ID A0A1H8LH84_9ACTN Unreviewed; 921 AA.
AC A0A1H8LH84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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:SEO04521.1};
GN ORFNames=SAMN05216267_10164 {ECO:0000313|EMBL:SEO04521.1};
OS Actinacidiphila rubida.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310780 {ECO:0000313|EMBL:SEO04521.1, ECO:0000313|Proteomes:UP000181951};
RN [1] {ECO:0000313|EMBL:SEO04521.1, ECO:0000313|Proteomes:UP000181951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEO04521.1,
RC ECO:0000313|Proteomes:UP000181951};
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; FODD01000016; SEO04521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8LH84; -.
DR STRING; 310780.SAMN05216267_10164; -.
DR Proteomes; UP000181951; 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:SEO04521.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEO04521.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000181951};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 60..207
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 477..512
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 473..512
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 894..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 99545 MW; 9C1BC0FB68665563 CRC64;
MPVNRREPAA DPGSGQGSGA DEGTDRTMTN GFTGPEDDPF GDFFARFFGG QRPGPRQVDI
GRLLSQPARD LVQGAAQYAS DHGSRDLDTE HLLRAALALE PTRSLLSRAG ADPDSLASQI
DARSGPLRPV PGDGQGPPAA LSLTPAVKRA LLDAHEVARA GGAGYIGPEH VLTALAANPD
SAAGHILNAA RFEASRLPAE SGDAAAPPGA ERERPSTTPT LDGYGRDLTD LAAKGRIDPV
IGRDQEIEQT IEVLSRRGKN NPVLIGDAGV GKTAVVEGLA QHIADGDVPD VLIGRRVVAL
DLSSVVAGTR YRGDFEERLN TIVGEIRAHS DELIIFIDEL HTVVGAGGGG EGGSMDAGNI
LKPPLARGEL HIVGATTLEE YRRIEKDAAL ARRFQPILVP EPTVADTLEI LRGLRDRYEA
HHQVRYTDEA LTAAVELSDR YLTDRRLPDK AIDLIDQAGA RVKLRSRTRG TDVRALEREA
ERLTRDKDQA VADEQYEEAT RLRDRIADVK QRMAEVGGDD QADEGQHLEV TAEAIAEVVS
RQTGIPVSSL TQEEKERLLG LEQRLHERVI GQEEAVTVVS DAVLRSRAGL ASPARPIGSF
LFLGPTGVGK TELARALAEA LFGSEDRMVR LDMSEYQERH TVSRLVGAPP GYVGHEEAGQ
LTEVVRRHPY SLLLLDEVEK AHPDVFNILL QVLDDGRLTD SQGRTVDFTN TVIVMTSNLG
SEAITRRGAG IGFGGGGADA DEEARREQIL RPLREHFRPE FLNRIDEIVV FRQLTAEQLR
EITDLLLEST RRLMHAQGVT AEFTAEAVDW LAQRGYQPEY GARPLRRTIQ REVDNQLSRQ
LLDGRIREGS TVTVDVADDA LRFRTHDESG EAGGAGRTRE GGTETAGEAT GGASGEEARD
ESRDGNRDEQ PSSPAAAPDD T
//