ID A0A519ETZ8_9BURK Unreviewed; 723 AA.
AC A0A519ETZ8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RZI66971.1};
DE Flags: Fragment;
GN Name=clpA {ECO:0000313|EMBL:RZI66971.1};
GN ORFNames=EOP80_18845 {ECO:0000313|EMBL:RZI66971.1};
OS Variovorax sp.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1871043 {ECO:0000313|EMBL:RZI66971.1, ECO:0000313|Proteomes:UP000315748};
RN [1] {ECO:0000313|EMBL:RZI66971.1, ECO:0000313|Proteomes:UP000315748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PMG_208 {ECO:0000313|EMBL:RZI66971.1};
RX PubMed=30498029; DOI=.1073/pnas.1812668115;
RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA Murphy G.P., McGenity T.J., Murrell J.C.;
RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
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:RZI66971.1}.
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DR EMBL; SEGR01000492; RZI66971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A519ETZ8; -.
DR Proteomes; UP000315748; 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; 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:RZI66971.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZI66971.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000315748};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..114
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 112..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RZI66971.1"
FT NON_TER 723
FT /evidence="ECO:0000313|EMBL:RZI66971.1"
SQ SEQUENCE 723 AA; 78852 MW; 3E0ECA0D813B461C CRC64;
ALLDNPSAAE VLRACSANVD DLRASLTNFI KDNTPQVAGT DDVDTQPTLG FQRVIQRAIM
HVQSTGNGKK EVTGANVLVA IFGEKDSHAV YYLHQQGVTR LDVVNFIAHG IKKSDPPEAT
KGSSESSSSE GEEGGGEKNE KASPLEQFTQ NLNQAAKDGK IDPLIGREYE VERVIQILCR
RRKNNPLLVG EAGVGKTAIA EGLAWRITQG DVPEILAESH VYSLDMGALL AGTKYRGDFE
QRLKGVLKSL KDKPNAILFI DEIHTLIGAG AASGGTLDAS NLLKPALSSG QLKCIGATTF
TEYRGIFEKD AALSRRFQKV DVVEPTVQET VEILKGLKSR FEEHHGVKYA VAALQAAAEL
SAKYINDRHL PDKAIDVIDE AGAAQRILAP SKRKKTISKT EVEDIVAKIA RIPPANVSND
DRGKLQTIER DLKSVVFGQD KALEVLASAV KMARSGLGRA DKPIGSFLFS GPTGVGKTEA
AKQLAYIMGI ELIRFDMSEY MERHAVSRLI GAPPGYVGFD QGGLLTEAVT KKPHAVLLLD
EIEKAHPDIF NVLLQVMDHG TLTDNNGRKA DFRNVIIVMT TNAGAETMNK ATIGFTNPRQ
AGDEMADIKR LFTPEFRNRL DATVSFKALD EVVILRVVDK FLLQLEQQLT EKKVDVTFSD
ALRKHLAKTG FDPLMGARPM QRLIQDTIRR ALADELLFGR LIDGGRLSVD IDDKNEVVLD
IQP
//
