ID A0A4Y9SWW7_9BURK Unreviewed; 766 AA.
AC A0A4Y9SWW7;
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:TFW30017.1};
GN Name=clpA {ECO:0000313|EMBL:TFW30017.1};
GN ORFNames=E4L96_00735 {ECO:0000313|EMBL:TFW30017.1};
OS Massilia arenosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=2561931 {ECO:0000313|EMBL:TFW30017.1, ECO:0000313|Proteomes:UP000298438};
RN [1] {ECO:0000313|EMBL:TFW30017.1, ECO:0000313|Proteomes:UP000298438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC02 {ECO:0000313|EMBL:TFW30017.1,
RC ECO:0000313|Proteomes:UP000298438};
RA Raths R., Peta V., Bucking H.;
RT "Draft Genome Sequence of Massilia arenosa sp. nov., a Novel Massilia
RT Species Isolated from a Sandy-loam Maize Soil.";
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:TFW30017.1}.
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DR EMBL; SPVF01000010; TFW30017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9SWW7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000298438; 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:TFW30017.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TFW30017.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000298438};
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; 84530 MW; 2AF17CA311C13229 CRC64;
MIAQELEVSL HMAFVEARQA RHEFITVEHL LLALLDNPSA AEVLRACAVN IDDLRKTLTN
FIGDNTPTVP GTGEVDTQPT LGFQRVIQRA IMHVQSASNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIS HGVRKDQQID SQKASEGVEE AQVEGQAKES PLDQFTQNLN
KAAADGRIDP LIGREEEVER VIQILCRRRK NNPLLVGEAG VGKTAIAEGL AWRIVQEDVP
EILQNAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKET PNGILFIDEI HTIIGAGSAS
GGTLDASNLL KPALANGQLK CIGATTFTEF RGVFEKDHAL SRRFQKVDVN EPSVEQTVQI
LRGLKSRFEE HHGVKYSASA LSTAAELAAR FINDRHLPDK AIDVIDEAGA AQRVLPKSKQ
KKTIGKTEIE EIISKIARIP PQTVNQDDRS KLQTIDRDLR NVVFGQDPAI DALSSAIKMA
RAGLGKQDKP IGAFLFSGPT GVGKTEVAKQ LAFILGVELI RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAITKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESLTKRSV GFVDSKAAGD EMADIKRMFT PEFRNRLDSI ISFKALDEEI
ILRVVDKFLM QLEEQLHEKK VEAVFTENLR KFLAKKGFDP LMGARPMARL IQDMIRKALA
DELLFGRLVS GGRVTVDLDE KDQIRLEFPE GDIEPPTIPP ETVEIE
//