ID A0A410UVB2_9BURK Unreviewed; 766 AA.
AC A0A410UVB2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:QAU35309.1};
GN Name=clpA {ECO:0000313|EMBL:QAU35309.1};
GN ORFNames=EKL02_14610 {ECO:0000313|EMBL:QAU35309.1};
OS Janthinobacterium sp. 17J80-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2497863 {ECO:0000313|EMBL:QAU35309.1, ECO:0000313|Proteomes:UP000288813};
RN [1] {ECO:0000313|EMBL:QAU35309.1, ECO:0000313|Proteomes:UP000288813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J80-10 {ECO:0000313|EMBL:QAU35309.1,
RC ECO:0000313|Proteomes:UP000288813};
RA Kim M., Maeng S., Sathiyaraj S.;
RT "genome sequence of Janthinobacteria sp. 17J80-10.";
RL Submitted (JAN-2019) 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; CP035311; QAU35309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410UVB2; -.
DR KEGG; jaj:EKL02_14610; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000288813; Chromosome.
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:QAU35309.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:QAU35309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288813};
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..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 84407 MW; 0CF73C1AE09E4682 CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN IEDLRKTLTN
FISDNTPTVP GTSEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQQSD PQKSPEGAED AQVEGQAKES PLEQFTQNLN
KAAAEGKIDP LIGREAEVER VIQTLCRRRK NNPLLVGEAG VGKTAIAEGL AWRVTQGDVP
EVLQNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKDN PNGILFIDEI HTIIGAGAAS
GGTLDASNLL KPALSSGQLK CIGATTFTEY RGVFEKDHAL SRRFQKIDVN EPTVEQTVQI
LRGLKSRFEE HHGIKYSASA LTTAAELAAR FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKAEIE DIIAKIARIP PQTVNQDDRS KLQTIDRDLK NVVFGQDPAI EALASAIKMA
RAGLGKTDKP IGSFLFSGPT GVGKTEVAKQ LAFILGIDLI RFDMSEYMER HAVSRMIGAP
PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESLQRRTI GFTEQREAGD EMADIKRMFT PEFRNRLDAV ISFKALDEEI
ILRVVDKFLM QLEEQLHEKK VDAVFSEKLR RFLAKKGFDP LMGARPMSRL IQDMIRKALA
DELLFGRLVS GGRVTVDLDE KDQVKLEFIE GDIAPPAAPL EAAEIE
//
