ID A0A4Y9IZH7_9BACT Unreviewed; 839 AA.
AC A0A4Y9IZH7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:TFU94103.1};
GN ORFNames=E4T81_05800 {ECO:0000313|EMBL:TFU94103.1};
OS Barnesiella sp. WM24.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=2558278 {ECO:0000313|EMBL:TFU94103.1, ECO:0000313|Proteomes:UP000298121};
RN [1] {ECO:0000313|EMBL:TFU94103.1, ECO:0000313|Proteomes:UP000298121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM24 {ECO:0000313|EMBL:TFU94103.1,
RC ECO:0000313|Proteomes:UP000298121};
RA Joseph S., Aduse-Opoku J., Curtis M., Wade W., Hashim A.;
RT "Diversity of the mouse oral microbiome.";
RL Submitted (MAR-2019) 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:TFU94103.1}.
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DR EMBL; SPPC01000004; TFU94103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9IZH7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000298121; 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:SF193; CHAPERONE PROTEIN CLPB; 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:TFU94103.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TFU94103.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000298121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 447..482
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 170..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..489
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 839 AA; 94066 MW; D39B765F40FED597 CRC64;
MDTNFSNELK TVLDQSRVEA SRHNDNVIRA EHLLLAILSN NDSNAFRTLR QLLDDDTMYR
LRDNLDNSIY RQREGTEGMG VSDLANRIIK LSVLEARMLK TNVVDSEHLL LALFHNNEVQ
SLDIMAQFHE AGVTYEALYK LLANVTDAPK MGASFGEDEE DEDDEIFRNE QKEPASSQQR
AGAPKRGNDT PVLDKFGNDM TRAAEEGRLD PVIGRGVEIE RLAQILSRRK KNNPVLIGEP
GVGKSAIVEG LALRIVQRKV SRILFGKRVI SLDMASIVAG TKYRGQFEER IKAILNELSK
NKDVILFIDE LHTIVGAGNA SGSMDAANLL KPALARGEIQ CIGATTIDEY RKNIEKDGAL
ERRFQKVMVE PTSPEETLTI LNNIKDKYED HHNVNYTPEA IEACVKLTDR YVSDRNFPDK
AIDALDEAGS RVHVTNIVVP KEIESIEAQI AEANANKLKA AQSQNFESAA SFRDKEQRLK
LELDDAKRKW EASLNEHRET VDEDKVAEVV AMMTGVPVQR IAQAEGMRLR EMAPELKHAI
IGQDGAIDKI VKAIQRNRVG LKDPNKPIGT FMFLGPTGVG KTHLAKKLAE YLFDSADTLI
RVDMSEYMEK FTVSRLVGAP PGYVGYEEGG QLTEKVRTHP YSVVLLDEIE KAHPDVFNLL
LQVLDEGRLT DSLGRKVDFK NTIIIMTSNI GSRQLKDFGT SVGFATKPAD KEYSHSVIQK
ALNKAFSPEF LNRVDDIVMF DALDKEAIFK IIDIELAGFY KRVDGLGYRL TITDEAKNFI
AERGYDAQFG ARPLKRAIQK YLEDELAEMI INASIQPGNL IFVDYDKEKD KIVTEIRTE
//
