ID A0A239ST19_9BURK Unreviewed; 765 AA.
AC A0A239ST19;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SNU87884.1};
GN Name=clpA {ECO:0000313|EMBL:SNU87884.1};
GN ORFNames=SAMEA4530655_04000 {ECO:0000313|EMBL:SNU87884.1};
OS Pandoraea sputorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU87884.1, ECO:0000313|Proteomes:UP000215126};
RN [1] {ECO:0000313|EMBL:SNU87884.1, ECO:0000313|Proteomes:UP000215126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU87884.1,
RC ECO:0000313|Proteomes:UP000215126};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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; LT906435; SNU87884.1; -; Genomic_DNA.
DR RefSeq; WP_039400867.1; NZ_LT906435.1.
DR AlphaFoldDB; A0A239ST19; -.
DR STRING; 93222.NA29_24065; -.
DR KEGG; pspu:NA29_24065; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000215126; Chromosome 1.
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:SNU87884.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNU87884.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 83853 MW; 3811029D0D52D6B4 CRC64;
MIAQELEVSL HMAFMEARQA RHEFITVEHL LLALLDNPTA AEVLRACAAN LDDLRQNLRN
FIADNTPTVP GSDEVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFIS HGITKTGASG ESAKAGEGSA EGEEGANAKE SPLAQYTQNL
NQMARDGKID PLIGRESEVE RVVQVLCRRR KNNPLLVGEA GVGKTAIAEG LAWRVTRGEV
PEILQDATVY SLDMGALLAG TKYRGDFEQR LKAVLKELKE RNNAILFIDE IHTLIGAGAA
SGGTLDASNL LKPALSSGQL KCIGATTFTE YRGIFEKDAA LSRRFQKIDV NEPTVEQTVQ
ILRGLKSRFE EHHGVKYSSS ALSAAAELSA KFITDRHLPD KAIDVIDEAG AAQRILPKSK
QKKTIGKGEI EEIVSKIARI PAQSVSADDR GKLQTLDRDL KSVVFGQDPA IDALSAAIKM
SRAGLGKTDK PIGAFLFSGP TGVGKTEVAK QLAFTLGIEL IRFDMSEYME RHAVSRLIGA
PPGYVGFDQG GLLTEAVTKK PHCVLLLDEI EKAHPDIFNV LLQVMDHGTL TDNNGRKADF
RNVIIIMTTN AGAETINRAS IGFTNERQAG DEMADIKRMF TPEFRNRLDS IISFKPLDEQ
IILRVVDKFL IQLEDQLHEK KVEVVFTDKL RAYLSKKGFD PLMGARPMQR LIQDTIRRAL
ADELLFGRLT SGGRVTVDLD ENDQVQLSFP EDGNTKAQPE AAEVE
//