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Database: UniProt
Entry: A0A1I6U9I7_9PSEU
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Original site: A0A1I6U9I7_9PSEU 
ID   A0A1I6U9I7_9PSEU        Unreviewed;       828 AA.
AC   A0A1I6U9I7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFS97937.1};
GN   ORFNames=SAMN05660874_04728 {ECO:0000313|EMBL:SFS97937.1};
OS   Saccharopolyspora flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS97937.1, ECO:0000313|Proteomes:UP000198852};
RN   [1] {ECO:0000313|EMBL:SFS97937.1, ECO:0000313|Proteomes:UP000198852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS97937.1,
RC   ECO:0000313|Proteomes:UP000198852};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FOZX01000009; SFS97937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6U9I7; -.
DR   STRING; 95161.SAMN05660874_04728; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198852; 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};
KW   Hydrolase {ECO:0000313|EMBL:SFS97937.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFS97937.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          35..176
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          444..479
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          153..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  89522 MW;  2C3E8EC447336538 CRC64;
     MATFFGPVGG PFDEYFARFF GADDSTAGSR RVDITELMTE QAQQLVGEAA KFARDRGQGS
     LDALHLLWSA AKQDPTRAQL SQLGVDTEAF AKEVEGHLPA SGTPVEDESV SLTLAARTAL
     ADAHRVARAL GSTYIGPQHL LLALSANPET EAGRLLGGAG AGPEALRDAT QRPAPQQAPK
     SGPSGGETPT LDEYGRDLTA TAREGGLDPV IGRADEIEQT IEILSRRTKN NPVLVGEAGV
     GKTAIVEGLA QRIASGDVPE VLTGKRVVQL DLSAMLSGTR YRGDFEERMT KVIDEISEHS
     GELIVFIDEL HTVVGAGGAE GAMDAGNMLK PRLARGELHI VGATTLDEYR KNIEKDPALE
     RRFQPVQVPE PSVADTITIL RGLQEQYEKH HKVSYTEEAV EAAAKLSDQY INDRFLPDKA
     IDLIDQAGAR KRLNSGVADD GELRAKVERL EQLKNEAVAS EDYERASALR DEITAAQERL
     NEGGSGVLEI GPADIAEVVS RATGVPVSRL TAEEKVRLRN LESELHQRVV GQDDAVRALA
     RAVRRSRSGL GDPSRPVGSF LFLGPTGVGK TELAKALAES LFGDEQRMIR LDMSEFQERH
     TASRLVGAPP GYVGHGEAGE LTEAVRRSPY SVVLLDEIEK AHPDVFNTLL QVLDDGRLTD
     GQGRTVDFSN TVLIMTSNLA SEVVSSAGGK IGFTAGSPTQ DLEERVMPKL KDAFRPEFLN
     RINEIVVFKR LDGEQLHTIT RALLETTTKR LADMGVEVVF DDDAVAWVAD RGYQPEFGAR
     PLRRAIEREV DDRISDLLLD GELTEGTRLR VGARDGALDF QVEAPVAA
//
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