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Database: UniProt
Entry: A0A1H1D9K1_9ACTN
LinkDB: A0A1H1D9K1_9ACTN
Original site: A0A1H1D9K1_9ACTN 
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
//
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