ID A0A3A9T6U6_9FIRM Unreviewed; 867 AA.
AC A0A3A9T6U6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RKM61214.1};
GN ORFNames=D6855_04795 {ECO:0000313|EMBL:RKM61214.1};
OS Butyrivibrio sp. CB08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=2364879 {ECO:0000313|EMBL:RKM61214.1, ECO:0000313|Proteomes:UP000281491};
RN [1] {ECO:0000313|Proteomes:UP000281491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB08 {ECO:0000313|Proteomes:UP000281491};
RA Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RKM61214.1}.
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DR EMBL; RAIR01000002; RKM61214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9T6U6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000281491; 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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:RKM61214.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:RKM61214.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:RKM61214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281491};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 831..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..470
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 852..867
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 95503 MW; B5B185261365718E CRC64;
MDSKFTVMAN EALKLAKKTA RTLKLNYVGT EHILMGLILE DGCVASRILI DNGIDENRMM
EMIRDLIVPD SNVRTLDRDG FSPRAEKVLE EAHKMAERFH ADKTGTEHIL LALIKEGENV
AVRLISTMNV PAQKIYAETL AAMGEDPNLV KEDLGKKSAT SAKTGKKPSI LAQYSRDMTA
LAIEGKLDPV IGREREIKRV IQILSRRTKN NPCLIGEPGV GKTAVVEGLA QRIASGDVPL
TVQNKRLMTL DLSGMIAGSK YRGEFEERIK KVIKEVADDG NIILFVDEMH TLIGAGGAEG
AIDASNILKP SLARGEIQMI GATTISEYRK YVEKDAALER RFQPVNVDEP TKEEATDILN
GIVSKYEEHH KVTVTPEAIK AAVDLSERYI NDRNLPDKAI DLIDEAASAV RLRTMGVSPK
VKEMEKQVAE LDKQIEDALK NSDFTAAGRL NKEQNTLMTK LARVKNAEAR KQKSSGFIVD
ENDIAEVVAE WTRIPVKKIA EKESEKLLKL ESVLHKRVIG QEDAVKAVSK AIRRGRVGLQ
DPNRPIGSFL FLGPTGVGKT ELSKALAEAM FGDENALIRV DMSEYMEGHS VSKMIGSPPG
YVGYDEGGQL SEKVRRHPYS VILFDEIEKA HPDIFNVLLQ VLDDGHITDA KGRKVSFKNT
ILIMTSNVGA QRIVDPKKLG FGAGADAKRD YEDMKSGVMD EVKKLFKPEF INRIDEIMVF
HTLTEKEMMD IVTLLSQNLS KRCKAQMDIN LTISPAVKKH LVSKHSDAKM GARPLKRAIQ
QTIEDAMAEE LLKGNIKAGM DVTVTLKDDK IVFVGKDGKA ASVKKVQVKT TKPGKATKVA
KAVTTKKPRG SAAKKPAAKK PAAKKKK
//