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Database: UniProt
Entry: A0A3N4S5Y1_9ACTN
LinkDB: A0A3N4S5Y1_9ACTN
Original site: A0A3N4S5Y1_9ACTN 
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}.
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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
//
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