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Database: UniProt
Entry: A0A1H8LH84_9ACTN
LinkDB: A0A1H8LH84_9ACTN
Original site: A0A1H8LH84_9ACTN 
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
//
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