ID A0A1H1D9K1_9ACTN Unreviewed; 864 AA.
AC A0A1H1D9K1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SDQ73114.1};
GN ORFNames=SAMN04489764_1890 {ECO:0000313|EMBL:SDQ73114.1};
OS Thermostaphylospora chromogena.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermostaphylospora.
OX NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ73114.1, ECO:0000313|Proteomes:UP000217103};
RN [1] {ECO:0000313|EMBL:SDQ73114.1, ECO:0000313|Proteomes:UP000217103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ73114.1,
RC ECO:0000313|Proteomes:UP000217103};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FNKK01000002; SDQ73114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1D9K1; -.
DR STRING; 35622.SAMN04489764_1890; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000217103; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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.
DR PROSITE; PS50151; UVR; 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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SDQ73114.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDQ73114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217103};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 41..181
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 449..484
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 825..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 842..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 96126 MW; 69B55035846F8E7C CRC64;
MTSGDYWPSG FGPLDELLAR FFGGYGPPEP GGRGFIRRVD IGRLLSEDAI ELLRTAVQKA
AEWGAEYLDS EHLLWAATRF ESIRTLLEQA GADPDGIART IESSVERKPA RQGPMPLSPA
VKRALLDARQ IARATGDSYI GPHHIVLALS ANPDSAAGRL LHGSHITPQS FHVEAAGAAE
PMAARMTPSS TPTLDQYGRD LTELAREGRI DPVIGRDVEI EQTIEVLSRR TKNNPVLLGE
PGVGKTAVIE GLAQRIVDGE VPDTLRNKRV VQIDLAGMVA GTKFRGEFEE RLKKVMEEIR
DHGEELVVFI DELHTVVGAG GAEGAIDASN MLKPALARGE LHVVGATTLD EYRRFVEKDA
ALERRFQPII VPEPSVADTI EILRGLRDRY EAHHQVRFSD EALIAAAELS DRYVTGRFLP
DKAIDLMDQA GARIALRTKT TPTDTRELEQ RLEQRKREKD QAVAREDYDR AKELRDEIAE
LRRAIDEARE GNRGIPEVTA ADIAEIVSRT TGIPVAQLTQ EEKERLLALE EHLHQRVVGQ
DEAVTAVAEA VRRSRAGLSD PNRPIGSFLF LGPTGVGKTE LARALAEALF GDQDRMIRFD
MSEFQERHTV SRLVGAPPGY VGYEEAGQLT EAVRRRPYSV ILLDEIEKAH PDVFNLLLQV
LDDGRLTDGQ GRTVDFKNTV LIMTSNIGAD IIMAHQGEAA NSLRPQLIRL LQHAFRPEFL
NRIDETIIFR SLDMNQLRQI TLLLLEESRR RLHAQDVILD VADSAVDWLV RQGYQPHFGA
RPLRRTIQRK LDNTLSRMLL DGTLKPQQRV YVSTQGDDLA FTVLDREAKG PEPGTEPHAT
APPEHRPAEG EERRRQPDAY GQYL
//