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Database: UniProt
Entry: A0A238XVL4_9ACTN
LinkDB: A0A238XVL4_9ACTN
Original site: A0A238XVL4_9ACTN 
ID   A0A238XVL4_9ACTN        Unreviewed;       869 AA.
AC   A0A238XVL4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-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:SNR62730.1};
GN   ORFNames=SAMN06264365_10438 {ECO:0000313|EMBL:SNR62730.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR62730.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNR62730.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR62730.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNR01000004; SNR62730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238XVL4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198415; 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:SNR62730.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNR62730.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..200
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          476..511
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          186..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  94685 MW;  ED400C563A91E2A8 CRC64;
     MSIGPLGPGG PGQWDDLFAR FFGAAEPRRA AQRIDIARYM SNDARRVLAD AARRAADSGP
     GDGGPADLDT DHLLWAVLQQ EPMKQTVRRA GADPQILLSE LELRVGDESA RIASANRRAE
     MGAVGLDQPE QVSLTPAAKR ALLDSLQISR AMGASYIGPE HILMALGLNT DSVAGRLLAG
     RLDTRAIPNS ETPTGPVAGG QGGSRVTGRA APATPTPTLE QFGVDLTEMA RRGEIDPVIG
     RADEIEQAVE ILSRRTKNNP VLIGEAGVGK TAIVEGLAQR IVDGDVPLTL QDKRVVQLDL
     AGLVAGTRYR GDFEERLRKI IDEIQASGDG LVVFLDEIHT LVGAGGGGEG GGMDAGNMLK
     PALARGRLRV IGATTLDEYR KHIEKDAALA RRFQPVQVGE PSVEDAVAIL RGLRDNYEAH
     HQVRITDEAL DAAALLSDRY IADRFLPDKA IDLIDQAGAR VRLRTKMPDA DLRERERQLE
     QLSRDRDQAV AAENYEVASQ LRDRINELKA RITGAGAGAD GVPRVTADDI AEMVARATGI
     PVAQLTETER DRLLGLEEHL HEHVVGQDDA VTAVAEAVRR SRAGLGDPGR PVGSFLFLGP
     TGVGKTELAR SLAEALFGDA DRMVRLDMSE FQERHAVSRL VGAPPGYVGY DEAGQLTEAV
     RRRPYSVVLL DELEKAHHDV FNILLQVLDD GRLTDSQGRT VSFKNTVLIM TSNLGSDLIN
     GSSRSVGFGG AENGRSPEDD LRDRLDRRLK EQLRPEFINR IDEIIIFRQL ETEQLRKITE
     MLLESTRRRL DAQDVRMEIT TAAVDWLADK GYQPEFGARP LRRTIQRELD NRLSKMLLAA
     DLAPGRIVRV DVRDGELTFE IESASLSTR
//
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