002; SEN47246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8GTF1; -.
DR STRING; 1881038.SAMN05428959_10236; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198691; 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:SEN47246.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEN47246.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198691};
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 146..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 84394 MW; DD3BD47C5175CADF CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN IEDLRKTLTN
FIGDNTPTVP GTGEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQQTD AAKASEGVEE GAPGGEGQTK ESPLDQFTQN
LNKSAAEGKI DPLIGREDEV DRVIQILCRR RKNNPLLVGE AGVGKTAIAE GLAYRITQSD
VPEILQNAVV YSLDMGALLA GTKYRGDFEQ RLKAVLKQLK DNPNGILFID EIHTIIGAGS
ASGGTLDASN LLKPALANGQ LKCIGATTYT EFRGVFEKDH ALSRRFQKVD VNEPTVEQTV
QILRGLKSRF EEHHGVKYSS SALSTAAELA ARFINDRHLP DKAIDVIDEA GAAQRILPKS
KQKKTIGKTE IEDIIAKIAR IPPQTVNQDD RSKLQTIDRD LRNVVFGQDP AIEALASAIK
MARAGLGKTD KPIGSFLFSG PTGVGKTEVA KQLAFILGIE LIRFDMSEYM ERHAVSRLIG
APPGYVGFDQ GGLLTEAITK KPHAVLLLDE IEKAHPDIFN ILLQVMDHGT LTDNNGRKAD
FRNVIIIMTT NAGAESLQKS SIGFTNSKQA GDEMADIKRM FTPEFRNRID ATISFRALDE
EIILRVVDKF LMQLEEQLHE KKVEAIFTEK LRKFLAKKGF DPLMGARPMS RLIQDMIRKA
LADELLFGRL VTGGRVTVDM DEKDSVKLEF PEPPDAAPTT PPETVEVD
//