ID A0A4Y9SUR0_9BURK Unreviewed; 766 AA.
AC A0A4Y9SUR0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TFW28393.1};
GN Name=clpA {ECO:0000313|EMBL:TFW28393.1};
GN ORFNames=E4O92_21450 {ECO:0000313|EMBL:TFW28393.1};
OS Massilia horti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=2562153 {ECO:0000313|EMBL:TFW28393.1, ECO:0000313|Proteomes:UP000297258};
RN [1] {ECO:0000313|EMBL:TFW28393.1, ECO:0000313|Proteomes:UP000297258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ONC3 {ECO:0000313|EMBL:TFW28393.1,
RC ECO:0000313|Proteomes:UP000297258};
RA Peta V., Raths R., Bucking H.;
RT "Draft genome of Massilia hortus sp. nov., a novel bacterial species of the
RT Oxalobacteraceae family.";
RL Submitted (MAR-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}.
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:TFW28393.1}.
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DR EMBL; SPUM01000139; TFW28393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9SUR0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000297258; 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:TFW28393.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TFW28393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297258};
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"
SQ SEQUENCE 766 AA; 84229 MW; 5A37E20EF1D69AF5 CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN IEDLRKTLTN
FIGDNTPTVP GTGEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQQLD TQKASEGVEE AQVDGQTKES PLDQFTQNLN
KAAADGKIDP LIGREEEVDR VIQILCRRRK NNPLLVGEAG VGKTAIAEGL AWRIVQEDVP
DILGNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKDT PNGILFIDEI HTIIGAGSAS
GGTLDASNLL KPALANGQLK CIGATTFTEF RGVFEKDHAL SRRFQKVDVN EPSVEQTVAI
LRGLKSRFEE HHGVKYSSSA LSTAAELAAR FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKTEIE DIIAKIARIP PQTVNQDDRS KLQTIDRDLR NVVFGQDPAI EALASAIKMA
RAGLGKTDKP IGSFLFSGPT GVGKTEVAKQ LAFILGIELV RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESLTRRSV GFVDARAAGD EMADIKRMFT PEFRNRLDAI ISFRALDEEI
ILRVVDKFLM QLEEQLHEKK VDAVFSERLR KYLSKKGFDP LMGARPMARL IQDMIRKALA
DELLFGRLVS GGRVTVDLDD KDNVILDFPE GDVLPPPAPA EAVEIE
//