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Database: UniProt
Entry: C1CVH0_DEIDV
LinkDB: C1CVH0_DEIDV
Original site: C1CVH0_DEIDV 
ID   C1CVH0_DEIDV            Unreviewed;       747 AA.
AC   C1CVH0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Putative ATP-dependent Clp protease, ATP-binding subunit ClpC {ECO:0000313|EMBL:ACO46187.1};
GN   OrderedLocusNames=Deide_12680 {ECO:0000313|EMBL:ACO46187.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46187.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO46187.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP001114; ACO46187.1; -; Genomic_DNA.
DR   RefSeq; WP_012693310.1; NC_012526.1.
DR   AlphaFoldDB; C1CVH0; -.
DR   STRING; 546414.Deide_12680; -.
DR   PaxDb; 546414-Deide_12680; -.
DR   KEGG; ddr:Deide_12680; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_0; -.
DR   OMA; HDKFLPD; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000002208; 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: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; 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:SF175; ATP-DEPENDENT CLP PROTEASE, ATP-BINDING SUBUNIT CLPC; 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   Hydrolase {ECO:0000313|EMBL:ACO46187.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ACO46187.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   747 AA;  82334 MW;  F9C1372849B3AB1E CRC64;
     MTNRYDDRAR LVFHYAREEG NRLGHAMVGP EHMLLGLMRE GGTAATILGE FGASLDGLRR
     RVEDIIGRGE GSRLNDAPSI TPRARRVMEL ASSEARSLGA QVTSTEHILL GIIREGDGVA
     FRILQELTKD VDTIRWRVLA QGEGSSAKPA KPVATPFLDE YGRDLTRWAR EGKLDPVIGR
     SEEIRRVTQI LTRRTKNNPV LIGDPGVGKT AIVEGLALAI HEKRTPPNLH GVRLVSLDLS
     GVVAGTKYRG EFEERLRQII EELRNAKVVA FIDELHTLVG AGGAEGTLDA ANILKPALSR
     GEIQVIGATT TGEYHRYIEK DAALERRFQP VIVLEPSPAE TLQILRGLRP KYEEHHGVQI
     PDTALELSVR IGERSLPGRN FPDKAIDLID EAASRVRLNM SVGLPVAENE QGEPYVTRED
     IESVINSMGG IYSEETAAQL SDLDLQLSEQ VYGQPDAVKA LSSALRRARV GLGGRTRVAA
     SFLFVGPSGV GKTHLAKALA RTLFSSERAL IRVDMSEFQE SHSISKLIGS PPGYVGFEQG
     GRLTEAVRRQ PFSVILLDEI EKAHPDVYNT FLQVLDDGRL TDGLGRTVDF RRTIIIMTSN
     TGFNVNPTVG FSPVTPDNNA PLRHIFTPEF LDRLDDVIRF RSLGEEELVR VAQQLLGEMR
     EELISREMRV TFDPAIAAWL VGKLKARSPK HAVGSSRQLR TLVREELEDP LAMELMAIDG
     QELRVVLGET GIQFEKGEEA APRQILA
//
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