ID A0A1Q5JHN2_9ACTN Unreviewed; 837 AA.
AC A0A1Q5JHN2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Clp protease {ECO:0000313|EMBL:OKJ68803.1};
GN ORFNames=AMK31_37595 {ECO:0000313|EMBL:OKJ68803.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ68803.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ68803.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ68803.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OKJ68803.1}.
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; LIVZ01000025; OKJ68803.1; -; Genomic_DNA.
DR RefSeq; WP_073945393.1; NZ_LIVZ01000025.1.
DR AlphaFoldDB; A0A1Q5JHN2; -.
DR STRING; 1703942.AMK31_37595; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000185813; Unassembled WGS sequence.
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 78, MITOCHONDRIAL; 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:OKJ68803.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OKJ68803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 39..179
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 443..478
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 156..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 176..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 90333 MW; 5FD53A5AC21EC495 CRC64;
MTVVTTSPFG SGDPFSDLFN RFFGMSPAAS PPAVQRVPIG RLLSDSSHEL LTAAGSRAAE
DGSDLDTVHL LWAATQVSAS RQLLEQAGAD PDRLAADLQE SLPSGAGTGE PGLTPAAKRA
LLAAHARSQA TGSSYIGPEH ILAALLEDPR SGLVRTLGPE GVSSGLLSGG EGGRKAASGE
HSDTPTLDEY GRDLTEEARS GRLDPVVGRA EEIEQTVEVL SRRTKNNPVL IGEPGVGKTA
IVEGLAQRIV AGEVPKALRN RRVVSLDMAG LVAGSKYRGE FEERLKKVID EVTEAESGII
VFIDELHTVV GAGGGGEGAM DAGNILKPAL ARGDLSVVGA TTIDEYRRYI EKDAALERRF
QPVMVREPTV EETVQILSGL RDSYEAHHQV RYTDEALEAA AALSDRYITD RFLPDKAIDL
MDQAGARVGL RSLGAPVGTA SLEDRLTKLR REKDEAVSTE DYARAAQLKE QIRQVEQELA
VAGGEREEAG SVTAEDIADV LSARTGIPVS QLTETERERL TKLEESLHER VVGQDEAVAA
VSQAVRRGRA GMGDPDRPTG SFLFLGPTGV GKTELAKALA ELLFGDSDRM VRFDMSEFQE
KHTVSRLVGS PPGYVGYEEA GQLTEAVRRK PYSVVLFDEV EKAHPDVFNL LLQVLDDGRL
TDAQGRTIDF RHTVVIMTSN IASKRILDHQ GAVEDIRDDL MAELQAHFRP EFLNRIDEII
VFHALTRADL VRIVDLLLER SRRRLHAQQI DLEVTETAKE WLANRGYQPE FGARPLRRTI
QTELDNRLSN MLLGGSVNPG DTVIVDVKDG ELALTLGPAA ASGGADQPEP DTASSPE
//
