ID A0A0L6T5V0_9BURK Unreviewed; 767 AA.
AC A0A0L6T5V0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KNZ31541.1};
GN Name=clpA {ECO:0000313|EMBL:KNZ31541.1};
GN ORFNames=AD742_16235 {ECO:0000313|EMBL:KNZ31541.1};
OS Methylibium sp. NZG.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ31541.1, ECO:0000313|Proteomes:UP000053102};
RN [1] {ECO:0000313|Proteomes:UP000053102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bi G.;
RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT NZG.";
RL Submitted (JUL-2015) 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:KNZ31541.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGRD01000030; KNZ31541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6T5V0; -.
DR STRING; 1686064.AD742_16235; -.
DR PATRIC; fig|1686064.3.peg.2062; -.
DR Proteomes; UP000053102; 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:KNZ31541.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KNZ31541.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053102};
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 143..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 83807 MW; 599B1091FED6CA07 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LMALLDNPSA AEVLRACSAN IDDLRKSLAG
FIKENTPTVG GNEEVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKSDPPE PAKPSEGAPG AEGEKEEGEG KGSPLDQFTQ
NLNQLARDGK IDPLIGREHE VERVIQILCR RRKNNPLLVG EAGVGKTAIA EGLAWRITQE
DVPEVLGKAV VYSLDMGALL AGTKYRGDFE QRLKGVLKQL KDQPNAILFI DEIHTLIGAG
AASGGTLDAS NLLKPALSSG AMKCIGATTF SEYRGIFEKD AALSRRFQKI DVVEPSVEQT
IEILKGLKSR FEEHHSVKYA IGALQAAAEL SAKFINDRHL PDKAIDVIDE AGAAQRILPK
NKQKKTITRA EVEEIVAKIA RIPPASVSND DRSKLKSLDR DLNSVVFGQE PAIEALAAAI
KMARSGLGKP DRPIGSFLFS GPTGVGKTEV AKQLAYILGI ELIRFDMSEY MERHAVSRLI
GAPPGYVGFD QGGLLTEAIS KKPHAVLLLD EIEKAHPDVF NVLLQVMDHG TLTDNNGRKA
DFRNVIIIMT TNAGAETMNK ATIGFTNSRE AGDEMADIKR LFTPEFRNRL DATVSFKALN
EEIILRVVDK FLLQLESQLT EKKVEVTFTD ALRKHLAKNG FDPLMGARPM QRLIQDTIRR
ALADELLFGQ LVDGGRLSVD IDADGKPLLD ITPNKKSDKP KAEPATA
//