ID A0A1H5PPE3_9ACTN Unreviewed; 823 AA.
AC A0A1H5PPE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SEF15773.1};
GN ORFNames=SAMN05216533_7513 {ECO:0000313|EMBL:SEF15773.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEF15773.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEF15773.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEF15773.1,
RC ECO:0000313|Proteomes:UP000198812};
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; FNTQ01000001; SEF15773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5PPE3; -.
DR STRING; 1855349.SAMN05216533_7513; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198812; 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:SEF15773.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEF15773.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198812};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 41..181
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 88..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 88..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90134 MW; DBD61EB6BBA02DF3 CRC64;
MSTSGFGFGR SPFEDFDELM SRFFGGAGAG AQPRRAQRVD IGSLLSERAR ELVAEARDIA
AVEGSDELDT RHLLAAATTH DSTRRLLTEA GADPDQLRER LTAGHGGGEK AEPATLTPAT
KRALLDAYQI SRAEGASYIG PEHLLRALAV NPESAAGRAL GESGWEPTRM PAEGAGERRK
PSTTPTIDEY GRDLTEDARA GRLDPVIGRD EEVEQTIEVL SRRSKNNPVL IGDPGVGKTA
IVEGIAQRIV TGDVPKTLEG KRLVSLDLAG MVAGTKYRGE FEERLKKLLD EVREHGDELV
LFLDELHTVV GAGGGGDGSL DAGNILKPAL ARGELHLIGA TTVDEYRKHI EKDAALERRF
APILVGEPTV DDTIEILRGL RDRYEAHHQV RITDEAVVAA AELSDRYITS RFLPDKAIDL
MDQAAARVRL RSKTSPTDTR DIEDRIAALN REKDQAVADE EYERAKELRD RIKAAEAELD
QAGTAEEHAP KVTAEDIAEV ASRTTGIPVA ELTEEERERL MKLEEHLHER VVGQDEAITA
VARAVRRARA GMSDPNRPVG SFLFLGPTGV GKTELARALA AALFGDETRM IRLDMSEFQE
RHTVSRLVGA PPGYVGHEEA GQLTEAVRRQ PYAVLLLDEV EKAHPDVFNT LLQLLDDGRL
TDAQGRTVDF KNTVVIMTSN IGADRILAAG TEDYAKVREA VMPALQQHFR PEFLNRIDEI
IVFRGLDRTQ LREIVDLLLE HTRRRLHAQD VTLEVTDSAA ELLANLGHQP DFGARPLRRT
IQREVDDRLA DLLLSGQLVA GERAVVDAAN GEIVIRSDKP ATV
//
