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Database: UniProt
Entry: F3NM51_9ACTN
LinkDB: F3NM51_9ACTN
Original site: F3NM51_9ACTN 
ID   F3NM51_9ACTN            Unreviewed;       841 AA.
AC   F3NM51;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Clp-family ATP-binding protease {ECO:0000313|EMBL:EGG45601.1};
GN   ORFNames=SGM_4306 {ECO:0000313|EMBL:EGG45601.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG45601.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG45601.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG45601.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
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:EGG45601.1}.
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DR   EMBL; AEYX01000040; EGG45601.1; -; Genomic_DNA.
DR   RefSeq; WP_006142108.1; NZ_AEYX01000040.1.
DR   AlphaFoldDB; F3NM51; -.
DR   STRING; 996637.SGM_4306; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000003022; 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; 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; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:EGG45601.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:EGG45601.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:EGG45601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          421..456
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          817..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  92985 MW;  6678998AEF3D87C3 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGISLEAVR
     QQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LNRVRQQVIQ LLSGYQGKET ATAGGPAEGT PSTSLVLDQF GRNLTQAARE
     SKLDPVIGRE KEIERVMQVL SRRTKNNPVL IGEPGVGKTA VVEGLAQAIV KGEVPETLKD
     KHLYTLDLGA LVAGSRYRGD FEERLKKVLK EIRTRGDIIL FIDELHTLVG AGAAEGAIDA
     ASILKPMLAR GELQTIGATT LDEYRKHLEK DAALERRFQP IQVAEPSLPH TIEILKGLRD
     RYEAHHRVSI TDEALVQAAT LADRYISDRF LPDKAIDLID EAGSRMRIRR MTAPPDLREF
     DEKIAGVRRD KESAIDSQDF EKAASLRDKE KQLLAAKAKR EKEWKAGDMD VVAEVDGDLI
     AEVLATATGI PVFKLTEEES SRLLRMEDEL HKRVIGQKDA VKALSKAIRR TRAGLKDPKR
     PGGSFIFAGP SGVGKTELSK ALAEFLFGDE DALISLDMSE FSEKHTVSRL FGSPPGYVGY
     EEGGQLTEKV RRKPFSVVLF DEVEKAHPDI FNSLLQILED GRLTDSQGRV VDFKNTVIIM
     TTNLGTRDIS KGFNLGFAAQ GDTKSNYERM KNKVSDELKQ HFRPEFLNRV DDVVVFPQLT
     QQDILAIVDL MIEKVDERLK DRDMGLELSQ SAKELLSRKG YDPVLGARPL RRTIQREVED
     TLSEKILFGE LRPGHIVVVD TEGEGDTATF TFRGEEKAAL PDVPPIEQAA GGAGPNLSKE
     A
//
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