ID A0A158GC57_9BURK Unreviewed; 877 AA.
AC A0A158GC57;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Protease associated ATPase ClpB {ECO:0000313|EMBL:SAL29602.1};
GN ORFNames=AWB64_02534 {ECO:0000313|EMBL:SAL29602.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL29602.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL29602.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL29602.1};
RA Oliw E.H.;
RL Submitted (JAN-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}.
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DR EMBL; FCOC02000006; SAL29602.1; -; Genomic_DNA.
DR RefSeq; WP_060819312.1; NZ_FCOC02000006.1.
DR AlphaFoldDB; A0A158GC57; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000054893; 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: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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:SAL29602.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SAL29602.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..155
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 154..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 95226 MW; 9C95A08829AD016C CRC64;
MSTPLKTLIA KLNPTCRQAA ERAASACLSR GHYEVELEHL FIALIDVPAS DTVLALRASN
IDQLAVRRDL ERELSRLQTG NTRTPVFSVH LIALFEQAWL IASLDAQGAL IRSGHLLLAL
ANAPELAQFA QRMSPQFASV RVDRLKHEFD QLTDGSVESQ PVHMEEASSP ASAGASRTPA
LDTYTSDLTA RARQGSIDPV IGREGEIRQA IDILMRRRQN NPIMTGEAGV GKTAVVEGLA
LRIAAGDVPV PLREVALHVL DMGLLQAGAS VKGEFENRLK QVIDEVKKSP YPIILFIDEA
HTIIGAGGQA GQNDAANLLK PALARGELRT IAATTWSEYK KYFEKDAALA RRFQVVKIEE
PSEPLAAAML RGMSALMEKH FNVRILDDAI TEAVRLSHRY VSGRQLPDKA ISVLDTACAK
VALAQSSAPA VIDDTKRRIE RTDVELASLE REAASGAPHD ERIAVLREAR AADLETLERD
EARFQQERSL AGEIEALRRQ IDAARDGGEA SSVETIRSTL DARVSELRAL QNAQPIVPLQ
VDGHVVAEIV ASWTGVPLGR MVKNELQTVL NLPALLAARV IGQDHALLAI AQRVRTASAN
LEDPDKPRGV FMFVGPSGVG KTETALALAD VLYGGERKLV TVNMSEYQEA HSVSGLKGSP
PGYVGYGEGG VLTEAVRRNP YSVVLLDEVE KAHPDVMELF FQVFDKGMMD DAEGREIDFR
NTLIILTSNV GSAAVMSACL NKSADELPGA DELAETLRPQ LFKVFKPAFL GRMKVVPYYP
IPDDVLAEII ELKLGRIARR IETNHKALFE WDESLVDAVL ARCTEVDSGA RNVDHILSGT
LLPEIAGHVL ERMASGEAIA RITVSAGDSG DFNYAIA
//
