ID A0A1R1CNK0_9BACL Unreviewed; 819 AA.
AC A0A1R1CNK0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:OMF23779.1};
GN ORFNames=BK133_24040 {ECO:0000313|EMBL:OMF23779.1};
OS Paenibacillus sp. FSL H8-0548.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF23779.1, ECO:0000313|Proteomes:UP000187405};
RN [1] {ECO:0000313|EMBL:OMF23779.1, ECO:0000313|Proteomes:UP000187405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF23779.1,
RC ECO:0000313|Proteomes:UP000187405};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF23779.1}.
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DR EMBL; MRTK01000044; OMF23779.1; -; Genomic_DNA.
DR RefSeq; WP_076338932.1; NZ_MRTK01000044.1.
DR AlphaFoldDB; A0A1R1CNK0; -.
DR STRING; 1920422.BK133_24040; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000187405; 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:OMF23779.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OMF23779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187405};
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 417..452
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 797..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..459
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 819 AA; 91194 MW; FDFFDE8137F2C332 CRC64;
MMFGRFTERA QKVLALAQEE AVRLGHNNIG TEHILLGLIR EGEGIAAKAL IGLGLGLEKI
QDEVEALIGR GQEQPNNIAY TPRAKKVIEL SMDEARKLGH TYVGTEHILL GLIREGEGVA
ARVLNNLGIS LNKARQQVLQ LLGSSEAVSS NHGSPANVST PTLDGLARDL TAYAKEGNLD
PVIGRSKEIE RVIQVLSRRT KNNPVLIGEP GVGKTAIAEG LAQKIIENEI PETLRDKRVM
TLDMGSVVAG TKYRGEFEDR LKKIMDEIRQ AGNIILFIDE LHTLIGAGGA EGAIDASNIL
KPALARGELQ CIGATTLDEY RKYIEKDAAL ERRFQPITVD QPSPEEAIQI LYGLRDRYEA
HHRVKITDEA IVQAVKLSDR YIPDRFLPDK AIDLIDEAGS KVRLHSYTVP PNLKQLENRL
EDIRKEKDAA VQSQEFEKAA ALRDTEQKIR EELDITKNQW KEKQGRTDSE VTPEDIAQVV
ASWTGIPVSK LAEGETERLL KMEEILHDRI IGQDEAVRSV SRAIRRARAG LKDPKRPIGS
FIFLGPTGVG KTELARALAE AMFGDENAVI RIDMSEYMEK HSTSRLVGAP PGYVGYEEGG
QLTEKVRRKP YSVVLLDEIE KAHPEVFNIL LQVLEDGRLT DSKGRVVDFR NTLIIMTSNI
GADQIKRNSS LGFTAVQDAG RDFQQMKDKV LAELKKSFRP EFLNRIDESI VFHSLGEEHI
AQIVTLMSEE LRKRLREQEV DFVLTDAAKA FLAKEGYDPQ YGARPLRRAI QKHIEDRLSE
DLLMGKIQKG DTFTIDEKDG GLTVTKSIPE QEPEETTAK
//