ID A0A0M2WV13_9BURK Unreviewed; 766 AA.
AC A0A0M2WV13;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KKO65078.1};
GN Name=clpA {ECO:0000313|EMBL:KKO65078.1};
GN ORFNames=VM94_01130 {ECO:0000313|EMBL:KKO65078.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO65078.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO65078.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO65078.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-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:KKO65078.1}.
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DR EMBL; LBCO01000010; KKO65078.1; -; Genomic_DNA.
DR RefSeq; WP_034751575.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WV13; -.
DR GeneID; 56945324; -.
DR PATRIC; fig|1649647.5.peg.1156; -.
DR Proteomes; UP000034315; 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:KKO65078.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKO65078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034315};
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..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 84094 MW; AEE80CBF9942717F CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN IEDLRKTLTN
FIGDNTPTVP GTGEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQSTE SAKASEGVEE APVDGQPKES PLDQFTQNLN
KAAAEGKIDP LIGREEEVDR VIQILCRRRK NNPLLVGEAG VGKTAIAEGL AYRITQSDVP
EILQNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKDN PNGILFIDEI HTIIGAGSAS
GGTLDASNLL KPALANGQLK CIGATTYTEF RGVFEKDHAL SRRFQKVDVN EPTVEQTVQI
LRGLKSRFEE HHGVKYSASA LSTAAELAAR FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKAEIE DIIAKIARIP PQTVNQDDRS KLQTIDRDLR NVVFGQDPAI DALASAIKMA
RAGLGKTDKP IGSFLFSGPT GVGKTEVAKQ LAFILGIELI RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESLQKTSI GFTNSKQAGD EMADIKRMFT PEFRNRIDAT ISFRALDQEI
ILRVVDKFLM QLEEQLHEKK VEAVFTEKLR AFLGKKGFDP LMGARPMARL IQDMIRKALA
DELLFGRLVT GGRVTVDLDD KDQVLLEFPE PPDAAPTAAP ETVEVE
//
