ID A0A3N4S5Y1_9ACTN Unreviewed; 847 AA.
AC A0A3N4S5Y1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RPE38841.1};
GN ORFNames=EDD90_1774 {ECO:0000313|EMBL:RPE38841.1};
OS Streptomyces sp. Ag109_O5-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938851 {ECO:0000313|EMBL:RPE38841.1, ECO:0000313|Proteomes:UP000271204};
RN [1] {ECO:0000313|EMBL:RPE38841.1, ECO:0000313|Proteomes:UP000271204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-1 {ECO:0000313|EMBL:RPE38841.1,
RC ECO:0000313|Proteomes:UP000271204};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPE38841.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RKQF01000001; RPE38841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4S5Y1; -.
DR Proteomes; UP000271204; 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:RPE38841.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RPE38841.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 38..184
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 454..489
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 80..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 92621 MW; 05E3EB4E5931B879 CRC64;
MTSGYPGPGD YGQDPFGDFL ARFFGGGGAR QGPRQIDIGR LLSQPARELV KGAAQYAAEH
GSRDLDTEHL LRAALSAEPT RSLLSRSGAD PDSLATEIDG RAGPVQHSPG EAPPPTSLSL
TPAVKRALLD AHELARASGT GYIGPEHVLG ALAANPDSAA GHILNAARFA AGLPQDTAET
DRSLPGTDHR RRTNTPTLDK YGRDLTEQAG QGRIDPVIGR DDEIEQTIEV LSRRGKNNPV
LIGDAGVGKT AIVEGLAQRI ADGDVPDVLS CRRVVALDLP AVVAGTRFRG DFEERLTNIV
NEIRAHSDQL IVFIDELHTV VGAGGGSEGG AMDAGNILKP ALARGELHIV GATTLEEFRK
IEKDAALARR FQPILVPEPT VPDAIEILRG LRDRYEAHHQ VRYTDEALVA AVELSDRYLT
DRRLPDKAID LIDQAGARVR LGSRTKGSDV RTMEREIEQL TRDKDQAVAD EQYERATQLR
DRIGELKTRT TELSGEDQAD EGMNLEVTAE AIAEVVSRQT GIPVSSLTQE EKERLLGLEA
HLHQRVIGQD EAVSVVSEAV MRSRAGLASP HRPIGSFLFL GPTGVGKTEL ARALAEVLFG
SEDRMVRLDM SEYQERHTVS RLVGAPPGYV GHEEAGQLTE VVRRHPYSLL LLDEVEKAHP
DVFNILLQVL DDGRLTDSQG RTVDFTNTVI VMTSNLGSDV ITRRGIGVGF GPSGEEATEE
ARREQVLRPL RDHFRPEFLN RIDEIVVFRQ LTGDQLHQIT ELLLEHTRRM LHAQGITAHF
TDKAVNWLAE HGYQPEYGAR PLRRTIQREV DNQLSRLLLD GTITEGSEVT VEESHGHLEF
RPAKAPR
//