ID A0A2V1IKA1_9BACT Unreviewed; 870 AA.
AC A0A2V1IKA1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:PWB00390.1};
GN ORFNames=C5O23_12985 {ECO:0000313|EMBL:PWB00390.1};
OS Duncaniella muris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Duncaniella.
OX NCBI_TaxID=2094150 {ECO:0000313|EMBL:PWB00390.1, ECO:0000313|Proteomes:UP000244905};
RN [1] {ECO:0000313|Proteomes:UP000244905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103720 {ECO:0000313|Proteomes:UP000244905};
RA Clavel T., Strowig T.;
RL Submitted (FEB-2018) 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:PWB00390.1}.
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DR EMBL; PUEC01000044; PWB00390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1IKA1; -.
DR Proteomes; UP000244905; 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:PWB00390.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PWB00390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244905};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..159
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 463..498
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 166..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 459..523
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 178..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 96527 MW; BD514B88F43820B6 CRC64;
MDTVYSQNFK EIISDSPRQA ARHNTRYVMP EHLLLSLLSD IEGEPARLID RAAKGASAYE
LRENLDKALF NAATDADYQG TVGISDVSLS DLTGRIIKLS ALEARMLKSN EVDATHLLLA
IFHNSDAQNS EFMTAFHRAG ITYEAIYRLL ATDSDLATPL NADFAEEDED DEMPPRSSAP
QGGQQSSSAS GKRQGAPTAQ RRGNDTPVLD KYGNDMTLAA EENRLDPVVG RDVEIERLAQ
ILSRRKKNNP VLIGEPGVGK SAIVEGLALR IVQRKVSRIL FGKRVVSLDM ASIVAGTKYR
GQFEERIKAI LDELSKNKDI ILFIDELHTI VGAGNAAGSM DAANLLKPAL ARGEIQCIGA
TTLDEYRKNI ENDGALERRF QKVMVEPTTA EETRIILDNI KDKYEEHHNV NYTPEALDAC
VQLTERYVSD RNFPDKAIDA MDEAGSRVHV TNIAVPKEIE QLEQRIEEVA AQKLRAAQSQ
NFEKAASYRD QEQQLKATLE ESKARWEEQL NAMRETVDAE KVAEVVAMMT GVPVQRIAQA
EGKRLKEMAP TLKGSIIGQD PAIEKVVKAI QRNRIGLKDP NKPIGTFLFL GPTGVGKTHL
AKKLAEYMFD SADTLIRIDM SEYMEKFTVS RLVGAPPGYV GYEEGGQLTE KVRRHPYSIV
LLDEIEKAHP DVFNLLLQVM DEGRLTDSLG RRIDFKNTII IMTSNIGSRQ LKDFGSGIGF
ASPSSNDKDY SQSVLRKALN KAFAPEFLNR IDDVIMFDSL SKEAIFKIID IELAGFNKRV
KELGYTLTIT DEAKNFIAEK GYDANYGARP LKRSIQKYLE DKLAELIIDA SISAGDEIFV
SYHPGAEELD TEIRRPSAPA RADSLTDGQA
//