ID F8GNC8_CUPNN Unreviewed; 924 AA.
AC F8GNC8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=ATP-dependent protease Clp, ATPase subunit {ECO:0000313|EMBL:AEI80303.1};
GN Name=clpC {ECO:0000313|EMBL:AEI80303.1};
GN OrderedLocusNames=CNE_2c13400 {ECO:0000313|EMBL:AEI80303.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI80303.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI80303.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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; CP002878; AEI80303.1; -; Genomic_DNA.
DR RefSeq; WP_013952998.1; NC_015723.1.
DR AlphaFoldDB; F8GNC8; -.
DR KEGG; cnc:CNE_2c13400; -.
DR HOGENOM; CLU_005070_4_2_4; -.
DR Proteomes; UP000006798; 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:AEI80303.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEI80303.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 88..231
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 900..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..546
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 924 AA; 101677 MW; C58C4983C936F5E7 CRC64;
MPTLCEICNA RPAVARVTVV QDGERKTMSI CDYDYRQLLR HQDMLNPFDS LLGGGGLSRF
FRGMGGGMDD DEHPGYSTEV PRESVDPTDA FSEQTMELLQ RAAEKAHELR RNELDTEHLL
YVLADTDVCT ALLKELKLSP QDIKGYIDEH AQTGTAEPDA AIDRMTISPR LKKAFQFAFQ
ASRDLGHSYV GPEHLLIGLA SVPDSIAGTL LKKYGVTPEA LRQKVVKVVG KGAEDGRVDT
PTGTPTLDKF GRDLTAIARQ GKLDPVLGRA QEIESTIEVL ARRKKNNPVL IGEPGVGKTA
IVEGLAQRIV NGDVPEVLRG KRLVEVNINS MVAGAKYRGE FEERAKQLID EVTAKNDELI
LFIDELHTIV GAGQGGGEGG LDIANVLKPA LARGELSLIG ATTLNEYQKY IEKDAALERR
FQPVLVPEPT VEQTIVILRG LRDKLEAHHQ VTFADDAFVA AAELSDRYIT SRFLPDKAID
LIDQAAARVR IGATSRPADI QELEAEIAQL KREQDYASSR KRFDEAKGFE DRINDKQKRL
DELTEAWQRK TGSETLEVTV AAIAEVVSRL TGIPVTDLTQ EERQKLLKME ARLRERVVGQ
EDAVVAVSDA VRLSRAGLGQ ANRPIATFLF LGPTGVGKTE LAKALAETVF GDEQAIIRID
MSEYMERHAV ARLIGAPPGY VGYDEGGQLT ERVRRKPYSV ILLDEIEKAH PDVNNVLLQV
FDDGRLTDGK GRVVDFSNTV IIATSNLGAP IIMDNLEQPE DKRMPEKDLR EALMKVLKGH
FRPEFLNRID DIIVFHALSR ENIRAIVQIQ LERVVRTAAA QDITVKLDDD LVDHLVEVGY
QPEFGARELR RQIRQSVETG LAKEILGDKL KSGDSVELGY DKASDAVVFR KMEAVQKPKA
GKAAAKGAAP KQADSTVAAG DSSA
//
