ID A9BWB9_DELAS Unreviewed; 778 AA.
AC A9BWB9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit clpA {ECO:0000313|EMBL:ABX36139.1};
GN OrderedLocusNames=Daci_3503 {ECO:0000313|EMBL:ABX36139.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX36139.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX36139.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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}.
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DR EMBL; CP000884; ABX36139.1; -; Genomic_DNA.
DR RefSeq; WP_012205339.1; NC_010002.1.
DR AlphaFoldDB; A9BWB9; -.
DR STRING; 398578.Daci_3503; -.
DR GeneID; 24116820; -.
DR KEGG; dac:Daci_3503; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_4; -.
DR OMA; GRVIQEH; -.
DR Proteomes; UP000000784; Chromosome.
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:ABX36139.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABX36139.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
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 144..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 85124 MW; 7BD09A8C4E8CF5E2 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN IDDLRSALSN
FIKDNTPQVA GSDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKGEPPE PAKAENPAES EEGAGGERNE KASPLEQFTL
NLNQAAKDGK IDPLIGRDYE VERTIQILCR RRKNNPLLVG EAGVGKTAIA EGLAWRITEG
KVPEVLTEAV VYSLDMGALL AGTKYRGDFE QRLKGVLKSL KDRPNAILFI DEIHTLIGAG
AASGGTLDAS NLLKPALSSG QLKCIGATTF TEYRGIFEKD AALSRRFQKV DVVEPTVAET
VDILKGLKSR FEEHHSVQYA AAALQAAAEL SAKYINDRHL PDKAIDVIDE AGAAQRIIPV
EQRKQTIDKA EIEAIVAKIA RIPPANVSND DRSKLQTLER DLKSVVFGQD KALEALASSV
KMARSGLGKP DKPIGSFLFS GPTGVGKTEA AKQLAYILGV DLIRFDMSEY MERHAVSRLI
GAPPGYVGFD QGGLLTEAVT KKPHSVLLLD EIEKAHPDIF NVLLQVMDHG TLTDNNGRKA
DFRNVILIMT TNAGAETINK ASIGFTNPRQ AGDEMGDIKR LFTPEFRNRL DAIVSFKPLD
EQVILRVVDK FLLQLEQQLA EKRVEVTFTD ALRKHLAKKG FDPLMGARPM QRLIQDTIRR
SLADELLFGQ LVDGGRLEVD WVADADDADK GEVKLDITPQ PKQDPASEPA EPKEATAD
//