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Database: UniProt
Entry: A0A1I2AGX9_9BACI
LinkDB: A0A1I2AGX9_9BACI
Original site: A0A1I2AGX9_9BACI 
ID   A0A1I2AGX9_9BACI        Unreviewed;       809 AA.
AC   A0A1I2AGX9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFE42243.1};
GN   ORFNames=SAMN05216238_11579 {ECO:0000313|EMBL:SFE42243.1};
OS   Lentibacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=640948 {ECO:0000313|EMBL:SFE42243.1, ECO:0000313|Proteomes:UP000199474};
RN   [1] {ECO:0000313|EMBL:SFE42243.1, ECO:0000313|Proteomes:UP000199474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22530 {ECO:0000313|EMBL:SFE42243.1,
RC   ECO:0000313|Proteomes:UP000199474};
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; FOMR01000015; SFE42243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2AGX9; -.
DR   STRING; 640948.SAMN05216238_11579; -.
DR   Proteomes; UP000199474; 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:SFE42243.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFE42243.1};
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          419..454
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          144..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          415..472
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   809 AA;  90519 MW;  8BBD7D62B3DCB7AF CRC64;
     MFGRFTERAQ KVLALSQEEA VRLGHNNIGT EHVLLGLVRE GNGIAAKALE SLGLEVSKIQ
     QEVEKLIGTG KQPMQTIHYT PRAKKVVELS QDEARKLGHS YVGTEHILLG LIREGEGVAA
     RVLNNLGVSL NKARQQVLQL LGSNESQAGR QGRGAQSSNA NTPTLDSLAR DLTESAKDGN
     VDPVIGRGSE IERVIQVLSR RTKNNPVLIG EPGVGKTAVA EGLAQQIVNN EVPEILRDKR
     VMTLDMGTVV AGTKYRGEFE DRLKKVMEEI RQATNIILFI DELHTLIGAG GAEGAIDASN
     ILKPALARGD LQCIGATTLD EYRKYIEKDA ALERRFQPVQ VDEPTLEETI EILKGLRDRY
     EAHHRVTITD DAIEAAANLS NRYITDRFLP DKAIDLIDEA GSKVRLSSYT VPPNLKELEQ
     KLEDVRKEKD SAVQGQEFEK AASLRDSEQH LREELEETKN EWKQKQGQKD SEVTTEDIAK
     VVSIWTGVPV TSMTKDESER LLHLEDTLHN RVIGQDEAVN AVAKAIRRAR AGLKDPKRPI
     GSFIFLGPTG VGKTELARAL AEAMFADEEA MIRIDMSEYM EKHATSRLVG SPPGYVGYEE
     GGQLTEKVRT KPYSVVLLDE VEKAHPEVFN ILLQVLEDGR LTDSKGRLVD FRNTVLIMTS
     NVGANELKQN KYVGFTLDED KEQDYQDMKK KVTDELKKAF RPEFLNRVDE TIVFHSLERK
     HMKYIVNLML KQLQNRLKEQ EIEFSLTDKA VEKIANEGFD PEYGARPLRR SIQKNIEDLM
     SEELLQENFK KGEKVKIGLN NKGEFTILS
//
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