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Database: UniProt
Entry: A0A2C1K6M5_9BACI
LinkDB: A0A2C1K6M5_9BACI
Original site: A0A2C1K6M5_9BACI 
ID   A0A2C1K6M5_9BACI        Unreviewed;       815 AA.
AC   A0A2C1K6M5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PGT81288.1};
GN   ORFNames=COD11_18415 {ECO:0000313|EMBL:PGT81288.1};
OS   Bacillus sp. AFS040349.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT81288.1, ECO:0000313|Proteomes:UP000222674};
RN   [1] {ECO:0000313|EMBL:PGT81288.1, ECO:0000313|Proteomes:UP000222674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS040349 {ECO:0000313|EMBL:PGT81288.1,
RC   ECO:0000313|Proteomes:UP000222674};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:PGT81288.1}.
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DR   EMBL; NUMC01000084; PGT81288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1K6M5; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000222674; 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:PGT81288.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PGT81288.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222674};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          418..453
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   COILED          414..464
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   815 AA;  90747 MW;  232F4CF8CF4B5AE2 CRC64;
     MMFGRFTERA QKVLALAQEE AVRLGHNNIG TEHILLGLVS EGEGIAAKAL LALGLGPDKI
     QKEVEGLIGR GQDASQTIHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
     ARVLNNLGVS LNKARQQVLQ LLGSNESSAN HQGGGITNAN TPTLDSLARD LTAIAREGSL
     DPVIGRSKEI QRVIEVLSRR TKNNPVLIGE PGVGKTAIAE GLAQQIVQNE VPEILRDKRV
     MTLDMGTVVA GTKYRGEFED RLKKVMDEIR QAGNIILFID ELHTLIGAGG AEGAIDASNI
     LKPSLARGEL QCIGATTLDE YRKYIEKDAA LERRFQPIQV DEPSVDESVQ ILKGLRDRYE
     AHHRVSITDE AIDAAVKLSD RYISDRFLPD KAIDLIDEAG SKVRLRSFTT PPNLKELELK
     LEEIRKEKDA SVQSQEFEKA ASLRDTEQRL REQLEETKKT WKEKQGQENT EVTVEDIAMV
     VSSWTGVPVS KLAQTETDKL LNMESLLHSR VVGQEEAVVA VAKAVRRARA GLKDPKRPIG
     SFIFLGPTGV GKTELARALA ESIFGDEDAM IRIDMSEYME KHSTSRLVGS PPGYVGYDEG
     GQLTEKVRRK PYSVVLLDEI EKAHPDVFNI LLQVLEDGRL TDSKGRTVDF RNTILIMTSN
     VGASELKRNK YVGFNIQDET QNYKDMKDKV MNELKRAFRP EFINRIDEII VFHSLEKKHL
     KEIVSLMSDQ LTKRLKEQDL SLELTESAKE KIADEGIDLE YGARPLRRSI QKNVEDRLSE
     ELLKGTIDKG QKIILDVENG EFVVKTAEKE EVKSN
//
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