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Database: UniProt
Entry: A0A4R4PBK7_9ACTN
LinkDB: A0A4R4PBK7_9ACTN
Original site: A0A4R4PBK7_9ACTN 
ID   A0A4R4PBK7_9ACTN        Unreviewed;       844 AA.
AC   A0A4R4PBK7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JUN-2023, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:TDC18460.1};
GN   ORFNames=E1284_06180 {ECO:0000313|EMBL:TDC18460.1};
OS   Actinomadura bangladeshensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=453573 {ECO:0000313|EMBL:TDC18460.1, ECO:0000313|Proteomes:UP000295431};
RN   [1] {ECO:0000313|EMBL:TDC18460.1, ECO:0000313|Proteomes:UP000295431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45347 {ECO:0000313|EMBL:TDC18460.1,
RC   ECO:0000313|Proteomes:UP000295431};
RA   Sahin N., Ay H., Saygin H.;
RT   "Draft genome sequences of novel Actinobacteria.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TDC18460.1}.
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DR   EMBL; SMJW01000019; TDC18460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R4PBK7; -.
DR   OrthoDB; 3170949at2; -.
DR   Proteomes; UP000295431; 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:TDC18460.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:TDC18460.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:TDC18460.1};
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          805..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  93889 MW;  03D22277769BAD76 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGISLEAVR
     QQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LNRVRQQVIQ LLHGYQGKEP AASGGPSESA PSTSLVLDQF GRNLTQAARE
     GKLDPVIGRD KEIERVMQVL SRRTKNNPVL VGEPGVGKTA VVEGLAQKIV KGEVPETLKD
     KQLYTLDLGA LVAGSRYRGD FEERLKKVLK EIRTRGDIIL FIDELHTLVG AGAAEGAIDA
     ASILKPMLAR GELQTIGATT LDEYRKHLEK DAALERRFQP IQVAEPSLSH TIEILKGLRD
     RYEAHHRVSI TDSALVAAAQ LADRYISDRF LPDKAIDLID EAGSRMRIRR MTAPPDLREY
     DEKIADVRRD KESAIDAQDF EKAAALRDSE KQLLGQKAQR EKEWKAGDMD VVAEVTDELI
     AEVLATATGI PVFKLTEEES TRLLRMEDEL HKRVIGQHDA IKALSQSIRR TRAGLKDPKR
     PGGSFIFAGP SGVGKTELSK TLAEFLFGDE DALIQLDMSE FMEKHTVSRL FGSPPGYVGY
     EEGGQLTEKV RRKPFSVVLF DEIEKAHQDI FNSLLQILED GRLTDAQGRV VDFKNTVIIM
     TTNLGSKDIS KGVSMGFARQ NDEQGSYERM KAKVSEELKQ HFRPEFLNRV DDTVVFHQLT
     PKEIIQIVDL MIAKVDDRLH DRDMGIELRQ EAKDLLAIRG YDPVLGARPL RRTIQREIED
     NLSEKILYNE LKPGQIVIVG TEGFDPENKD SAENAKFTFK GVPKPTGVPD SPPPIEGAVN
     FNKD
//
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