ID A0A246JG26_9BURK Unreviewed; 773 AA.
AC A0A246JG26;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:OWQ91559.1};
GN Name=clpA {ECO:0000313|EMBL:OWQ91559.1};
GN ORFNames=CDN99_10480 {ECO:0000313|EMBL:OWQ91559.1};
OS Roseateles aquatilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ91559.1, ECO:0000313|Proteomes:UP000197468};
RN [1] {ECO:0000313|EMBL:OWQ91559.1, ECO:0000313|Proteomes:UP000197468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ91559.1,
RC ECO:0000313|Proteomes:UP000197468};
RX PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT nov., in the class Betaproteobacteria, and emended description of the genus
RT Roseateles.";
RL Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
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:OWQ91559.1}.
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DR EMBL; NIOF01000003; OWQ91559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JG26; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000197468; 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:OWQ91559.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OWQ91559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000197468};
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..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 84289 MW; 80566503F0F47069 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LMALLDNPSA AEVLRACAAN IEDLRKSLAQ
FIKENTPTVG GTDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKSEPPE PPKGPEGTGA ESEREEGEGQ GNGGGKGSPL
EQFTQNLNQQ ARDGKIDPLI GRELEVERVV QVLCRRRKNN PLLVGEAGVG KTAIAEGLAW
RITEGQVPDV LADAVVYSLD MGALLAGTKY RGDFEQRLKA VIKQLKDQPG AILFIDEIHT
LIGAGAASGG TLDASNLLKP ALSSGQLKCI GATTFSEYRG IFEKDAALSR RFQKIDVVEP
TVDQTIEILK GLKSRFEEHH SVKYALGALQ AAAELSAKYI NDRHLPDKAI DVIDEAGAAQ
RVLPKSKQKK TITRAEVEDI VAKIARIPPA SVSSDDRGKL KSLDRDLKSV VFGQDPAIDA
LAAAIKMARS GLGKPDKPIG SFLFSGPTGV GKTEVAKQLA YILGIELIRF DMSEYMERHA
VSRLIGAPPG YVGFDQGGLL TEAVTKKPHA VLLLDEIEKA HPDVFNVLLQ VMDHGTLTDN
NGRKADFRNV IVIMTTNAGA EAMQKSTIGF TTKREQGDEM ADIKRLFTPE FRNRLDAIVN
FGALDQDIIL RVVDKFLLQL ESQLAEKKVE VTFSDALRKQ LAAKGFDPQM GARPMQRLIQ
DMIRRALADE LLFGRLVDGG RLSVDVDDKG EVLLDITPTK KDNKPKAEPA TAD
//
