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Database: UniProt
Entry: A0A1G9V2F9_9FIRM
LinkDB: A0A1G9V2F9_9FIRM
Original site: A0A1G9V2F9_9FIRM 
ID   A0A1G9V2F9_9FIRM        Unreviewed;       826 AA.
AC   A0A1G9V2F9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SDM66283.1};
GN   ORFNames=SAMN04488502_106146 {ECO:0000313|EMBL:SDM66283.1};
OS   Dendrosporobacter quercicolus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Dendrosporobacter.
OX   NCBI_TaxID=146817 {ECO:0000313|EMBL:SDM66283.1, ECO:0000313|Proteomes:UP000214880};
RN   [1] {ECO:0000313|EMBL:SDM66283.1, ECO:0000313|Proteomes:UP000214880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1736 {ECO:0000313|EMBL:SDM66283.1,
RC   ECO:0000313|Proteomes:UP000214880};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FNHB01000006; SDM66283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9V2F9; -.
DR   STRING; 146817.SAMN04488502_106146; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000214880; 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 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; 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|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:SDM66283.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDM66283.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214880};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..143
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          423..458
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          419..465
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   826 AA;  90231 MW;  348CDD29C0531226 CRC64;
     MYNRFTGRAI KVLELAQQEA GRLGHGYVGT EHLLLGLVHE GEGVAAKALA SIHINLAAVR
     AQTEALIGRG DSASTEIGYT PRAKQVMELA VEEAKLLGHN YIGTEHILLG LIREGEGVAG
     RVLASLGADL NVVRQVVIKM LGGADHAGAA PQANNGARPE NANGNTPNLN EFGRDLNSLA
     KEGKIDPVVG RDNEIDRVIQ ILSRRTKNNP VLIGEPGVGK TAIAEGLAQR IVQGAVPEVL
     RGKRVVSLNM ASLVAGSKYR GEFEERLKKV MEEIRTAGNV ILFIDEMHTL IGAGAAEGAI
     DAANILKPAL ARGELQAIGA TTLNEYKKYI EKDAALERRF QPIVVGEPSV EDAITILQGI
     RDKYEAFHRA QITDEAIDAA VKLSHRYISD RFLPDKAIDL MDEAASRVRL QSFSAPPDIQ
     DSEKKLEKLR AEKEAAITAQ EYERAAQLRD EEGRLKAELE SKQKQWRERQ SGRSVVTAED
     IAHVVAAWTG IPVARMAEGE AERLLKLEAV LHNRLIGQED AVKSVARAVR RARAGLKDPK
     RPIGSFIFLG PTGVGKTELA RALAEALFGD ESAMIRLDMS EYMEKHTVSR LVGAPPGYVG
     FDEGGQLTDA IRRKPYAVIL LDEIEKAHYD VFNILLQVLE DGRLTDSQGR TVDFKNTVII
     MTSNVGAKHL KQDSGTMGFL TDSRAASDQN AKTRVLDEVK RTFRPEFLNR VDELIVFSSL
     TDHELIKIVD IMLGSVAERL ADNGIGLTIT DKAKGELLKE GRDYAYGARP LRRAIQRLIE
     DEIADMLLRQ EAVAGVTVVV DADSDGKLVF SRRDSQPESP AVQEIK
//
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