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Database: UniProt
Entry: A0A2T0SJQ7_9ACTN
LinkDB: A0A2T0SJQ7_9ACTN
Original site: A0A2T0SJQ7_9ACTN 
ID   A0A2T0SJQ7_9ACTN        Unreviewed;       841 AA.
AC   A0A2T0SJQ7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PRY33638.1};
GN   ORFNames=CLV70_101801 {ECO:0000313|EMBL:PRY33638.1};
OS   Pseudosporangium ferrugineum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Pseudosporangium.
OX   NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY33638.1, ECO:0000313|Proteomes:UP000239209};
RN   [1] {ECO:0000313|EMBL:PRY33638.1, ECO:0000313|Proteomes:UP000239209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY33638.1,
RC   ECO:0000313|Proteomes:UP000239209};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:PRY33638.1}.
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DR   EMBL; PVZG01000001; PRY33638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0SJQ7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000239209; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; 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:PRY33638.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PRY33638.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239209};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          449..484
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          168..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   841 AA;  91191 MW;  EFB9170EFAFB3CBF CRC64;
     MSIGPLGPTG PGDWDDLFAR FFGAEPRRSA QRIDITRFMS ADAREVLSDS ARRAAEVAPP
     GAAIADLDTD HLLWGALQQD AQKALVRRAG ADPDALLAEL GVPARTPGSP LPERVALTPA
     AKRALLDSLQ ISRAVGASYV GPEHILMALG LNPDSAGGRL LAGRVDPRTL QQGEPPTGGG
     QGGGGTDTPT LDEYGVDLTE LARRGEIDPV IGRADEIEQA VEVLSRRTKN NPVLIGEAGV
     GKTAVVEGLA QRIVDGDVPQ TLAGKRVIQL DLAGLVAGTR YRGDFEERLR KVIDEIQERG
     DGLIVFLDEI HTLVGAGGGG GEGGGMDAGN MLKPALARGR MRVVGATTLD EYRRHIEKDA
     ALARRFQPVL IGEPGIEDTV AILRGLRDNY EAHHQVRITD EALDAAAELS SRYITDRFLP
     DKAIDLIDQA GARVRLRVKT PAADVRERER LLEQLARDRD QAVAAENYEK ASRLRDEISE
     VRQRAAEAAG GGDGVPQVTP ADVAEVVSRA TGIPVAQLTE EERDRLLRLE AHLHDRVVGQ
     EDAVAAVAEA VRRSRAGLGD PDRPVGSFLF LGPTGVGKTE LARSLAGALF GDADRMIRLD
     MSEFQERHTV SRLVGAPPGY VGYDEAGQLT EAVRRRPYSV VLLDEIEKAH PDVFNILLQV
     LDDGRLTDSQ GRTVSFRNTV LIMTSNIGSE IISGTKRTVG FGTGGARSAD EELRDRLERR
     LREQFRPEFI NRIDEIIVFR QLETDQLRQI TSMMLDDTRR RLHAQDVTLE VTTAAVDRLA
     ELGFQAEYGA RPLRRTIQRE LDNRLSRMLL DAELAPGRTV RVDADGGRLT FTVESPAPAA
     A
//
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