ID A0A3E1RIM9_9BURK Unreviewed; 773 AA.
AC A0A3E1RIM9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RFO98852.1};
GN Name=clpA {ECO:0000313|EMBL:RFO98852.1};
GN ORFNames=DIC66_02995 {ECO:0000313|EMBL:RFO98852.1};
OS Rhodoferax lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO98852.1, ECO:0000313|Proteomes:UP000260665};
RN [1] {ECO:0000313|EMBL:RFO98852.1, ECO:0000313|Proteomes:UP000260665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO98852.1,
RC ECO:0000313|Proteomes:UP000260665};
RA Park M.;
RT "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT lake.";
RL Submitted (MAY-2018) 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:RFO98852.1}.
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DR EMBL; QFZK01000001; RFO98852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1RIM9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000260665; 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:RFO98852.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RFO98852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000260665};
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 146..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..773
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; 84848 MW; 819A7D1ADC210BBF CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN IDDLRKSLAN
FIKDNTPQVA GTDEVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKNDPPE AAKSSEAPNE AEEGGAEKNE KSSPLEQYTV
NLNQLAKDGK IDPLIGREYE VERVIQILCR RRKNNPLLVG EAGVGKTAIA EGLAWRITQN
DVPEILAEAV VYSLDMGALL AGTKYRGDFE QRLKGVLKSL KDKPNGILFI DEIHTLIGAG
AASGGTLDAS NLLKPGLSSG QLKCIGATTF TEYRGIFEKD AALSRRFQKV DVVEPTVEQT
VEILKGLKSR FEEHHGVKYA VAALQAAAEL SAKYINDRHL PDKAIDVIDE AGAAQRILPP
SKRKKTISKT EVEEIVAKIA RIPAANVSND DRGKLKTLER DLRNVVFGQD KAIDVLASAV
KMARSGLGKG DKPIGSFLFS GPTGVGKTEA AKQLAYIMGI DLIRFDMSEY MERHAVSRLI
GAPPGYVGFD QGGLLTEAVT KKPHCVLLLD EIEKAHPDIF NVLLQVMDHG TLTDNNGRKA
DFRNVIIIMT TNAGAETMNK ATIGFTNPRE SGDEMADIKR LFTPEFRNRL DALVSFKALD
ENIILRVVDK FLLQLETQLA EKKVDVTFTD KLRKHLGKKG FDPLMGARPM QRLIQDTIRR
ALADELLFGR LTDGGRLTVD LDDKDESKTE VLLDIQPLPK KEGKSKPEEA TAG
//