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Database: UniProt
Entry: B0S3X9_FINM2
LinkDB: B0S3X9_FINM2
Original site: B0S3X9_FINM2 
ID   B0S3X9_FINM2            Unreviewed;       806 AA.
AC   B0S3X9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=ATP-dependent protease Clp ATP-binding subunit ClpC {ECO:0000313|EMBL:BAG07753.1};
GN   OrderedLocusNames=FMG_0335 {ECO:0000313|EMBL:BAG07753.1};
OS   Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS   (Peptostreptococcus magnus).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG07753.1, ECO:0000313|Proteomes:UP000001319};
RN   [1] {ECO:0000313|EMBL:BAG07753.1, ECO:0000313|Proteomes:UP000001319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC   {ECO:0000313|Proteomes:UP000001319};
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT   pathogen.";
RL   DNA Res. 15:39-47(2008).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AP008971; BAG07753.1; -; Genomic_DNA.
DR   RefSeq; WP_012290340.1; NC_010376.1.
DR   AlphaFoldDB; B0S3X9; -.
DR   STRING; 334413.FMG_0335; -.
DR   KEGG; fma:FMG_0335; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   Proteomes; UP000001319; Chromosome.
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; 2.
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:SF193; CHAPERONE PROTEIN CLPB; 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|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:BAG07753.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAG07753.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001319};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          412..447
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          408..461
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   806 AA;  91319 MW;  AC5C557D694A62E5 CRC64;
     MRKSDIYNLR TEAVYEAISL KHADLGVEHV LLAMFKFDFK ASQYLKKHGG NYEKIRNLII
     DELGYGDSDE TNQRISPKLE EIITQAVQLS NTYGERTITP EHIMAALCLD SSNYANHLMK
     RTGVDIMKLT AELRKYFFMK MKRERGDVND NSANSSKPNE IEKYTKNLNE MAKEGKIDPC
     IGREEEIERI IQVLLRRKKN NPVLIGNPGV GKTAIVEGLA VKIVKGDVND IFKDKEILSL
     DLAALLAGTK YRGDFEERIK KVIDTLSNSE NKILFIDELH SLMGAGGAEG ALDASNILKP
     SLARGDLQII GATTINEYRK TIEKDQAFER RLQTIMVDEP SVSDSIQVIE GLKDKYESHH
     HVLISDEAIK ASVELSHRYL NDRYLPDKAI DLIDEAQSMV RVKNFTGGKN YAKILEELEE
     EKQEAIQNSD FLLAAEKRDA IKEVEAEMEE EDQDENKLEI GFDEIANIVS RWAKVPVSKL
     TESESQKYLF LADNLKKVVI GQDKAIDSIS NAIKRARVGL KNPNKPIGSF VFVGPTGVGK
     TYLAKKLAKE LFNDENAMIR IDMTEYMEKH SVSKLIGSPP GYVGHDDGGQ LTDMVRTKPY
     SVILFDEIEK AHPDVFNTLL QVLDDGRLTD SKGRVVNFKD TVIIMTSNIG ASELESKNVI
     GFNTAEDVEV DEYNRNKETI NNAMKSMFKP EFMNRLDDVI VFSNLNKENV KEIAGLMMDE
     LVDRMAKNDL IISYDEKILD YLVDKGYDKK FGARPLERLI RTDIENELAD KILNGDIDNN
     RKTTITVVND KVSFRRYVRR KKTVKQ
//
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