ID A0A1D9H4Q1_9BURK Unreviewed; 947 AA.
AC A0A1D9H4Q1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:AOY94856.1};
GN ORFNames=BKK79_23610 {ECO:0000313|EMBL:AOY94856.1};
OS Cupriavidus sp. USMAA2-4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY94856.1, ECO:0000313|Proteomes:UP000178101};
RN [1] {ECO:0000313|EMBL:AOY94856.1, ECO:0000313|Proteomes:UP000178101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY94856.1,
RC ECO:0000313|Proteomes:UP000178101};
RA Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT "Complete genome sequences of three Cupriavidus strains isolated from
RT various Malaysian environments.";
RL Submitted (OCT-2016) 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; CP017749; AOY94856.1; -; Genomic_DNA.
DR RefSeq; WP_071038974.1; NZ_CP017749.1.
DR AlphaFoldDB; A0A1D9H4Q1; -.
DR STRING; 876364.BKK79_23610; -.
DR KEGG; cuu:BKK79_23610; -.
DR Proteomes; UP000178101; Chromosome 2.
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: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 Gene3D; 4.10.860.10; UVR domain; 1.
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; 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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA/B PROTEASE ATP BINDING SUBUNIT-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AOY94856.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AOY94856.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000178101};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 86..229
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 897..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..548
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 947 AA; 102890 MW; 7BDFDE7D99C7E90E CRC64;
MPALCDLCHA RPAVARVSVT EDGARRTLSI CDYHYRQLLR HQEMLNPFDS LLGAGSGLSR
WLGEAGEAGY GALLAAEVPR ESVDPTDAFS EQTLELLQRA AEKAHELRRG ELDSEHLLYV
LADNDIAAAL LKELKLSAAD IRAYIDEHAH TGRADPDMPL ERMTVSPRLK KALQFAFQAS
HELGHSYVGP EHLLIGLAAV PDSIAGALLR KYGVTPEALR QKVVKVVGKG AEDGRIEQGT
GTPHLDKVGR DLTAMARQGK LDPVLGRSQE IESTIEVLAR RKKNNPVLIG EPGVGKTAIV
EGLAQRIVNG DVPEVLRDKR LVEVNINAMV AGAKYRGEFE ERAKQLIDEV TARQDELILF
VDELHTIVGA GQGGGEGGLD IANVLKPALA RGELSLIGAT TLNEYQKYIE KDAALERRFQ
PVLVPEPTVE QTIVILRGLR DKLEAHHQVT FSDEAFVAAA ELADRYVTSR FLPDKAIDLI
DQAAARVRIG ATSRPAAIQE LEAEVAQLKR EQDYAASRKR FDEAKGFEER IGARRKELDE
QVEAWQRKTG SETLEVTVAV VAEVVSRLTG IPVAELTQEE RQKLLAMEAT LRERVIGQDD
AVVAVSDAVR LSRAGLGHAN RPIATLLFLG PTGVGKTELA KALAETVFGD EQAIIRIDMS
EYMERHAVAR LIGAPPGYVG YEEGGQLTER VRRRPYSVIL LDEIEKAHPD VYNVLLQVFD
DGRLTDGKGR VVDFTHTILI ATSNLGASII MENLARPEAS RQSDKAIREA LMGVLKGHFR
PEFLNRIDEI IVFHALSEAN IRAIVQIQLD RIARTAAAQD IRLEFGEGLV AHLVELGYQP
EFGARELKRQ IRQVIETRLA KQILGDALQS GDSVRIDFDQ DSGEVRFDKL AAAAGAASGP
ASAAGPAPAS GADGAGAPAA HKAARPPAAK PAKRAARANG DRPGQPG
//